|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5260 |
| Enzyme 1 Name |
3-ketoacyl-CoA thiolase, mitochondrial |
| Enzyme 1 Synonyms |
- Acetyl-CoA acyltransferase
- Beta-ketothiolase
- Mitochondrial 3-oxoacyl-CoA thiolase
- T1
|
| Enzyme 1 Gene Name |
ACAA2 |
| Enzyme 1 Protein Sequence |
>3-ketoacyl-CoA thiolase, mitochondrial
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
|
| Enzyme 1 Number of Residues |
397 |
| Enzyme 1 Molecular Weight |
41923.8 |
| Enzyme 1 Theoretical pI |
8.21 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 1 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 1 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 1 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
12804931  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P42765  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
THIM_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGTGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
|
| Enzyme 1 GenBank Gene ID |
BC001918  |
| Enzyme 1 GeneCard ID |
ACAA2  |
| Enzyme 1 GenAtlas ID |
ACAA2  |
| Enzyme 1 HGNC ID |
HGNC:83  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
18q21.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Abe H, Ohtake A, Yamamoto S, Satoh Y, Takayanagi M, Amaya Y, Takiguchi M, Sakuraba H, Suzuki Y, Mori M, et al.: Cloning and sequence analysis of a full length cDNA encoding human mitochondrial 3-oxoacyl-CoA thiolase. Biochim Biophys Acta. 1993 Nov 16;1216(2):304-6. [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
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5277 |
| Enzyme 2 Name |
Trifunctional enzyme subunit beta, mitochondrial |
| Enzyme 2 Synonyms |
- TP-beta
- 3-ketoacyl-CoA thiolase
- Acetyl-CoA acyltransferase
- Beta-ketothiolase
|
| Enzyme 2 Gene Name |
HADHB |
| Enzyme 2 Protein Sequence |
>Trifunctional enzyme subunit beta, mitochondrial
MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
|
| Enzyme 2 Number of Residues |
474 |
| Enzyme 2 Molecular Weight |
51294.0 |
| Enzyme 2 Theoretical pI |
9.94 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 2 Specific Function |
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA |
| Enzyme 2 Pathways |
- Benzoate Degradation via Hydroxylation (map00362
)
- Bile Acid Biosynthesis (map00120
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 2 Reactions |
- acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P55084  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ECHB_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1425 bp
ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA
|
| Enzyme 2 GenBank Gene ID |
D16481  |
| Enzyme 2 GeneCard ID |
HADHB  |
| Enzyme 2 GenAtlas ID |
HADHB  |
| Enzyme 2 HGNC ID |
HGNC:4803  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
2p23 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed
]
- Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [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
]
- 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
]
- Middleton B: The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase. Biochem Soc Trans. 1994 May;22(2):427-31. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Kamijo T, Wanders RJ, Saudubray JM, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest. 1994 Apr;93(4):1740-7. [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
]
- Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed
]
- Spiekerkoetter U, Sun B, Khuchua Z, Bennett MJ, Strauss AW: Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations. Hum Mutat. 2003 Jun;21(6):598-607. [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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5616 |
| Enzyme 3 Name |
3-hydroxyacyl-CoA dehydrogenase type-2 |
| Enzyme 3 Synonyms |
- 17-beta-hydroxysteroid dehydrogenase 10
- 17-beta-HSD 10
- 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
- 3-hydroxyacyl-CoA dehydrogenase type II
- Endoplasmic reticulum-associated amyloid beta-peptide-binding protein
- Mitochondrial ribonuclease P protein 2
- Mitochondrial RNase P protein 2
- Short-chain type dehydrogenase/reductase XH98G2
- Type II HADH
|
| Enzyme 3 Gene Name |
HSD17B10 |
| Enzyme 3 Protein Sequence |
>3-hydroxyacyl-CoA dehydrogenase type-2
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAI
IENPFLNGEVIRLDGAIRMQP
|
| Enzyme 3 Number of Residues |
261 |
| Enzyme 3 Molecular Weight |
26922.9 |
| Enzyme 3 Theoretical pI |
7.94 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in oxidoreductase activity |
| Enzyme 3 Specific Function |
Functions in mitochondrial tRNA maturation. Part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5'-ends. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) |
| Enzyme 3 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 3 Reactions |
- (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+ [RN:R04203]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q99714  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
HCD2_HUMAN  |
| Enzyme 3 PDB ID |
1SO8  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>786 bp
ATGGCAGCAGCGTGTCGGAGCGTGAAGGGCCTGGTGGCGGTAATAACCGGAGGAGCCTCG
GGCCTGGGCCTGGCCACGGCGGAGCGACTTGTGGGGCAGGGAGCCTCTGCTGTGCTTCTG
GACCTGCCCAACTCGGGTGGGGAGGCCCAAGCCAAGAAGTTAGGAAACAACTGCGTTTTC
GCCCCAGCCGACGTGACCTCTGAGAAGGATGTGCAAACAGCTCTGGCTCTAGCAAAAGGA
AAGTTTGGCCGTGTGGATGTAGCTGTCAACTGTGCAGGCATCGCGGTGGCTAGCAAGACG
TACAACTTAAAGAAGGGCCAGACCCATACCTTGGAAGACTTCCAGCGAGTTCTTGATGTG
AATCTCATGGGCACCTTCAATGTGATCCGCCTGGTGGCTGGTGAGATGGGCCAGAATGAA
CCAGACCAGGGAGGCCAACGTGGGGTCATCATCAACACTGCCAGTGTGGCTGCCTTCGAG
GGTCAGGTTGGACAAGCTGCATACTCTGCTTCCAAGGGGGGAATAGTGGGCATGACACTG
CCCATTGCTCGGGATCTGGCTCCCATAGGTATCCGGGTGATGACCATTGCCCCAGGTCTG
TTTGGCACCCCACTGCTGACCAGCCTCCCAGAGAAAGTGTGCAACTTCTTGGCCAGCCAA
GTGCCCTTCCCTAGCCGACTGGGTGACCCTGCTGAGTATGCTCACCTCGTACAGGCCATC
ATCGAGAACCCATTCCTCAATGGAGAGGTCATCCGGCTGGATGGGGCCATTCGTATGCAG
CCTTGA
|
| Enzyme 3 GenBank Gene ID |
U96132  |
| Enzyme 3 GeneCard ID |
HSD17B10  |
| Enzyme 3 GenAtlas ID |
HSD17B10  |
| Enzyme 3 HGNC ID |
HGNC:4800  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Yan SD, Fu J, Soto C, Chen X, Zhu H, Al-Mohanna F, Collison K, Zhu A, Stern E, Saido T, Tohyama M, Ogawa S, Roher A, Stern D: An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. Nature. 1997 Oct 16;389(6652):689-95. [PubMed
]
- Miller AP, Willard HF: Chromosomal basis of X chromosome inactivation: identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8709-14. [PubMed
]
- He XY, Schulz H, Yang SY: A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease. J Biol Chem. 1998 Apr 24;273(17):10741-6. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [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
]
- Lenski C, Kooy RF, Reyniers E, Loessner D, Wanders RJ, Winnepenninckx B, Hellebrand H, Engert S, Schwartz CE, Meindl A, Ramser J: The reduced expression of the HADH2 protein causes X-linked mental retardation, choreoathetosis, and abnormal behavior. Am J Hum Genet. 2007 Feb;80(2):372-7. Epub 2006 Dec 28. [PubMed
]
- Froyen G, Corbett M, Vandewalle J, Jarvela I, Lawrence O, Meldrum C, Bauters M, Govaerts K, Vandeleur L, Van Esch H, Chelly J, Sanlaville D, van Bokhoven H, Ropers HH, Laumonnier F, Ranieri E, Schwartz CE, Abidi F, Tarpey PS, Futreal PA, Whibley A, Raymond FL, Stratton MR, Fryns JP, Scott R, Peippo M, Sipponen M, Partington M, Mowat D, Field M, Hackett A, Marynen P, Turner G, Gecz J: Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation. Am J Hum Genet. 2008 Feb;82(2):432-43. Epub 2008 Jan 24. [PubMed
]
- Holzmann J, Frank P, Loffler E, Bennett KL, Gerner C, Rossmanith W: RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell. 2008 Oct 31;135(3):462-74. [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
]
- Kissinger CR, Rejto PA, Pelletier LA, Thomson JA, Showalter RE, Abreo MA, Agree CS, Margosiak S, Meng JJ, Aust RM, Vanderpool D, Li B, Tempczyk-Russell A, Villafranca JE: Crystal structure of human ABAD/HSD10 with a bound inhibitor: implications for design of Alzheimer's disease therapeutics. J Mol Biol. 2004 Sep 17;342(3):943-52. [PubMed
]
- Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, Caspersen C, Chen X, Pollak S, Chaney M, Trinchese F, Liu S, Gunn-Moore F, Lue LF, Walker DG, Kuppusamy P, Zewier ZL, Arancio O, Stern D, Yan SS, Wu H: ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science. 2004 Apr 16;304(5669):448-52. [PubMed
]
- Ofman R, Ruiter JP, Feenstra M, Duran M, Poll-The BT, Zschocke J, Ensenauer R, Lehnert W, Sass JO, Sperl W, Wanders RJ: 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene. Am J Hum Genet. 2003 May;72(5):1300-7. Epub 2003 Apr 14. [PubMed
]
- Perez-Cerda C, Garcia-Villoria J, Ofman R, Sala PR, Merinero B, Ramos J, Garcia-Silva MT, Beseler B, Dalmau J, Wanders RJ, Ugarte M, Ribes A: 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease. Pediatr Res. 2005 Sep;58(3):488-91. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5618 |
| Enzyme 4 Name |
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial |
| Enzyme 4 Synonyms |
- HCDH
- Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
- Short-chain 3-hydroxyacyl-CoA dehydrogenase
|
| Enzyme 4 Gene Name |
HADH |
| Enzyme 4 Protein Sequence |
>Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
MAFVTRQFMRSVSSSSTASASAKKIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTE
DILAKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATSTDAASVVHSTDLVVEAI
VENLKVKNELFKRLDKFAAEHTIFASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKL
VEVIKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLLVPYLMEAIRLYERGDAS
KEDIDTAMKLGAGYPMGPFELLDYVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAEN
KFGKKTGEGFYKYK
|
| Enzyme 4 Number of Residues |
314 |
| Enzyme 4 Molecular Weight |
34277.2 |
| Enzyme 4 Theoretical pI |
9.41 |
| Enzyme 4 GO Classification |
| Function |
- 3-hydroxyacyl-CoA dehydrogenase activity
- NAD binding
- NAD or NADH binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in 3-hydroxyacyl-CoA dehydrogenase activity |
| Enzyme 4 Specific Function |
Plays an essential role in the mitochondrial beta- oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA |
| Enzyme 4 Pathways |
- Benzoate Degradation via CoA Ligation (map00632
)
- Butyrate Metabolism (map00650
)
- Caprolactam degradation (map00930
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Lysine Degradation (map00310
)
- Tryptophan Metabolism (map00380
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 4 Reactions |
- (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+ [RN:R01778]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
1483511  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q16836  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
HCDH_HUMAN  |
| Enzyme 4 PDB ID |
1F0Y  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>945 bp
ATGGCCTTCGTCACCAGGCAGTTCATGCGTTCCGTGTCCTCCTCGTCCACCGCCTCGGCC
TCGGCCAAGAAGATAATCGTCAAGCACGTGACGGTCATCGGCGGCGGGCTGATGGGCGCC
GGCATTGCCCAGGTTGCTGCAGCAACTGGTCACACAGTAGTGTTGGTAGACCAGACAGAG
GACATCCTGGCAAAATCCAAAAAGGGAATTGAGGAAAGCCTTAGGAAAGTGGCAAAGAAG
AAGTTTGCAGAAAACCCTAAGGCCGGCGATGAATTTGTGGAGAAGACCCTGAGCACCATA
GCGACCAGCACGGATGCAGCCTCCGTTGTCCACAGCACAGACTTGGTGGTGGAAGCCATC
GTGGAGAATCTGAAGGTGAAAAACGAGCTCTTCAAAAGGCTGGACAAGTTTGCTGCTGAA
CATACAATCTTTGCCAGCAACACTTCCTCCTTGCATATTACAAGCATAGCTAATGCCACC
ACCAGACAAGACCGATTCGCTGGCCTCCATTTCTTCAACCCAGTGCCTGTCATGAAACTT
GTGGAGGTCATTAAAACACCAATGACCAGCCAGAAGACATTTGAATCTTTGGTAGACTTT
AGCAAAGCCCTAGGAAAGCATCCTGTTTCTTGCAAGGACACTCCTGGGTTTATTGTGAAC
CGCCTCCTGGTTCCATACCTCATGGAAGCAATCAGGCTGTATGAACGAGGTGACGCATCC
AAAGAAGACATTGACACTGCTATGAAATTAGGAGCCGGTTACCCCATGGGCCCATTTGAG
CTTCTAGATTATGTCGGACTGGATACTACGAAGTTCATCGTGGATGGGTGGCATGAAATG
GATGCAGAGAACCCATTACATCAGCCCAGCCCATCCTTAAATAAGCTGGTAGCAGAGAAC
AAGTTCGGCAAGAAGACTGGAGAAGGATTTTACAAATACAAGTGA
|
| Enzyme 4 GenBank Gene ID |
X96752  |
| Enzyme 4 GeneCard ID |
HADH  |
| Enzyme 4 GenAtlas ID |
HADH  |
| Enzyme 4 HGNC ID |
HGNC:4799  |
| Enzyme 4 Chromosome Location |
4 |
| Enzyme 4 Locus |
4q22-q26 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Vredendaal PJ, van den Berg IE, Malingre HE, Stroobants AK, Olde Weghuis DE, Berger R: Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence. Biochem Biophys Res Commun. 1996 Jun 25;223(3):718-23. [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
]
- 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
]
- Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, Banaszak LJ: Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism. Biochemistry. 1999 May 4;38(18):5786-98. [PubMed
]
- Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ: Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J Biol Chem. 2000 Sep 1;275(35):27186-96. [PubMed
]
- Yang SY, He XY, Schulz H: 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease. FEBS J. 2005 Oct;272(19):4874-83. [PubMed
]
- Clayton PT, Eaton S, Aynsley-Green A, Edginton M, Hussain K, Krywawych S, Datta V, Malingre HE, Berger R, van den Berg IE: Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion. J Clin Invest. 2001 Aug;108(3):457-65. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5716 |
| Enzyme 5 Name |
Peroxisomal multifunctional enzyme type 2 |
| Enzyme 5 Synonyms |
- MFE-2
- 17-beta-hydroxysteroid dehydrogenase 4
- 17-beta-HSD 4
- D-bifunctional protein
- DBP
- 3-hydroxyacyl-CoA dehydrogenase
- 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
|
| Enzyme 5 Gene Name |
HSD17B4 |
| Enzyme 5 Protein Sequence |
>Peroxisomal multifunctional enzyme type 2
MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVE
EIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIH
RVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAI
EGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVG
AGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLS
KIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKD
LKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRA
GKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKV
AVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFS
ARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISN
AYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNI
GAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNI
MLSQKLQMILKDYAKL
|
| Enzyme 5 Number of Residues |
736 |
| Enzyme 5 Molecular Weight |
79685.7 |
| Enzyme 5 Theoretical pI |
9.21 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- oxidoreductase activity
- steroid binding
- sterol binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in oxidoreductase activity |
| Enzyme 5 Specific Function |
Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids |
| Enzyme 5 Pathways |
- Benzoate Degradation via CoA Ligation (map00632
)
- Butyrate Metabolism (map00650
)
- Caprolactam degradation (map00930
)
- Fatty Acid Elongation In Mitochondria (map00062
)
- Fatty Acid Metabolism (map00071
)
- Lysine Degradation (map00310
)
- Tryptophan Metabolism (map00380
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 5 Reactions |
- (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl- CoA = (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H2O [RN:R04813]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
1050517  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P51659  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
DHB4_HUMAN  |
| Enzyme 5 PDB ID |
1ZBQ  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2211 bp
ATGGGCTCACCGCTGAGGTTCGACGGGCGGGTGGTACTGGTCACCGGCGCGGGGGCAGGA
TTGGGCCGAGCCTATGCCCTGGCTTTTGCAGAAAGAGGAGCGTTAGTTGTTGTGAATGAT
TTGGGAGGGGACTTCAAAGGAGTTGGTAAAGGCTCCTTAGCTGCTGATAAGGTTGTTGAA
GAAATAAGAAGGAGAGGTGGAAAAGCAGTGGCCAACTATGATTCAGTGGAAGAAGGAGAG
AAGGTTGTGAAGACAGCCCTGGATGCTTTTGGAAGAATAGATGTTGTGGTCAACAATGCT
GGAATTCTGAGGGATCGTTCCTTTGCTAGGATAAGTGATGAAGACTGGGATATAATCCAC
AGAGTTCATTTGCGGGGTTCATTCCAAGTGACACGGGCAGCATGGGAACACATGAAGAAA
CAGAAGTATGGAAGGATTATTATGACTTCATCAGCTTCAGGAATATATGGCAACTTTGGC
CAGGCCAATTATAGTGCTGCAAAGTTGGGTCTTCTGGGCCTTGCAAATTCTCTTGCAATT
GAAGGCAGGAAAAGCAACATTCATTGTAACACCATTGCTCCTAATGCGGGATCACGGATG
ACTCAGACAGTTATGCCTGAAGATCTTGTGGAAGCCCTGAAGCCAGAGTATGTGGCACCT
CTTGTCCTTTGGCTTTGTCACGAGAGTTGTGAGGAGAATGGTGGCTTGTTTGAGGTTGGA
GCAGGATGGATTGGAAAATTACGCTGGGAGCGGACTCTTGGAGCTATTGTAAGACAAAAG
AATCACCCAATGACTCCTGAGGCAGTCAAGGCTAACTGGAAGAAGATCTGTGACTTTGAG
AATGCCAGCAAGCCTCAGAGTATCCAAGAATCAACTGGCAGTATAATTGAAGTTCTGAGT
AAAATAGATTCAGAAGGAGGAGTTTCAGCAAATCATACTAGTCGTGCAACGTCTACAGCA
ACATCAGGATTTGCTGGAGCTATTGGCCAGAAACTCCCTCCATTTTCTTATGCTTATACG
GAACTGGAAGCTATTATGTATGCCCTTGGAGTGGGAGCGTCAATCAAGGATCCAAAAGAT
TTGAAATTTATTTATGAAGGAAGTTCTGATTTCTCCTGTTTGCCCACCTTCGGAGTTATC
ATAGGTCAGAAATCTATGATGGGTGGAGGATTAGCAGAAATTCCTGGACTTTCAATCAAC
TTTGCAAAGGTTCTTCATGGAGAGCAGTACTTAGAGTTATATAAACCACTTCCCAGAGCA
GGAAAATTAAAATGTGAAGCAGTTGTTGCTGATGTCCTAGATAAAGGATCCGGTGTAGTG
ATTATTATGGATGTCTATTCTTATTCTGAGAAGGAACTTATATGCCACAATCAGTTCTCT
CTCTTTCTTGTTGGCTCTGGAGGCTTTGGTGGAAAACGGACATCAGACAAAGTCAAGGTA
GCTGTAGCCATACCTAATAGACCTCCTGATGCTGTACTTACAGATACCACCTCTCTTAAT
CAGGCTGCTTTGTACCGCCTCAGTGGAGACTGGAATCCCTTACACATTGATCCTAACTTT
GCTAGTCTAGCAGGTTTTGACAAGCCCATATTACATGGATTATGTACATTTGGATTTTCT
GCCAGGCGTGTGTTACAGCAGTTTGCAGATAATGATGTGTCAAGATTCAAGGCAATTAAG
GCTCGTTTTGCAAAACCAGTATATCCAGGACAAACTCTACAAACTGAGATGTGGAAGGAA
GGAAACAGAATTCATTTTCAAACCAAGGTCCAAGAAACTGGAGACATTGTCATTTCAAAT
GCATATGTGGATCTTGCACCAACATCTGGTACTTCAGCTAAGACACCCTCTGAGGGCGGG
AAGCTTCAGAGTACCTTTGTATTTGAGGAAATAGGACGCCGCCTAAAGGATATTGGGCCT
GAGGTGGTGAAGAAAGTAAATGCTGTATTTGAGTGGCATATAACCAAAGGCGGAAATATT
GGGGCTAAGTGGACTATTGACCTGAAAAGTGGTTCTGGAAAAGTGTACCAAGGCCCTGCA
AAAGGTGCTGCTGATACAACAATCATACTTTCAGATGAAGATTTCATGGAGGTGGTCCTG
GGCAAGCTTGACCCTCAGAAGGCATTCTTTAGTGGCAGGCTGAAGGCCAGAGGGAACATC
ATGCTGAGCCAGAAACTTCAGATGATTCTTAAAGACTACGCCAAGCTCTGA
|
| Enzyme 5 GenBank Gene ID |
X87176  |
| Enzyme 5 GeneCard ID |
HSD17B4  |
| Enzyme 5 GenAtlas ID |
HSD17B4  |
| Enzyme 5 HGNC ID |
HGNC:5213  |
| Enzyme 5 Chromosome Location |
5 |
| Enzyme 5 Locus |
5q21 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Adamski J, Normand T, Leenders F, Monte D, Begue A, Stehelin D, Jungblut PW, de Launoit Y: Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. Biochem J. 1995 Oct 15;311 ( Pt 2):437-43. [PubMed
]
- Jiang LL, Miyazawa S, Souri M, Hashimoto T: Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J Biochem (Tokyo). 1997 Feb;121(2):364-9. [PubMed
]
- Leenders F, Dolez V, Begue A, Moller G, Gloeckner JC, de Launoit Y, Adamski J: Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV. Mamm Genome. 1998 Dec;9(12):1036-41. [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
]
- Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T: Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J Biochem (Tokyo). 1996 Sep;120(3):624-32. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [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
]
- 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
]
- Haapalainen AM, van Aalten DM, Merilainen G, Jalonen JE, Pirila P, Wierenga RK, Hiltunen JK, Glumoff T: Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. J Mol Biol. 2001 Nov 9;313(5):1127-38. [PubMed
]
- Koski KM, Haapalainen AM, Hiltunen JK, Glumoff T: Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2. J Mol Biol. 2005 Feb 4;345(5):1157-69. Epub 2004 Dec 10. [PubMed
]
- van Grunsven EG, van Berkel E, Ijlst L, Vreken P, de Klerk JB, Adamski J, Lemonde H, Clayton PT, Cuebas DA, Wanders RJ: Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency. Proc Natl Acad Sci U S A. 1998 Mar 3;95(5):2128-33. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8815 |
| Enzyme 6 Name |
Hydroxyacyl-Coenzyme A dehydrogenase, type II |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
HADH2 |
| Enzyme 6 Protein Sequence |
>Hydroxyacyl-Coenzyme A dehydrogenase, type II
MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVF
APADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDV
NLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTL
PIARDLAPIGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGE
VIRLDGAIRMQP
|
| Enzyme 6 Number of Residues |
252 |
| Enzyme 6 Molecular Weight |
25984 |
| Enzyme 6 Theoretical pI |
7.29 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Lipid transport and metabolism |
| Enzyme 6 Specific Function |
Not Available |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
57210025  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q5H927  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q5H927_HUMAN  |
| Enzyme 6 PDB ID |
1SO8  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>759 bp
ATGGCAGCAGCGTGTCGGAGCGTGAAGGGCCTGGTGGCGGTAATAACCGGAGGAGCCTCG
GGCCTGGGCCTGGCCACGGCGGAGCGACTTGTGGGGCAGGGAGCCTCTGCTGTGCTTCTG
GACCTGCCCAACTCGGGTGGGGAGGCCCAAGCCAAGAAGTTAGGAAACAACTGCGTTTTC
GCCCCAGCCGACGTGACCTCTGAGAAGGATGTGCAAACAGCTCTGGCTCTAGCAAAAGGA
AAGTTTGGCCGTGTGGATGTAGCTGTCAACTGTGCAGGCATCGCGGTGGCTAGCAAGACG
TACAACTTAAAGAAGGGCCAGACCCATACCTTGGAAGACTTCCAGCGAGTTCTTGATGTG
AATCTCATGGGCACCTTCAATGTGATCCGCCTGGTGGCTGGTGAGATGGGCCAGAATGAA
CCAGACCAGGGAGGCCAACGTGGGGTCATCATCAACACTGCCAGTGTGGCTGCCTTCGAG
GGTCAGGTTGGACAAGCTGCATACTCTGCTTCCAAGGGGGGAATAGTGGGCATGACACTG
CCCATTGCTCGGGATCTGGCTCCCATAGGTCTGTTTGGCACCCCACTGCTGACCAGCCTC
CCAGAGAAAGTGTGCAACTTCTTGGCCAGCCAAGTGCCCTTCCCTAGCCGACTGGGTGAC
CCTGCTGAGTATGCTCACCTCGTACAGGCCATCATCGAGAACCCATTCCTCAATGGAGAG
GTCATCCGGCTGGATGGGGCCATTCGTATGCAGCCTTGA
|
| Enzyme 6 GenBank Gene ID |
Z97054  |
| Enzyme 6 GeneCard ID |
HADH2  |
| Enzyme 6 GenAtlas ID |
HADH2  |
| Enzyme 6 HGNC ID |
HGNC:4800  |
| Enzyme 6 Chromosome Location |
X |
| Enzyme 6 Locus |
Xp11.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
11020 |
| Enzyme 7 Name |
Enoyl-CoA hydratase, mitochondrial |
| Enzyme 7 Synonyms |
- Enoyl-CoA hydratase 1
- Short-chain enoyl-CoA hydratase
- SCEH
|
| Enzyme 7 Gene Name |
ECHS1 |
| Enzyme 7 Protein Sequence |
>Enoyl-CoA hydratase, mitochondrial
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNA
LCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHW
DHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLT
RAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMA
KESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
|
| Enzyme 7 Number of Residues |
290 |
| Enzyme 7 Molecular Weight |
31387.1 |
| Enzyme 7 Theoretical pI |
8.19 |
| Enzyme 7 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in catalytic activity |
| Enzyme 7 Specific Function |
Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O [RN:R02685 R07314]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
55664849  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P30084  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
ECHM_HUMAN  |
| Enzyme 7 PDB ID |
2DUB  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>873 bp
ATGGCCGCCCTGCGTGTCCTGCTGTCCTGCGTCCGCGGCCCGCTGAGGCCCCCGGTTCGC
TGTCCCGCCTGGCGTCCCTTCGCCTCGGGTGCTAACTTTGAGTACATCATCGCAGAAAAA
AGAGGGAAGAATAACACCGTGGGGTTGATCCAACTGAACCGCCCCAAGGCCCTCAATGCA
CTTTGCGATGGCCTGATTGACGAGCTCAACCAGGCCCTGAAGACCTTCGAGGAGGACCCG
GCCGTGGGGGCCATTGTCCTCACCGGCGGGGATAAGGCCTTTGCAGCTGGAGCTGATATC
AAGGAAATGCAGAACCTGAGTTTCCAGGACTGTTACTCCAGCAAGTTCTTGAAGCACTGG
GACCACCTCACCCAGGTCAAGAAGCCAGTCATCGCTGCTGTCAATGGCTATGCCTTTGGC
GGGGGCTGTGAGCTTGCCATGATGTGTGATATCATCTATGCCGGTGAGAAGGCCCAGTTT
GCACAGCCGGAGATCTTAATAGGAACCATCCCAGGTGCGGGCGGCACCCAGAGACTCACC
CGTGCTGTTGGGAAGTCGCTGGCGATGGAGATGGTCCTCACTGGTGACCGGATCTCAGCC
CAGGACGCCAAGCAAGCAGGTCTTGTCAGCAAGATTTGTCCTGTTGAGACACTGGTGGAA
GAAGCCATCCAGTGTGCAGAAAAAATTGCCAGCAATTCTAAAATTGTAGTAGCGATGGCC
AAAGAATCAGTGAATGCAGCTTTTGAAATGACATTAACAGAAGGAAGTAAGTTGGAGAAG
AAACTCTTTTATTCAACCTTTGCCACTGATGACCGGAAAGAAGGGATGACCGCGTTTGTG
GAAAAGAGAAAGGCCAACTTCAAAGACCAGTGA
|
| Enzyme 7 GenBank Gene ID |
AL360181  |
| Enzyme 7 GeneCard ID |
ECHS1  |
| Enzyme 7 GenAtlas ID |
ECHS1  |
| Enzyme 7 HGNC ID |
HGNC:3151  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
10q26.2-q26.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Kanazawa M, Ohtake A, Abe H, Yamamoto S, Satoh Y, Takayanagi M, Niimi H, Mori M, Hashimoto T: Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase. Enzyme Protein. 1993;47(1):9-13. [PubMed
]
- Janssen U, Davis EM, Le Beau MM, Stoffel W: Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3. Genomics. 1997 Mar 15;40(3):470-5. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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
]
- Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
15876 |
| Enzyme 8 Name |
ACAA1 protein |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
ACAA1 |
| Enzyme 8 Protein Sequence |
>ACAA1 protein
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
|
| Enzyme 8 Number of Residues |
331 |
| Enzyme 8 Molecular Weight |
34636.4 |
| Enzyme 8 Theoretical pI |
8.49 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
15680239  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q96CA6  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
Q96CA6_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>996 bp
ATGCAGAGGCTGCAGGTAGTGCTGGGCCACCTGAGGGGTCCGGCCGATTCCGGCTGGATG
CCGCAGGCCGCGCCTTGCCTGAGCGGTGCCCCGCAGGCCTCGGCCGCGGACGTGGTGGTG
GTGCACGGGCGGCGCACGGCCATCTGCCGGGCGGGCCGCGGCGGCTTCAAGGACACCACC
CCCGACGAGCTTCTCTCGGCAGTCATGACCGCGGTTCTCAAGGACGTGAATCTGAGGCCG
GAACAGCTGGGGGACATCTGTGTCGGAAATGTGCTGCAGCCTGGGGCCGGGGCAATCATG
GCCCGAATCGCCCAGTTTCTGAGTGACATCCCGGAGACTGTGCCTTTGTCCACTGTCAAT
AGACAGTGTTCGTCGGGGCTACAGGCAGTGGCCAGCATAGCAGGTGGCATCAGAAATGGG
TCTTATGACATTGGCATGGCCTGTGGGATAACCTCTGAGAATGTGGCTGAGCGGTTTGGC
ATTTCACGGGAGAAGCAGGATACCTTTGCCCTGGCTTCCCAGCAGAAGGCAGCAAGAGCC
CAGAGCAAGGGCTGTTTCCAAGCTGAGATTGTGCCTGTGACCACCACGGTCCATGATGAC
AAGGGCACCAAGAGGAGCATCACTGTGACCCAGGATGAGGGTATCCGCCCCAGCACCACC
ATGGAGGGCCTGGCCAAACTGAAGCCTGCCTTCAAGAAAGATGGTTCTACCACAGCTGGG
CTGACAGTGAGTGACGTGGACATCTTCGAGATCAATGAGGCCTTTGCAAGCCAGGCTGCC
TACTGTGTGGAGAAGCTACGACTCCCCCCTGAGAAGGTGAACCCCCTGGGGGGTGCAGTG
GCCTTAGGGCACCCACTGGGCTGCACTGGGGCACGACAGGCCATCACGCTGCTCAATGAG
CTGAAGCGCCGTGGGAAGAGGGCATACGGAGTGGTGTCCATGTGCATCGGGACTGGAATG
GGAGCCGCTGCCGTCTTTGAATACCCTGGGAACTGA
|
| Enzyme 8 GenBank Gene ID |
BC014474  |
| Enzyme 8 GeneCard ID |
ACAA1  |
| Enzyme 8 GenAtlas ID |
ACAA1  |
| Enzyme 8 HGNC ID |
HGNC:82  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3p23-p22 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
16712 |
| Enzyme 9 Name |
cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
Not Available |
| Enzyme 9 Protein Sequence |
>cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEANEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
|
| Enzyme 9 Number of Residues |
397 |
| Enzyme 9 Molecular Weight |
41895.8 |
| Enzyme 9 Theoretical pI |
8.21 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
193786127  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B3KNP8  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B3KNP8_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1194 bp
ATGGCTCTGCTCCGAGGTGTGTTTGTAGTTGCTGCTAAGCGAACGCCCTTTGGAGCTTAC
GGAGGCCTTCTGAAAGACTTCACTGCTACTGACTTGTCTGAATTTGCTGCCAAGGCTGCC
TTGTCTGCTGGCAAAGTCTCACCTGAAACAGTTGACAGTGTGATTATGGGCAATGTCCTG
CAGAGTTCTTCAGATGCTATATATTTGGCAAGGCATGTTGGTTTGCGTGTGGGAATCCCA
AAGGAGACCCCAGCTCTCACGATTAATAGGCTCTGTGGTTCTGGTTTTCAGTCCATTGTG
AATGGATGTCAGGAAATTTGTGTTAAAGAAGCTGAAGTTGTTTTATGTGGAGGAACCGAA
AGCATGAGCCAAGCTCCCTACTGTGTCAGAAATGTGCGTTTTGGAACCAAGCTTGGATCA
GATATCAAGCTGGAAGATTCTTTATGGGTATCATTAACAGATCAGCATGTCCAGCTCCCC
ATGGCAATGACTGCAGAGAATCTTGCTGTAAAACACAAAATAAGCAGAGAAGAATGTGAC
AAATATGCCCTGCAGTCACAGCAGAGATGGAAAGCTGCTAATGATGCTGGCTACTTTAAT
GATGAAATGGCACCAATTGAAGTGAAGACAAAGAAAGGAAAACAGACAATGCAGGTAGAC
GAGCATGCTCGGCCCCAAACCACCCTGGAACAGTTACAGAAACTTCCTCCAGTATTCAAG
AAAGATGGAACTGTTACTGCAGGGAATGCATCGGGTGTAGCTGATGGTGCTGGAGCTGTT
ATCATAGCTAGTGAAGATGCTGTTAAGAAACATAACTTCACACCACTGGCAAGAATTGTG
GGCTACTTTGTATCTGGATGTGATCCCTCTATCATGGGTATTGGTCCTGTCCCTGCTATC
AGTGGGGCACTGAAGAAAGCAGGACTGAGTCTTAAGGACATGGATTTGGTAGAGGCGAAT
GAAGCTTTTGCTCCCCAGTACTTGGCTGTTGAGAGGAGTTTGGATCTTGACATAAGTAAA
ACCAATGTGAATGGAGGAGCCATTGCTTTGGGTCACCCACTGGGAGGATCTGGATCAAGA
ATTACTGCACACCTGGTTCACGAATTAAGGCGTCGAGGTGGAAAATATGCCGTTGGATCA
GCTTGCATTGGAGGTGGCCAAGGTATTGCTGTCATCATTCAGAGCACAGCCTGA
|
| Enzyme 9 GenBank Gene ID |
AK054673  |
| Enzyme 9 GeneCard ID |
Not Available |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
HGNC:83  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
Not Available |
| Enzyme 9 General References |
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |