|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5334 |
| Enzyme 1 Name |
Long-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 1 Synonyms |
- LCAD
|
| Enzyme 1 Gene Name |
ACADL |
| Enzyme 1 Protein Sequence |
>Long-chain specific acyl-CoA dehydrogenase, mitochondrial
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
|
| Enzyme 1 Number of Residues |
430 |
| Enzyme 1 Molecular Weight |
47655.3 |
| Enzyme 1 Theoretical pI |
7.89 |
| Enzyme 1 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 1 Specific Function |
Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
177962  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P28330  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ACADL_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1293 bp
ATGGCCGCACGCCTTCTCCGAGGGTCCCTACGCGTCCTGGGCGGCCACCGTGCGCCGCGC
CAGCTGCCCGCCGCGCGATGTTCTCATTCCGGAGGGGAAGAACGTCTAGAAACTCCTTCT
GCTAAAAAATTAACAGATATAGGAATTCGAAGAATCTTTTCTCCAGAGCATGACATTTTC
CGGAAAAGTGTAAGGAAGTTTTTCCAAGAAGAAGTGATTCCTCATCACTCAGAATGGGAG
AAAGCTGGAGAAGTAAGTAGGGAGGTTTGGGAAAAAGCTGGAAAACAAGGACTGCTTGGT
GTCAATATTGCAGAGCATCTTGGTGGAATTGGAGGGGATCTGTACTCCGCAGCTATTGTC
TGGGAGGAGCAAGCTTATTCAAATTGTTCAGGCCCAGGTTTTAGTATTCATTCAGGTATT
GTCATGTCCTATATTACAAACCATGGCTCAGAAGAACAGATTAAGCACTTTATTCCCCAG
ATGACTGCAGGCAAATGTATTGGTGCAATAGCAATGACAGAGCCTGGAGCTGGAAGTGAC
TTACAGGGAATAAAAACAAATGCTAAAAAGGATGGAAGTGACTGGATTCTCAATGGAAGC
AAGGTGTTCATCAGTAATGGGTCATTAAGTGATGTTGTGATTGTAGTTGCGGTCACAAAT
CATGAAGCTCCCTCCCCTGCCCATGGTATTAGCCTTTTTCTGGTGGAAAATGGAATGAAA
GGATTTATCAAGGGACGAAAGCTACATAAAATGGGATTAAAAGCCCAGGATACCGCAGAA
CTATTCTTTGAAGATATACGGTTGCCAGCTAGTGCCCTACTTGGAGAAGAGAATAAAGGC
TTCTATTACATCATGAAAGAGCTTCCACAGGAAAGGCTGTTAATTGCTGATGTGGCAATT
TCAGCTAGTGAATTCATGTTTGAAGAAACCAGGAACTATGTTAAACAAAGAAAAGCTTTT
GGCAAAACAGTTGCTCACCTACAGACAGTGCAACATAAATTAGCAGAATTAAAAACACAT
ATATGTGTAACCCGAGCATTTGTGGACAACTGTCTCCAGCTGCATGAAGCGAAACGTTTG
GACTCCGCCACTGCTTGCATGGCGAAATATTGGGCATCTGAGTTACAAAATAGTGTAGCT
TACGACTGTGTACAGCTCCATGGAGGTTGGGGATACATGTGGGAGTACCCAATTGCAAAA
GCTTATGTGGATGCCAGAGTTCAGCCAATCTATGGTGGTACAAATGAAATAATGAAGGAG
CTGATTGCAAGAGAGATTGTCTTTGACAAGTAG
|
| Enzyme 1 GenBank Gene ID |
M74096  |
| Enzyme 1 GeneCard ID |
ACADL  |
| Enzyme 1 GenAtlas ID |
ACADL  |
| Enzyme 1 HGNC ID |
HGNC:88  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2q34-q35 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1991 Nov;11(3):609-20. [PubMed
]
- Indo Y, Yang-Feng T, Glassberg R, Tanaka K: Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase and assignment of the location of its gene (ACADL) to chromosome 2. Genomics. 1992 Mar;12(3):626. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5335 |
| Enzyme 2 Name |
Short-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 2 Synonyms |
- SCAD
- Butyryl-CoA dehydrogenase
|
| Enzyme 2 Gene Name |
ACADS |
| Enzyme 2 Protein Sequence |
>Short-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS
|
| Enzyme 2 Number of Residues |
412 |
| Enzyme 2 Molecular Weight |
44296.7 |
| Enzyme 2 Theoretical pI |
8.12 |
| Enzyme 2 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 2 Specific Function |
Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor |
| Enzyme 2 Pathways |
- Butyrate Metabolism (map00650
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 2 Reactions |
- butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor [RN:R01178]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
337928  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P16219  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACADS_HUMAN  |
| Enzyme 2 PDB ID |
1JQI  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1239 bp
ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA
|
| Enzyme 2 GenBank Gene ID |
M26393  |
| Enzyme 2 GeneCard ID |
ACADS  |
| Enzyme 2 GenAtlas ID |
ACADS  |
| Enzyme 2 HGNC ID |
HGNC:90  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
12q22-qter |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed
]
- Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed
]
- Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed
]
- Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed
]
- Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5336 |
| Enzyme 3 Name |
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial |
| Enzyme 3 Synonyms |
- MCAD
|
| Enzyme 3 Gene Name |
ACADM |
| Enzyme 3 Protein Sequence |
>Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEI
IPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQ
TAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKG
DEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNM
GQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEAT
KYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAF
AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK
N
|
| Enzyme 3 Number of Residues |
421 |
| Enzyme 3 Molecular Weight |
46588.0 |
| Enzyme 3 Theoretical pI |
8.51 |
| Enzyme 3 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 3 Specific Function |
This enzyme is specific for acyl chain lengths of 4 to 16 |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor [RN:R00392]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
177964  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P11310  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACADM_HUMAN  |
| Enzyme 3 PDB ID |
1T9G  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1266 bp
ATGGCAGCGGGGTTCGGGCGATGCTGCAGGGTCCTGAGAAGTATTTCTCGTTTTCATTGG
AGATCACAGCATACAAAAGCCAATCGACAACGTGAACCAGGATTAGGATTTAGTTTTGAG
TTCACCGAACAGCAGAAAGAATTTCAAGCTACTGCTCGTAAATTTGCCAGAGAGGAAATC
ATCCCAGTGGCTGCAGAATATGATAAAACTGGTGAATATCCAGTCCCCCTAATTAGAAGA
GCCTGGGAACTTGGTTTAATGAACACACACATTCCAGAGAACTGTGGAGGTCTTGGACTT
GGAACTTTTGATGCTTGTTTAATTAGTGAAGAATTGGCTTATGGATGTACAGGGGTTCAG
ACTGCTATTGAAGGAAATTCTTTGGGGCAAATGCCTATTATTATTGCTGGAAATGATCAA
CAAAAGAAGAAGTATTTGGGGAGAATGACTGAGGAGCCATTGATGTGTGCTTATTGTGTA
ACAGAACCTGGAGCAGGCTCTGATGTAGCTGGTATAAAGACCAAAGCAGAAAAGAAAGGA
GATGAGTATATTATTAATGGTCAGAAGATGTGGATAACCAACGGAGGAAAAGCTAATTGG
TATTTTTTATTGGCACGTTCTGATCCAGATCCTAAAGCTCCTGCTAATAAAGCCTTTACT
GGATTCATTGTGGAAGCAGATACCCCAGGAATTCAGATTGGGAGAAAGGAATTAAACATG
GGCCAGCGATGTTCAGATACTAGAGGAATTGTCTTCGAAGATGTGAAAGTGCCTAAAGAA
AATGTTTTAATTGGTGACGGAGCTGGTTTCAAAGTTGCAATGGGAGCTTTTGATAAAACC
AGACCTGTAGTAGCTGCTGGTGCTGTTGGATTAGCACAAAGAGCTTTGGATGAAGCTACC
AAGTATGCCCTGGAAAGGAAAACTTTCGGAAAGCTACTTGTAGAGCACCAAGCAATATCA
TTTATGCTGGCTGAAATGGCAATGAAAGTTGAACTAGCTAGAATGAGTTACCAGAGAGCA
GCTTGGGAGGTTGATTCTGGTCGTCGAAATACCTATTATGCTTCTATTGCAAAGGCATTT
GCTGGAGATATTGCAAATCAGTTAGCTACTGATGCTGTGCAGATACTTGGAGGCAATGGA
TTTAATACAGAATATCCTGTAGAAAAACTAATGAGGGATGCCAAAATCTATCAGATTTAT
GAAGGTACTTCACAAATTCAAAGACTTATTGTAGCCCGTGAACACATTGACAAGTACAAA
AATTAA
|
| Enzyme 3 GenBank Gene ID |
M16827  |
| Enzyme 3 GeneCard ID |
ACADM  |
| Enzyme 3 GenAtlas ID |
ACADM  |
| Enzyme 3 HGNC ID |
HGNC:89  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p31 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Kelly DP, Kim JJ, Billadello JJ, Hainline BE, Chu TW, Strauss AW: Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc Natl Acad Sci U S A. 1987 Jun;84(12):4068-72. [PubMed
]
- Zhang ZF, Kelly DP, Kim JJ, Zhou YQ, Ogden ML, Whelan AJ, Strauss AW: Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene. Biochemistry. 1992 Jan 14;31(1):81-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR: Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ: Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Biochemistry. 1996 Sep 24;35(38):12412-20. [PubMed
]
- Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D: Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. [PubMed
]
- Toogood HS, van Thiel A, Scrutton NS, Leys D: Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. [PubMed
]
- Tanaka K, Yokota I, Coates PM, Strauss AW, Kelly DP, Zhang Z, Gregersen N, Andresen BS, Matsubara Y, Curtis D, et al.: Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. Hum Mutat. 1992;1(4):271-9. [PubMed
]
- Yokota I, Indo Y, Coates PM, Tanaka K: Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. [PubMed
]
- Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW: Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. [PubMed
]
- Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K: Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. [PubMed
]
- Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.: Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. [PubMed
]
- Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D: Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. [PubMed
]
- Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.: Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. [PubMed
]
- Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW: Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. [PubMed
]
- Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW: A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. [PubMed
]
- Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N: The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. [PubMed
]
- Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S: Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. [PubMed
]
- Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR: Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. [PubMed
]
- Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N: Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. [PubMed
]
- Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E: Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. [PubMed
]
- Albers S, Levy HL, Irons M, Strauss AW, Marsden D: Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5378 |
| Enzyme 4 Name |
Peroxisomal acyl-coenzyme A oxidase 1 |
| Enzyme 4 Synonyms |
- AOX
- Palmitoyl-CoA oxidase
- Straight-chain acyl-CoA oxidase
- SCOX
|
| Enzyme 4 Gene Name |
ACOX1 |
| Enzyme 4 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 1
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRY
EVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQK
EKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGL
GKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYL
KMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIA
IRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIG
QGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF
EGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSP
ESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFS
EKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIR
SDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
|
| Enzyme 4 Number of Residues |
660 |
| Enzyme 4 Molecular Weight |
74423.0 |
| Enzyme 4 Theoretical pI |
8.29 |
| Enzyme 4 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 4 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 4 Specific Function |
Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
14250616  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q15067  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
ACOX1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1983 bp
ATGAACCCGGACCTGCGCAGGGAGCGGGATTCCGCCAGCTTCAACCCGGAGCTGCTTACA
CACATCCTGGACGGCAGCCCCGAGAAAACCCGGCGCCGCCGAGAGATCGAGAACATGATC
CTGAACGACCCAGACTTCCAGCATGAGGACTTGAACTTCCTCACTCGCAGCCAGCGTTAT
GAGGTGGCTGTCAGGAAAAGTGCCATCATGGTGAAGAAGATGAGGGAGTTTGGCATCGCT
GACCCTGATGAAATTATGTGGTTTAAAAATTTTGTGCACCGAGGGCGGCCTGAGCCTCTG
GATCTTCACTTGGGCATGTTCCTGCCCACCTTGCTTCACCAGGCAACTGCGGAGCAGCAG
GAGCGCTTCTTCATGCCCGCCTGGAACTTGGAGATCATTGGCACTTATGCCCAGACAGAG
ATGGGTCATGGAACTCACCTTCGAGGCTTGGAAACCACAGCCACGTATGACCCTGAAACC
CAGGAGTTCATTCTCAACAGTCCTACTGTGACCTCCATTAAATGGTGGCCTGGTGGGCTT
GGAAAGACTTCAAATCATGCAATAGTTCTTGCCCAGCTCATCACTAAGGGGAAATGCTAT
GGATTACATGCCTTTATCGTACCTATTCGTGAAATCGGGACCCATAAGCCTTTGCCAGGA
ATTACCGTTGGTGACATCGGCCCCAAATTTGGTTATGATGAGATAGACAATGGCTACCTC
AAAATGGACAACCATCGTATTCCCAGAGAAAACATGCTGATGAAGTATGCCCAGGTGAAG
CCTGATGGCACATACGTGAAACCGCTGAGTAACAAGCTGACTTACGGGACCATGGTGTTT
GTCAGGTCCTTCCTTGTGGGAGAAGCTGCTCGGGCTCTGTCTAAGGCGTGCACCATTGCC
ATCCGATACAGCGCTGTGAGGCACCAGTCTGAAATGAAGCCAGGTGAACCAGAACCACAG
ATTTTGGATTTTCAAACCCAGCAGTATAAACTCTTTCCACTCCTGGCCACTGCCTATGCC
TTCCAGTTTGTGGGCGCATACATGAAGGAGACCTATCACCGGATTAACGAAGGCATTGGT
CAAGGGGACCTGAGTGAACTGCCTGAGCTTCATGCCCTCACCGCTGGACTGAAGGCTTTC
ACCTCCTGGACTGCAAACACTGGCATTGAAGCATGTCGGATGGCTTGTGGTGGGCATGGC
TATTCTCATTGCAGTGGTCTTCCAAATATTTATGTCAATTTCACCCCAAGCTGTACCTTT
GAGGGAGAAAACACTGTCATGATGCTCCAGACGGCTAGGTTCCTGATGAAAAGTTATGAT
CAGGTGCACTCAGGAAAGTTGGTGTGTGGCATGGTGTCCTATTTGAACGACCTGCCCAGT
CAGCGCATCCAGCCACAGCAGGTAGCAGTCTGGCCAACCATGGTGGATATCAACAGCCCC
GAAAGCCTAACCGAAGCATATAAACTCCGTGCAGCCAGATTAGTAGAAATTGCTGCAAAA
AACCTTCAAAAAGAAGTGATTCACAGAAAAAGCAAGGAGGTAGCTTGGAACCTAACTTCT
GTTGACCTTGTTCGAGCAAGTGAGGCACATTGCCACTATGTGGTAGTTAAGCTCTTTTCA
GAAAAACTCCTCAAAATTCAAGATAAAGCCATTCAAGCTGTCTTAAGGAGTTTATGTCTG
CTGTATTCTCTGTATGGAATCAGTCAGAACGCGGGGGATTTCCTTCAGGGGAGCATCATG
ACAGAGCCTCAGATTACACAAGTAAACCAGCGTGTAAAGGAGTTACTCACTCTGATTCGC
TCAGATGCTGTTGCTTTGGTTGATGCATTTGATTTTCAGGATGTGACACTTGGCTCTGTG
CTTGGCCGCTATGATGGGAATGTGTATGAAAACTTGTTTGAGTGGGCTAAGAACTCCCCA
CTGAACAAAGCAGAGGTCCACGAATCTTACAAGCACCTGAAGTCACTGCAGTCCAAGCTC
TGA
|
| Enzyme 4 GenBank Gene ID |
BC008767  |
| Enzyme 4 GeneCard ID |
ACOX1  |
| Enzyme 4 GenAtlas ID |
ACOX1  |
| Enzyme 4 HGNC ID |
HGNC:119  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
17q24-q25|17q25.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK: Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3107-11. [PubMed
]
- Chu R, Varanasi U, Chu S, Lin Y, Usuda N, Rao MS, Reddy JK: Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. J Biol Chem. 1995 Mar 3;270(9):4908-15. [PubMed
]
- Fournier B, Saudubray JM, Benichou B, Lyonnet S, Munnich A, Clevers H, Poll-The BT: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest. 1994 Aug;94(2):526-31. [PubMed
]
- Aoyama T, Tsushima K, Souri M, Kamijo T, Suzuki Y, Shimozawa N, Orii T, Hashimoto T: Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Suzuki Y, Iai M, Kamei A, Tanabe Y, Chida S, Yamaguchi S, Zhang Z, Takemoto Y, Shimozawa N, Kondo N: Peroxisomal acyl CoA oxidase deficiency. J Pediatr. 2002 Jan;140(1):128-30. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5383 |
| Enzyme 5 Name |
Heme oxygenase 2 |
| Enzyme 5 Synonyms |
- HO-2
|
| Enzyme 5 Gene Name |
HMOX2 |
| Enzyme 5 Protein Sequence |
>Heme oxygenase 2
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG
NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN
WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA
GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL
AAGVALAAGLLAWYYM
|
| Enzyme 5 Number of Residues |
316 |
| Enzyme 5 Molecular Weight |
36032.6 |
| Enzyme 5 Theoretical pI |
5.09 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
|
| Process |
- heme metabolic process
- heme oxidation
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in heme oxygenase (decyclizing) activity |
| Enzyme 5 Specific Function |
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
187761307  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P30519  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
HMOX2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>951 bp
ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG
GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG
ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC
AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC
CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC
ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC
TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC
ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT
CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA
GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG
CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG
GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC
GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA
GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC
AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG
GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
|
| Enzyme 5 GenBank Gene ID |
NM_001127204.1  |
| Enzyme 5 GeneCard ID |
HMOX2  |
| Enzyme 5 GenAtlas ID |
HMOX2  |
| Enzyme 5 HGNC ID |
HGNC:5014  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
16p13.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J Biol Chem. 1995 Mar 17;270(11):6345-50. [PubMed
]
- McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. 1992 May 15;295(1):13-20. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr: Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5398 |
| Enzyme 6 Name |
Isovaleryl-CoA dehydrogenase, mitochondrial |
| Enzyme 6 Synonyms |
- IVD
|
| Enzyme 6 Gene Name |
IVD |
| Enzyme 6 Protein Sequence |
>Isovaleryl-CoA dehydrogenase, mitochondrial
MATATRLLGWRVASWRLRPPLAGFVSQRAHSLLPVDDAINGLSEEQRQLRQTMAKFLQEH
LAPKAQEIDRSNEFKNLREFWKQLGNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASG
AVGLSYGAHSNLCINQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKA
EKKGNHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGFSTSKKL
DKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLERLVLAGGPLGLMQAVLD
HTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLMACRQYVYNVAKACDEGHCTAKDCAGV
ILYSAECATQVALDGIQCFGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNA
DFH
|
| Enzyme 6 Number of Residues |
423 |
| Enzyme 6 Molecular Weight |
46319.0 |
| Enzyme 6 Theoretical pI |
8.31 |
| Enzyme 6 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 6 Specific Function |
3-methylbutanoyl-CoA + acceptor = 3-methylbut- 2-enoyl-CoA + reduced acceptor |
| Enzyme 6 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 6 Reactions |
- 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor [RN:R04096]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
306897  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P26440  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
IVD_HUMAN  |
| Enzyme 6 PDB ID |
1IVH  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1272 bp
ATGGCGACTGCGACTCGGCTGCTGGGGTGGCGTGTGGCGAGCTGGAGGCTGCGGCCGCCG
CTTGCCGGCTTCGTTTCCCAGCGGGCCCACTCGCTTTTGCCCGTGGACGATGCAATCAAT
GGGCTAAGCGAGGAGCAGAGGCAGCTTCGTCAGACCATGGCTAAGTTCCTTCAGGAGCAC
CTGGCCCCCAAGGCCCAGGAGATCGATCGCAGCAATGAGTTCAAGAACCTGCGAGAATTT
TGGAAGCAGCTGGGGAACCTGGGCGTATTGGGCATCACAGCCCCTGTTCAGTATGGCGGC
TCCGGCCTGGGCTACCTGGAGCATGTGCTGGTGATGGAGGAGATATCCCGAGCTTCCGGA
GCAGTGGGGCTCAGTTACGGTGCCCACTCCAACCTCTGCATCAACCAGCTTGTACGCAAT
GGGAATGAGGCCCAGAAAGAGAAGTATCTCCCGAAGCTGATCAGTGGTGAGTACATCGGA
GCCCTGGCCATGAGTGAGCCCAATGCAGGCTCTGATGTTGTCTCTATGAAGCTCAAAGCG
GAAAAGAAAGGAAATCACTACATCCTGAATGGCAACAAGTTCTGGATCACTAATGGCCCT
GATGCTGACGTCCTGATTGTCTATGCCAAGACAGATCTGGCTGCTGTGCCAGCTTCTCGG
GGCATCACAGCCTTCATTGTGGAGAAGGGTATGCCTGGCTTTAGCACCTCTAAGAAGCTG
GACAAGCTGGGGATGAGGGGCTCTAACACCTGTGAGCTAATCTTTGAAGACTGCAAGATT
CCTGCTGCCAACATCCTGGGCCATGAGAATAAGGGTGTCTACGTGCTGATGAGTGGGCTG
GACCTGGAGCGGCTGGTGCTGGCCGGGGGGCCTCTTGGGCTCATGCAAGCGGTCCTGGAC
CACACCATTCCCTACCTGCACGTGAGGGAAGCCTTTGGCCAGAAGATCGGCCACTTCCAG
TTGATGCAGGGGAAGATGGCTGACATGTACACCCGCCTCATGGCGTGTCGGCAGTATGTC
TACAATGTCGCCAAGGCCTGCGATGAGGGCCATTGCACTGCTAAGGACTGTGCAGGTGTG
ATTCTTTACTCAGCTGAGTGTGCTACACAGGTAGCCCTGGACGGCATTCAGTGTTTTGGT
GGCAATGGCTACATCAATGACTTTCCCATGGGCCGCTTTCTTCGAGATGCCAAGCTGTAT
GAGATAGGGGCTGGGACCAGCGAGGTGAGGCGGCTGGTCATCGGCAGAGCCTTCAATGCA
GACTTTCACTAG
|
| Enzyme 6 GenBank Gene ID |
M34192  |
| Enzyme 6 GeneCard ID |
IVD  |
| Enzyme 6 GenAtlas ID |
IVD  |
| Enzyme 6 HGNC ID |
HGNC:6186  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
15q14-q15 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Matsubara Y, Ito M, Glassberg R, Satyabhama S, Ikeda Y, Tanaka K: Nucleotide sequence of messenger RNA encoding human isovaleryl-coenzyme A dehydrogenase and its expression in isovaleric acidemia fibroblasts. J Clin Invest. 1990 Apr;85(4):1058-64. [PubMed
]
- Vockley J, Rogan PK, Anderson BD, Willard J, Seelan RS, Smith DI, Liu W: Exon skipping in IVD RNA processing in isovaleric acidemia caused by point mutations in the coding region of the IVD gene. Am J Hum Genet. 2000 Feb;66(2):356-67. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Parimoo B, Tanaka K: Structural organization of the human isovaleryl-CoA dehydrogenase gene. Genomics. 1993 Mar;15(3):582-90. [PubMed
]
- Vockley J, Nagao M, Parimoo B, Tanaka K: The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors. J Biol Chem. 1992 Feb 5;267(4):2494-501. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Mohsen AW, Vockley J: Identification of the active site catalytic residue in human isovaleryl-CoA dehydrogenase. Biochemistry. 1995 Aug 15;34(32):10146-52. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Tiffany KA, Roberts DL, Wang M, Paschke R, Mohsen AW, Vockley J, Kim JJ: Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,. Biochemistry. 1997 Jul 15;36(28):8455-64. [PubMed
]
- Vockley J, Parimoo B, Tanaka K: Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia. Am J Hum Genet. 1991 Jul;49(1):147-57. [PubMed
]
- Mohsen AW, Anderson BD, Volchenboum SL, Battaile KP, Tiffany K, Roberts D, Kim JJ, Vockley J: Characterization of molecular defects in isovaleryl-CoA dehydrogenase in patients with isovaleric acidemia. Biochemistry. 1998 Jul 14;37(28):10325-35. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5424 |
| Enzyme 7 Name |
Peroxisomal acyl-coenzyme A oxidase 3 |
| Enzyme 7 Synonyms |
- Branched-chain acyl-CoA oxidase
- BRCACox
- Pristanoyl-CoA oxidase
|
| Enzyme 7 Gene Name |
ACOX3 |
| Enzyme 7 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL
|
| Enzyme 7 Number of Residues |
700 |
| Enzyme 7 Molecular Weight |
77628.3 |
| Enzyme 7 Theoretical pI |
7.27 |
| Enzyme 7 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 7 General Function |
Involved in oxidoreductase activity, acting on the CH-CH group of donors |
| Enzyme 7 Specific Function |
Oxidizes the CoA-esters of 2-methyl-branched fatty acids |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 [RN:R00388]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
2326549  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
O15254  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
ACOX3_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG
|
| Enzyme 7 GenBank Gene ID |
Y11411  |
| Enzyme 7 GeneCard ID |
ACOX3  |
| Enzyme 7 GenAtlas ID |
ACOX3  |
| Enzyme 7 HGNC ID |
HGNC:121  |
| Enzyme 7 Chromosome Location |
4 |
| Enzyme 7 Locus |
4p15.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5429 |
| Enzyme 8 Name |
Glycerol-3-phosphate dehydrogenase, mitochondrial |
| Enzyme 8 Synonyms |
- GPD-M
- GPDH-M
- mtGPD
|
| Enzyme 8 Gene Name |
GPD2 |
| Enzyme 8 Protein Sequence |
>Glycerol-3-phosphate dehydrogenase, mitochondrial
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
|
| Enzyme 8 Number of Residues |
727 |
| Enzyme 8 Molecular Weight |
80852.0 |
| Enzyme 8 Theoretical pI |
7.77 |
| Enzyme 8 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- glycerol-3-phosphate dehydrogenase activity
- ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
|
| Process |
- alcohol metabolic process
- alditol metabolic process
- glycerol metabolic process
- glycerol-3-phosphate metabolic process
- metabolic process
- oxidation reduction
- polyol metabolic process
- small molecule metabolic process
|
| Component |
- glycerol-3-phosphate dehydrogenase complex
- macromolecular complex
- protein complex
|
|
| Enzyme 8 General Function |
Involved in calcium ion binding |
| Enzyme 8 Specific Function |
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol [RN:R00849]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
285002233  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P43304  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GPDM_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2184 bp
ATGGCATTTCAAAAGGCAGTGAAAGGGACGATTCTTGTTGGAGGAGGTGCTCTTGCAACT
GTTTTAGGACTTTCTCAGTTTGCTCATTACAGAAGGAAACAAATGAACCTGGCCTATGTT
AAAGCAGCAGACTGCATTTCAGAACCAGTTAACAGGGAGCCTCCTTCCAGAGAAGCTCAG
CTACTGACTTTGCAAAACACATCTGAATTTGATATCCTTGTTATTGGAGGAGGAGCAACA
GGAAGTGGCTGTGCGCTAGATGCTGTCACCAGAGGACTAAAAACAGCCCTTGTAGAAAGA
GATGATTTCTCATCAGGGACCAGCAGCAGAAGCACTAAATTGATCCATGGTGGTGTGAGA
TATCTGCAGAAGGCCATCATGAAGTTGGATATTGAGCAGTATAGGATGGTAAAAGAAGCC
CTTCATGAGCGTGCCAACCTGCTAGAAATTGCTCCCCATTTATCAGCTCCATTGCCTATA
ATGCTTCCAGTTTACAAGTGGTGGCAGTTACCTTACTACTGGGTAGGAATCAAGCTGTAT
GATTTGGTTGCAGGAAGCAATTGCCTAAAAAGCAGTTATGTCCTCAGCAAATCAAGAGCC
CTTGAACATTTCCCAATGCTCCAGAAGGACAAACTGGTAGGAGCAATTGTCTACTATGAC
GGACAACATAACGATGCACGGATGAACCTTGCCATTGCTCTGACTGCTGCCAGGTATGGG
GCTGCCACAGCCAATTACATGGAGGTAGTGAGCTTGCTCAAGAAGACAGACCCCCAGACA
GGGAAAGTGCGTGTGAGCGGCGCACGGTGCAAGGATGTCCTCACAGGGCAGGAATTTGAC
GTGAGAGCCAAATGTGTTATCAATGCCACGGGACCTTTCACGGACTCTGTGCGCAAAATG
GATGATAAAGACGCAGCAGCTATCTGCCAGCCAAGTGCTGGTGTCCATATTGTGATGCCT
GGTTATTACAGCCCAGAGAGCATGGGACTTCTTGACCCAGCGACCAGTGATGGGCGAGTT
ATTTTCTTCTTACCCTGGCAAAAGATGACGATCGCTGGCACTACTGATACTCCAACTGAT
GTTACACACCATCCAATTCCTTCAGAAGAAGATATCAACTTCATTTTGAATGAAGTGCGT
AATTACCTGAGTTGTGATGTTGAAGTGAGAAGAGGGGATGTCCTGGCAGCATGGAGTGGA
ATCCGTCCTCTTGTTACAGACCCCAAATCTGCAGATACTCAGTCTATCTCCCGAAATCAT
GTTGTTGATATCAGTGAGAGTGGCCTTATTACTATAGCAGGTGGAAAGTGGACAACTTAT
CGGTCTATGGCAGAAGATACCATAAATGCTGCTGTCAAAACTCATAATTTAAAAGCAGGA
CCAAGTAGAACAGTTGGGCTTTTCCTTCAAGGGGGTAAAGATTGGAGCCCCACACTCTAC
ATTAGGCTTGTGCAGGATTATGGACTTGAAAGCGAGGTGGCACAGCATCTTGCCGCCACC
TATGGTGATAAGGCCTTTGAGGTGGCCAAAATGGCAAGTGTGACTGGCAAAAGGTGGCCT
ATTGTTGGAGTACGTCTTGTGTCAGAATTTCCATATATTGAAGCAGAGGTGAAATATGGG
ATTAAGGAGTATGCCTGCACTGCTGTGGATATGATTTCACGTCGTACTCGCCTGGCCTTT
CTAAATGTCCAGGCAGCAGAGGAAGCCCTACCCAGGATTGTTGAACTGATGGGCAGGGAA
CTGAATTGGGATGATTATAAGAAGCAGGAACAACTTGAAACAGCCAGGAAGTTTCTATAT
TATGAAATGGGCTATAAATCTCGATCAGAACAGTTAACAGATCGCTCTGAAATTAGCCTA
CTGCCTTCAGACATTGACAGGTATAAGAAGAGATTTCATAAGTTTGATGCAGACCAGAAA
GGCTTTATTACCATTGTTGATGTTCAGCGTGTATTAGAGAGTATCAATGTCCAAATGGAT
GAAAATACACTCCATGAAATTCTAAATGAAGTTGATTTGAATAAAAATGGACAGGTTGAA
CTCAATGAATTTTTGCAGCTGATGAGTGCTATTCAAAAAGGAAGGGTATCTGGAAGCCGG
CTTGCTATACTAATGAAAACTGCAGAAGAGAACCTCGACAGAAGAGTTCCAATTCCAGTG
GACCGTAGTTGTGGAGGATTGTGA
|
| Enzyme 8 GenBank Gene ID |
NM_000408.4  |
| Enzyme 8 GeneCard ID |
GPD2  |
| Enzyme 8 GenAtlas ID |
GPD2  |
| Enzyme 8 HGNC ID |
HGNC:4456  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
2q24.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Lehn DA, Brown LJ, Simonson GD, Moran SM, MacDonald MJ: The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA. Gene. 1994 Dec 15;150(2):417-8. [PubMed
]
- Ferrer J, Aoki M, Behn P, Nestorowicz A, Riggs A, Permutt MA: Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker. Diabetes. 1996 Feb;45(2):262-6. [PubMed
]
- Brown LJ, Stoffel M, Moran SM, Fernald AA, Lehn DA, LeBeau MM, MacDonald MJ: Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene. Gene. 1996 Jun 26;172(2):309-12. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5430 |
| Enzyme 9 Name |
Heme oxygenase 1 |
| Enzyme 9 Synonyms |
- HO-1
|
| Enzyme 9 Gene Name |
HMOX1 |
| Enzyme 9 Protein Sequence |
>Heme oxygenase 1
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA
LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE
VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ
LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA
SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
|
| Enzyme 9 Number of Residues |
288 |
| Enzyme 9 Molecular Weight |
32818.3 |
| Enzyme 9 Theoretical pI |
8.68 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
|
| Process |
- heme metabolic process
- heme oxidation
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in heme oxygenase (decyclizing) activity |
| Enzyme 9 Specific Function |
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
35173  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P09601  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
HMOX1_HUMAN  |
| Enzyme 9 PDB ID |
1T5P  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>867 bp
ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC
ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC
CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC
CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA
GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC
TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG
GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC
CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT
GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG
CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA
GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG
CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC
AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC
ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA
GTTGCTGTAGGGCTTTATGCCATGTGA
|
| Enzyme 9 GenBank Gene ID |
X06985  |
| Enzyme 9 GeneCard ID |
HMOX1  |
| Enzyme 9 GenAtlas ID |
HMOX1  |
| Enzyme 9 HGNC ID |
HGNC:5013  |
| Enzyme 9 Chromosome Location |
2 |
| Enzyme 9 Locus |
22q12|22q13.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S: Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988 Feb 1;171(3):457-61. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Keyse SM, Tyrrell RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989 Jan;86(1):99-103. [PubMed
]
- Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem. 1989 Feb 15;179(3):557-63. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL: Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5434 |
| Enzyme 10 Name |
Glutaryl-CoA dehydrogenase, mitochondrial |
| Enzyme 10 Synonyms |
- GCD
|
| Enzyme 10 Gene Name |
GCDH |
| Enzyme 10 Protein Sequence |
>Glutaryl-CoA dehydrogenase, mitochondrial
MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQL
TTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSS
VAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLT
EPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEK
GMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWG
VLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQD
KAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIH
ALILGRAITGIQAFTASK
|
| Enzyme 10 Number of Residues |
438 |
| Enzyme 10 Molecular Weight |
48126.7 |
| Enzyme 10 Theoretical pI |
8.15 |
| Enzyme 10 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 10 Specific Function |
Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- glutaryl-CoA + acceptor = crotonoyl-CoA + CO2 + reduced acceptor [RN:R02488]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
Not Available |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q92947  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
GCDH_HUMAN  |
| Enzyme 10 PDB ID |
1SIR  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1317 bp
ATGGCCCTGAGAGGCGTCTCCGTGCGGCTGCTGAGCCGCGGACCCGGCCTGCACGTCCTT
CGCACGTGGGTCTCGTCGGCGGCGCAGACCGAGAAAGGCGGGAGAACACAGAGCCAACTG
GCTAAGTCCTCGCGTCCCGAGTTTGACTGGCAGGACCCGCTGGTGCTGGAGGAGCAGCTG
ACCACAGATGAGATCCTCATCAGGGACACCTTCCGCACCTACTGCCAGGAGAGACTCATG
CCTCGCATCCTGTTGGCCAATCGCAACGAAGTTTTTCATCGGGAGATCATTTCGGAGATG
GGGGAGTTGGGTGTGCTGGGCCCCACCATCAAAGGATATGGCTGTGCTGGGGTTTCGTCT
GTGGCCTATGGGCTCCTGGCCCGAGAGCTGGAGCGGGTGGACAGTGGCTACAGGTCGGCG
ATGAGTGTCCAGTCCTCCCTCGTCATGCACCCTATCTATGCCTATGGCAGCGAGGAACAG
CGGCAGAAGTACCTGCCCCAGCTGGCCAAGGGGGAGCTCCTGGGCTGCTTCGGGCTCACA
GAGCCCAACAGCGGAAGTGACCCCAGCAGCATGGAGACCAGAGCCCACTACAACTCATCC
AACAAGAGCTACACCCTCAATGGGACCAAGACCTGGATCACGAACTCGCCTATGGCCGAT
CTGTTTGTAGTGTGGGCTCGGTGTGAAGATGGCTGCATTCGGGGCTTCCTGCTGGAGAAG
GGGATGCGGGGTCTCTCGGCCCCCAGGATCCAGGGCAAGTTCTCGCTGCGGGCCTCAGCC
ACAGGCATGATCATCATGGACGGTGTGGAGGTGCCAGAGGAGAATGTGCTCCCTGGTGCA
TCCAGCCTGGGGGGTCCCTTCGGCTGCCTGAACAACGCCCGGTACGGCATCGCGTGGGGC
GTGCTTGGAGCTTCGGAGTTCTGCTTGCACACAGCCCGGCAGTACGCCCTCGACAGGATG
CAGTTTGGTGTCCCACTGGCCAGGAACCAGCTGATTCAGAAGAAGCTGGCAGACATGCTC
ACTGAGATTACCCTGGGCCTTCACGCCTGCCTGCAGCTCGGCCGCTTGAAGGACCAGGAC
AAGGCTGCCCCCGAGATGGTTTCTCTGCTGAAGAGGAATAACTGTGGGAAAGCCCTGGAC
ATCGCCCGCCAGGCCCGAGACATGCTGGGGGGGAATGGGATTTCTGACGAGTATCACGTG
ATCCGGCACGCCATGAACCTGGAGGCCGTGAACACCTACGAAGGTACACATGACATTCAC
GCCCTGATCCTTGGGAGAGCTATCACGGGAATCCAGGCGTTCACGGCCAGCAAGTGA
|
| Enzyme 10 GenBank Gene ID |
U69141  |
| Enzyme 10 GeneCard ID |
GCDH  |
| Enzyme 10 GenAtlas ID |
GCDH  |
| Enzyme 10 HGNC ID |
HGNC:4189  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
19p13.2 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Goodman SI, Kratz LE, Frerman FE: Pork and human cDNAs encoding glutaryl-CoA dehydrogenase. Prog Clin Biol Res. 1992;375:169-73. [PubMed
]
- Goodman SI, Kratz LE, DiGiulio KA, Biery BJ, Goodman KE, Isaya G, Frerman FE: Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild type and mutant enzymes in Escherichia coli. Hum Mol Genet. 1995 Sep;4(9):1493-8. [PubMed
]
- Schwartz M, Christensen E, Superti-Furga A, Brandt NJ: The human glutaryl-CoA dehydrogenase gene: report of intronic sequences and of 13 novel mutations causing glutaric aciduria type I. Hum Genet. 1998 Apr;102(4):452-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Goodman SI, Stein DE, Schlesinger S, Christensen E, Schwartz M, Greenberg CR, Elpeleg ON: Glutaryl-CoA dehydrogenase mutations in glutaric acidemia (type I): review and report of thirty novel mutations. Hum Mutat. 1998;12(3):141-4. [PubMed
]
- Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ: Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry. 2004 Aug 3;43(30):9674-84. [PubMed
]
- Rao KS, Fu Z, Albro M, Narayanan B, Baddam S, Lee HJ, Kim JJ, Frerman FE: The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate. Biochemistry. 2007 Dec 18;46(50):14468-77. Epub 2007 Nov 17. [PubMed
]
- Biery BJ, Stein DE, Morton DH, Goodman SI: Gene structure and mutations of glutaryl-coenzyme A dehydrogenase: impaired association of enzyme subunits that is due to an A421V substitution causes glutaric acidemia type I in the Amish. Am J Hum Genet. 1996 Nov;59(5):1006-11. [PubMed
]
- Anikster Y, Shaag A, Joseph A, Mandel H, Ben-Zeev B, Christensen E, Elpeleg ON: Glutaric aciduria type I in the Arab and Jewish communities in Israel. Am J Hum Genet. 1996 Nov;59(5):1012-8. [PubMed
]
- Muhlhausen C, Christensen E, Schwartz M, Muschol N, Ullrich K, Lukacs Z: Severe phenotype despite high residual glutaryl-CoA dehydrogenase activity: a novel mutation in a Turkish patient with glutaric aciduria type I. J Inherit Metab Dis. 2003;26(7):713-4. [PubMed
]
- Keyser B, Muhlhausen C, Dickmanns A, Christensen E, Muschol N, Ullrich K, Braulke T: Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH). Hum Mol Genet. 2008 Dec 15;17(24):3854-63. Epub 2008 Sep 5. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
7987 |
| Enzyme 11 Name |
L-2-hydroxyglutarate dehydrogenase, mitochondrial |
| Enzyme 11 Synonyms |
- Duranin
|
| Enzyme 11 Gene Name |
L2HGDH |
| Enzyme 11 Protein Sequence |
>L-2-hydroxyglutarate dehydrogenase, mitochondrial
MVPALRYLVGACGRARGRFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVG
LASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALL
YEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCR
GLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPI
VIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNI
YPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKL
ASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFV
FDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL
|
| Enzyme 11 Number of Residues |
463 |
| Enzyme 11 Molecular Weight |
50358.6 |
| Enzyme 11 Theoretical pI |
8.34 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in 2-hydroxyglutarate dehydrogenase activity |
| Enzyme 11 Specific Function |
(S)-2-hydroxyglutarate + acceptor = 2- oxoglutarate + reduced acceptor |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor [RN:R00298]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
10434215  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9H9P8  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
L2HDH_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1392 bp
ATGGTGCCAGCGCTGCGTTATTTGGTTGGTGCCTGCGGACGGGCCCGCGGGCTTTTCGCC
GGTGGCTCCCCTGGGGCGTGCGGGTTCGCGTCTGGGAGGCCAAGACCGCTGTGTGGAGGT
AGCCGCAGCGCCAGCACCAGCTCATTTGATATAGTCATCGTTGGTGGCGGAATTGTGGGG
CTTGCCTCTGCCAGAGCACTCATCCTGCGACATCCATCACTTTCTATTGGTGTTCTGGAA
AAGGAGAAAGATTTAGCTGTTCACCAGACTGGACATAACAGTGGTGTCATACATAGTGGA
ATTTATTATAAACCTGAGTCTCTGAAAGCCAAATTATGTGTACAAGGTGCAGCCCTCCTC
TATGAGTACTGTCAGCAAAAGGGGATTTCCTACAAGCAGTGTGGCAAGCTTATAGTAGCT
GTTGAACAAGAAGAAATTCCCAGACTTCAGGCCCTATATGAGAAAGGCCTCCAGAATGGT
GTCCCGGGCCTGAGGCTGATCCAGCAGGAGGATATAAAAAAGAAGGAGCCATATTGTAGG
GGTCTAATGGCTATTGATTGTCCACATACTGGCATTGTGGACTATCGGCAGGTGGCTTTG
TCATTTGCCCAGGATTTCCAAGAAGCAGGTGGCTCTGTCTTGACCAATTTTGAAGTAAAA
GGTATTGAAATGGCTAAAGAAAGTCCTTCAAGAAGTATAGATGGAATGCAATATCCAATT
GTTATAAAGAATACAAAGGGAGAGGAAATTCGATGTCAGTATGTTGTGACATGTGCAGGA
CTTTACTCAGACCGTATTTCAGAGTTGAGTGGCTGCACTCCTGATCCTCGAATTGTACCA
TTCCGGGGAGATTACCTGCTTTTGAAGCCAGAAAAATGTTATCTTGTAAAAGGAAATATT
TATCCGGTCCCAGATAGCCGGTTTCCTTTCCTAGGAGTTCACTTCACACCAAGGATGGAT
GGCAGTATTTGGCTAGGGCCTAATGCAGTTCTTGCCTTTAAACGAGAGGGTTACAGACCC
TTTGACTTCAGTGCCACAGATGTTATGGATATAATTATCAATAGTGGCTTGATTAAACTG
GCATCCCAGAATTTTTCCTATGGAGTTACTGAAATGTATAAAGCATGTTTTCTTGGTGCA
ACAGTGAAGTATCTTCAAAAATTCATCCCTGAAATTACTATCAGTGATATACTTAGGGGC
CCAGCTGGAGTAAGAGCCCAGGCCCTGGATAGAGATGGAAATCTGGTAGAAGATTTTGTA
TTTGATGCAGGAGTTGGGGATATTGGAAATCGCATTCTTCATGTGAGAAATGCACCTTCT
CCTGCTGCTACTTCTTCCATTGCAATTTCTGGAATGATTGCAGATGAAGTACAACAAAGA
TTTGAATTATAA
|
| Enzyme 11 GenBank Gene ID |
AK022680  |
| Enzyme 11 GeneCard ID |
L2HGDH  |
| Enzyme 11 GenAtlas ID |
Not Available |
| Enzyme 11 HGNC ID |
Not Available |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
14q21.3 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Rzem R, Veiga-da-Cunha M, Noel G, Goffette S, Nassogne MC, Tabarki B, Scholler C, Marquardt T, Vikkula M, Van Schaftingen E: A gene encoding a putative FAD-dependent L-2-hydroxyglutarate dehydrogenase is mutated in L-2-hydroxyglutaric aciduria. Proc Natl Acad Sci U S A. 2004 Nov 30;101(48):16849-54. Epub 2004 Nov 17. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Rzem R, Van Schaftingen E, Veiga-da-Cunha M: The gene mutated in l-2-hydroxyglutaric aciduria encodes l-2-hydroxyglutarate dehydrogenase. Biochimie. 2006 Jan;88(1):113-6. Epub 2005 Jun 23. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Topcu M, Jobard F, Halliez S, Coskun T, Yalcinkayal C, Gerceker FO, Wanders RJ, Prud'homme JF, Lathrop M, Ozguc M, Fischer J: L-2-Hydroxyglutaric aciduria: identification of a mutant gene C14orf160, localized on chromosome 14q22.1. Hum Mol Genet. 2004 Nov 15;13(22):2803-11. Epub 2004 Sep 22. [PubMed
]
- Vilarinho L, Cardoso ML, Gaspar P, Barbot C, Azevedo L, Diogo L, Santos M, Carrilho I, Fineza I, Kok F, Chorao R, Alegria P, Martins E, Teixeira J, Cabral Fernandes H, Verhoeven NM, Salomons GS, Santorelli FM, Cabral P, Amorim A, Jakobs C: Novel L2HGDH mutations in 21 patients with L-2-hydroxyglutaric aciduria of Portuguese origin. Hum Mutat. 2005 Oct;26(4):395-6. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
13021 |
| Enzyme 12 Name |
cDNA FLJ76015, highly similar to Homo sapiens glutaryl-Coenzyme A dehydrogenase |
| Enzyme 12 Synonyms |
- GCDH, nuclear gene encoding mitochondrial protein, transcript variant 1, mRNA
- Glutaryl-Coenzyme A dehydrogenase, isoform CRA_a
|
| Enzyme 12 Gene Name |
GCDH |
| Enzyme 12 Protein Sequence |
>cDNA FLJ76015, highly similar to Homo sapiens glutaryl-Coenzyme A dehydrogenase
MALRGVSVRLLSRGPGLHVLRTWVSSAAQTEKGGRTQSQLAKSSRPEFDWQDPLVLEEQL
TTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSS
VAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLT
EPNSGSDPSSMETRAHYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEK
GMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYGIAWG
VLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQD
KAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYEGTHDIH
ALILGRAITGIQAFTASK
|
| Enzyme 12 Number of Residues |
438 |
| Enzyme 12 Molecular Weight |
48128 |
| Enzyme 12 Theoretical pI |
8.15 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Lipid transport and metabolism |
| Enzyme 12 Specific Function |
Not Available |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
Not Available |
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
158261837  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
A8K2Z2  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
A8K2Z2_HUMAN  |
| Enzyme 12 PDB ID |
1SIR  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
AK290407  |
| Enzyme 12 GeneCard ID |
A8K2Z2  |
| Enzyme 12 GenAtlas ID |
Not Available |
| Enzyme 12 HGNC ID |
Not Available |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
Not Available |
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
13023 |
| Enzyme 13 Name |
Acyl-Coenzyme A dehydrogenase, long chain |
| Enzyme 13 Synonyms |
- Putative uncharacterized protein ACADL
|
| Enzyme 13 Gene Name |
ACADL |
| Enzyme 13 Protein Sequence |
>Acyl-Coenzyme A dehydrogenase, long chain
MAARLLRGSLRVLGGHRAPRQLPAARCSHSGGEERLETPSAKKLTDIGIRRIFSPEHDIF
RKSVRKFFQEEVIPHHSEWEKAGEVSREVWEKAGKQGLLGVNIAEHLGGIGGDLYSAAIV
WEEQAYSNCSGPGFSIHSGIVMSYITNHGSEEQIKHFIPQMTAGKCIGAIAMTEPGAGSD
LQGIKTNAKKDGSDWILNGSKVFISNGSLSDVVIVVAVTNHEAPSPAHGISLFLVENGMK
GFIKGRKLHKMGLKAQDTAELFFEDIRLPASALLGEENKGFYYIMKELPQERLLIADVAI
SASEFMFEETRNYVKQRKAFGKTVAHLQTVQHKLAELKTHICVTRAFVDNCLQLHEAKRL
DSATACMAKYWASELQNSVAYDCVQLHGGWGYMWEYPIAKAYVDARVQPIYGGTNEIMKE
LIAREIVFDK
|
| Enzyme 13 Number of Residues |
430 |
| Enzyme 13 Molecular Weight |
47656 |
| Enzyme 13 Theoretical pI |
7.89 |
| Enzyme 13 GO Classification |
| Function |
- acyl-CoA dehydrogenase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Lipid transport and metabolism |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
24660234  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q8IUN8  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
Q8IUN8_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
Not Available |
| Enzyme 13 GenBank Gene ID |
BC039063  |
| Enzyme 13 GeneCard ID |
Q8IUN8  |
| Enzyme 13 GenAtlas ID |
ACADL  |
| Enzyme 13 HGNC ID |
HGNC:88  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
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Enzyme 14
[top]
|
| Enzyme 14 ID |
13047 |
| Enzyme 14 Name |
cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2 |
| Enzyme 14 Synonyms |
- mitochondrial
- GPD2, mRNA
- Glycerol-3-phosphate dehydrogenase 2
- Mitochondrial, isoform CRA_b
- cDNA FLJ78257, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
- mitochondrial
- GPD2, mRNA
|
| Enzyme 14 Gene Name |
GPD2 |
| Enzyme 14 Protein Sequence |
>cDNA FLJ75492, highly similar to Homo sapiens glycerol-3-phosphate dehydrogenase 2
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVHVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
|
| Enzyme 14 Number of Residues |
727 |
| Enzyme 14 Molecular Weight |
80835 |
| Enzyme 14 Theoretical pI |
7.58 |
| Enzyme 14 GO Classification |
Not Available |
| Enzyme 14 General Function |
Energy production and conversion |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
Not Available |
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
158255566  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
A8K4V0  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
A8K4V0_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
Not Available |
| Enzyme 14 GenBank Gene ID |
AK291065  |
| Enzyme 14 GeneCard ID |
A8K4V0  |
| Enzyme 14 GenAtlas ID |
Not Available |
| Enzyme 14 HGNC ID |
Not Available |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
Not Available |
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
15245 |
| Enzyme 15 Name |
Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c) |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
ZNF554 |
| Enzyme 15 Protein Sequence |
>Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
MDFSQEEWELLEPAQKNLYREVMLENYRNVVSLEALKNQCTDVGIKEGPLSPAQTSQVTS
LSSWTGYLLFQPVASSHLEQREALWIEEKGTPQASCSDWMTVLRNQDSTYKKVALQEEPA
SGINMIKLIREDGGWKQLEDSHEDPQGLLSQKASLHVVAVPQEKATAWHGFGENGNLSPA
LVLSQGSSKGNHLCGSELDITSLASDSVLNHHQLGYADRRPCESNECGNAIRQNSHFIQH
GGKMFVYLENGQSLNHGMALTIHNKINTAEKPFECHQCGKVFNRRHSLSEHQRIHTGEKP
YECQECGRAFTHSSTLTRHLRTHTGEKPYGCGECGKAFNRISSLTQHQRIHTGEKPYKCE
DCGKSFCQSSYLILHKRTHTGEKPYECSECGKAFSDRSSLNQHERTHTGENPYECKQCGR
AFSQRSSLVRHERTHTGEKPYRCQECGKAFSQSSSLVTHQKTHSSQKTYKIIDCGKAFYQ
NRHLIGY
|
| Enzyme 15 Number of Residues |
487 |
| Enzyme 15 Molecular Weight |
54974 |
| Enzyme 15 Theoretical pI |
7.67 |
| Enzyme 15 GO Classification |
Not Available |
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
A8MT35  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
A8MT35_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
Not Available |
| Enzyme 15 GenBank Gene ID |
AC006130  |
| Enzyme 15 GeneCard ID |
A8MT35  |
| Enzyme 15 GenAtlas ID |
HMOX2  |
| Enzyme 15 HGNC ID |
HGNC:5014  |
| Enzyme 15 Chromosome Location |
19 |
| Enzyme 15 Locus |
19p13.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
Not Available |
| Enzyme 15 Metabolite References |
Not Available |