|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5483 |
| Enzyme 1 Name |
Coproporphyrinogen-III oxidase, mitochondrial |
| Enzyme 1 Synonyms |
- COX
- Coprogen oxidase
- Coproporphyrinogenase
|
| Enzyme 1 Gene Name |
CPOX |
| Enzyme 1 Protein Sequence |
>Coproporphyrinogen-III oxidase, mitochondrial
MALQLGRLSSGPCWLVARGGCGGPRAWSQCGGGGLRAWSQRSAAGRVCRPPGPAGTEQSR
GLGHGSTSRGGPWVGTGLAAALAGLVGLATAAFGHVQRAEMLPKTSGTRATSLGRPEEEE
DELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQAQVCQALAQVDGGANFSVDR
WERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAKQMRSRGKVLKTKDGKLPFCA
MGVSSVIHPKNPHAPTIHFNYRYFEVEEADGNKQWWFGGGCDLTPTYLNQEDAVHFHRTL
KEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFDDLDSPSKEEVFRFVQSCARA
VVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYDRGTKFGLFTPGSRIESILMS
LPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR
|
| Enzyme 1 Number of Residues |
454 |
| Enzyme 1 Molecular Weight |
50151.6 |
| Enzyme 1 Theoretical pI |
8.33 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- coproporphyrinogen oxidase activity
- 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
|
| Process |
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in coproporphyrinogen oxidase activity |
| Enzyme 1 Specific Function |
Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O [RN:R03220]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P36551  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HEM6_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1365 bp
ATGGCCTTGCAGCTGGGCAGGCTGAGCTCGGGCCCCTGCTGGCTCGTGGCGCGGGGCGGC
TGCGGAGGGCCCCGCGCCTGGTCCCAGTGCGGCGGCGGAGGGCTCCGAGCCTGGTCCCAG
CGCAGCGCAGCCGGACGCGTCTGCCGGCCCCCTGGCCCGGCTGGCACGGAGCAGAGCCGC
GGGCTGGGGCACGGCTCGACGTCGAGAGGCGGCCCCTGGGTGGGGACAGGGCTGGCCGCG
GCGCTGGCGGGGTTGGTGGGGCTGGCCACCGCCGCCTTCGGGCATGTGCAGCGGGCGGAG
ATGTTGCCTAAGACCTCGGGGACGCGGGCCACTTCGCTGGGGAGGCCGGAGGAGGAGGAG
GATGAGCTGGCCCACCGCTGCAGCAGCTTCATGGCCCCGCCTGTGACCGACCTGGGCGAG
CTGCGAAGGAGGCCGGGCGACATGAAGACCAAGATGGAGCTGCTGATTCTGGAGACCCAG
GCCCAGGTGTGCCAGGCTCTGGCACAGGTAGACGGGGGCGCCAACTTTTCTGTGGACCGG
TGGGAGAGGAAGGAAGGAGGTGGCGGCATCAGCTGTGTACTTCAAGATGGGTGTGTTTTC
GAAAAGGCTGGGGTGAGCATTTCTGTTGTTCATGGAAATCTTTCAGAGGAAGCTGCAAAA
CAAATGAGAAGCAGAGGAAAAGTTCTGAAGACTAAAGATGGTAAATTGCCATTTTGTGCT
ATGGGCGTGAGCTCTGTTATCCACCCCAAGAATCCTCATGCTCCTACTATCCATTTCAAC
TACAGATACTTTGAAGTAGAAGAAGCTGATGGCAACAAGCAGTGGTGGTTTGGTGGTGGA
TGTGACCTCACTCCAACATACTTGAATCAAGAAGACGCTGTCCATTTTCACAGAACTCTG
AAGGAGGCTTGTGACCAGCATGGTCCAGATCTCTACCCCAAATTTAAAAAATGGTGTGAT
GATTACTTCTTTATAGCCCATCGTGGAGAACGGCGGGGCATTGGTGGTATCTTTTTTGAT
GATCTTGACTCTCCGTCCAAGGAGGAGGTGTTTCGCTTTGTACAGAGCTGTGCCAGGGCT
GTAGTTCCTTCTTACATTCCCCTTGTGAAAAAGCACTGTGATGACTCATTCACCCCCCAG
GAGAAGCTGTGGCAGCAGCTCAGAAGAGGACGGTATGTAGAATTTAATCTGCTGTATGAT
CGGGGCACAAAGTTTGGCCTCTTCACTCCAGGATCCAGAATTGAAAGTATCTTGATGTCT
TTACCTCTAACTGCCCGATGGGAGTACATGCATTCACCCTCAGAGAATTCCAAAGAAGCT
GAAATTCTGGAAGTTCTACGCCATCCAAGGGACTGGGTGCGTTGA
|
| Enzyme 1 GenBank Gene ID |
AK290140  |
| Enzyme 1 GeneCard ID |
CPOX  |
| Enzyme 1 GenAtlas ID |
CPOX  |
| Enzyme 1 HGNC ID |
HGNC:2321  |
| Enzyme 1 Chromosome Location |
3 |
| Enzyme 1 Locus |
3q12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Delfau-Larue MH, Martasek P, Grandchamp B: Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. Hum Mol Genet. 1994 Aug;3(8):1325-30. [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
]
- Taketani S, Kohno H, Furukawa T, Yoshinaga T, Tokunaga R: Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase. Biochim Biophys Acta. 1994 Jan 4;1183(3):547-9. [PubMed
]
- Martasek P, Camadro JM, Delfau-Larue MH, Dumas JB, Montagne JJ, de Verneuil H, Labbe P, Grandchamp B: Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3024-8. [PubMed
]
- Susa S, Daimon M, Ono H, Li S, Yoshida T, Kato T: The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria. Tohoku J Exp Med. 2003 May;200(1):39-45. [PubMed
]
- Lee DS, Flachsova E, Bodnarova M, Demeler B, Martasek P, Raman CS: Structural basis of hereditary coproporphyria. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14232-7. Epub 2005 Sep 21. [PubMed
]
- Martasek P, Nordmann Y, Grandchamp B: Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms. Hum Mol Genet. 1994 Mar;3(3):477-80. [PubMed
]
- Fujita H, Kondo M, Taketani S, Nomura N, Furuyama K, Akagi R, Nagai T, Terajima M, Galbraith RA, Sassa S: Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria. Hum Mol Genet. 1994 Oct;3(10):1807-10. [PubMed
]
- Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y: A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria. Hum Mol Genet. 1995 Feb;4(2):275-8. [PubMed
]
- Daimon M, Gojyou E, Sugawara M, Yamatani K, Tominaga M, Sasaki H: A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria. Hum Genet. 1997 Feb;99(2):199-201. [PubMed
]
- Lamoril J, Deybach JC, Puy H, Grandchamp B, Nordmann Y: Three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;9(1):78-80. [PubMed
]
- Schreiber WE, Zhang X, Senz J, Jamani A: Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;10(3):196-200. [PubMed
]
- Rosipal R, Lamoril J, Puy H, Da Silva V, Gouya L, De Rooij FW, Te Velde K, Nordmann Y, Martasek P, Deybach JC: Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update. Hum Mutat. 1999;13(1):44-53. [PubMed
]
- Wiman A, Floderus Y, Harper P: Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria. J Hum Genet. 2002;47(8):407-12. [PubMed
]
- To-Figueras J, Badenas C, Enriquez MT, Segura S, Alvarez C, Mila M, Lecha M, Herrero C: Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain. Mol Genet Metab. 2005 Jun;85(2):160-3. Epub 2005 Feb 25. [PubMed
]
- Akagi R, Inoue R, Muranaka S, Tahara T, Taketani S, Anderson KE, Phillips JD, Sassa S: Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient. Br J Haematol. 2006 Jan;132(2):237-43. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6309 |
| Enzyme 2 Name |
Protoporphyrinogen oxidase |
| Enzyme 2 Synonyms |
- PPO
|
| Enzyme 2 Gene Name |
PPOX |
| Enzyme 2 Protein Sequence |
>Protoporphyrinogen oxidase
MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG
IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP
PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI
RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL
ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA
PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP
PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP
QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS
|
| Enzyme 2 Number of Residues |
477 |
| Enzyme 2 Molecular Weight |
50764.8 |
| Enzyme 2 Theoretical pI |
8.24 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- 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
- oxygen-dependent protoporphyrinogen oxidase activity
|
| Process |
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- protoporphyrinogen IX + 3 O2 = protoporphyrin IX + 3 H2O2 [RN:R03222]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
55665937  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P50336  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PPOX_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1434 bp
ATGGGCCGGACCGTGGTCGTGCTGGGCGGAGGCATCAGCGGCTTGGCCGCCAGTTACCAC
CTGAGCCGGGCCCCCTGCCCCCCTAAGGTGGTCCTAGTGGAGAGCAGTGAGCGTCTGGGA
GGCTGGATTCGCTCCGTTCGAGGCCCTAATGGTGCTATCTTTGAGCTTGGACCTCGGGGA
ATTAGGCCAGCGGGAGCCCTAGGGGCCCGGACCTTGCTCCTGGTTTCTGAGCTTGGCTTG
GATTCAGAAGTGCTGCCTGTCCGGGGAGACCACCCAGCTGCCCAGAACAGGTTCCTCTAC
GTGGGCGGTGCCCTGCATGCCCTACCCACTGGCCTCAGGGGGCTACTCCGCCCTTCACCC
CCCTTCTCCAAACCTCTGTTTTGGGCTGGGCTGAGGGAGCTGACCAAGCCCCGGGGCAAA
GAGCCTGATGAGACTGTGCACAGTTTTGCCCAGCGCCGCCTTGGACCTGAGGTGGCGTCT
CTAGCCATGGACAGTCTCTGCCGTGGAGTGTTTGCAGGCAACAGCCGTGAGCTCAGCATC
AGGTCCTGCTTTCCCAGTCTCTTCCAAGCTGAGCAAACCCATCGTTCCATATTACTGGGC
CTGCTGCTGGGGGCAGGGCGGACCCCACAGCCAGACTCAGCACTCATTCGCCAGGCCTTG
GCTGAGCGCTGGAGCCAGTGGTCACTTCGTGGAGGTCTAGAGATGTTGCCTCAGGCCCTT
GAAACCCACCTGACTAGTAGGGGGGTCAGTGTTCTCAGAGGCCAGCCGGTCTGTGGGCTC
AGCCTCCAGGCAGAAGGGCGCTGGAAGGTATCTCTAAGGGACAGCAGTCTGGAGGCTGAC
CACGTTATTAGTGCCATTCCAGCTTCAGTGCTCAGTGAGCTGCTCCCTGCTGAGGCTGCC
CCTCTGGCTCGTGCCCTGAGTGCCATCACTGCAGTGTCTGTAGCTGTGGTGAATCTGCAG
TACCAAGGAGCCCATCTGCCTGTCCAGGGATTTGGACATTTGGTGCCATCTTCAGAAGAT
CCAGGAGTCCTGGGAATCGTGTATGACTCAGTTGCTTTCCCTGAGCAGGACGGGAGCCCC
CCTGGCCTCAGAGTGACTGTGATGCTGGGAGGTTCCTGGTTACAGACACTGGAGGCTAGT
GGCTGTGTCTTATCTCAGGAGCTGTTTCAACAGCGGGCCCAGGAAGCAGCTGCTACACAA
TTAGGACTGAAGGAGATGCCGAGCCACTGCTTGGTCCATCTACACAAGAACTGCATTCCC
CAGTATACACTAGGTCACTGGCAAAAACTAGAGTCAGCTAGGCAATTCCTGACTGCTCAC
AGGTTGCCCCTGACTCTGGCTGGAGCCTCCTATGAGGGAGTTGCTGTTAATGACTGTATA
GAGAGTGGGCGCCAGGCAGCAGTCAGTGTCCTGGGCACAGAACCTAACAGCTGA
|
| Enzyme 2 GenBank Gene ID |
AL590714  |
| Enzyme 2 GeneCard ID |
PPOX  |
| Enzyme 2 GenAtlas ID |
PPOX  |
| Enzyme 2 HGNC ID |
HGNC:9280  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1q22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Nishimura K, Taketani S, Inokuchi H: Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli. J Biol Chem. 1995 Apr 7;270(14):8076-80. [PubMed
]
- Dailey TA, Dailey HA: Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme. Protein Sci. 1996 Jan;5(1):98-105. [PubMed
]
- Puy H, Robreau AM, Rosipal R, Nordmann Y, Deybach JC: Protoporphyrinogen oxidase: complete genomic sequence and polymorphisms in the human gene. Biochem Biophys Res Commun. 1996 Sep 4;226(1):226-30. [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
]
- Deybach JC, Puy H, Robreau AM, Lamoril J, Da Silva V, Grandchamp B, Nordmann Y: Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. Hum Mol Genet. 1996 Mar;5(3):407-10. [PubMed
]
- Meissner PN, Dailey TA, Hift RJ, Ziman M, Corrigall AV, Roberts AG, Meissner DM, Kirsch RE, Dailey HA: A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. Nat Genet. 1996 May;13(1):95-7. [PubMed
]
- Frank J, Poh-Fitzpatrick MB, King LE Jr, Christiano AM: The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. Arch Dermatol Res. 1998 Aug;290(8):441-5. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6347 |
| Enzyme 3 Name |
Ferrochelatase, mitochondrial |
| Enzyme 3 Synonyms |
- Heme synthase
- Protoheme ferro-lyase
|
| Enzyme 3 Gene Name |
FECH |
| Enzyme 3 Protein Sequence |
>Ferrochelatase, mitochondrial
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLV
WQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKEC
GVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTS
QQL
|
| Enzyme 3 Number of Residues |
423 |
| Enzyme 3 Molecular Weight |
47861.8 |
| Enzyme 3 Theoretical pI |
8.91 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- ferrochelatase activity
- lyase activity
|
| Process |
- heme biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in ferrochelatase activity |
| Enzyme 3 Specific Function |
Catalyzes the ferrous insertion into protoporphyrin IX |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
60499021  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22830  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
HEMH_HUMAN  |
| Enzyme 3 PDB ID |
1HRK  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1272 bp
ATGCGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAA
ACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACA
CTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAA
GAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGA
GAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTAT
ATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGAT
GGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGC
AGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAG
TGGAGCACTATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCAT
ATTCTAAAGGAACTGGACCATTTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTT
TCTGCTCACTCACTGCCCATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTA
AGCGCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTG
TGGCAATCCAAGGTTGGTCCAATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAA
GGGCTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGAC
CATATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGT
GGAGTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCC
CTGGCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACC
CTGAGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGC
CAGCAGCTGTGA
|
| Enzyme 3 GenBank Gene ID |
NM_000140.3  |
| Enzyme 3 GeneCard ID |
FECH  |
| Enzyme 3 GenAtlas ID |
FECH  |
| Enzyme 3 HGNC ID |
HGNC:3647  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
18q21.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Nakahashi Y, Taketani S, Okuda M, Inoue K, Tokunaga R: Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase. Biochem Biophys Res Commun. 1990 Dec 14;173(2):748-55. [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
]
- Tugores A, Magness ST, Brenner DA: A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene. J Biol Chem. 1994 Dec 9;269(49):30789-97. [PubMed
]
- Dailey HA, Sellers VM, Dailey TA: Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases. J Biol Chem. 1994 Jan 7;269(1):390-5. [PubMed
]
- Crouse BR, Sellers VM, Finnegan MG, Dailey HA, Johnson MK: Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster. Biochemistry. 1996 Dec 17;35(50):16222-9. [PubMed
]
- Sellers VM, Wang KF, Johnson MK, Dailey HA: Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster. J Biol Chem. 1998 Aug 28;273(35):22311-6. [PubMed
]
- Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC: The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol. 2001 Feb;8(2):156-60. [PubMed
]
- Cox TM: Erythropoietic protoporphyria. J Inherit Metab Dis. 1997 Jun;20(2):258-69. [PubMed
]
- Lamoril J, Boulechfar S, de Verneuil H, Grandchamp B, Nordmann Y, Deybach JC: Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene. Biochem Biophys Res Commun. 1991 Dec 16;181(2):594-9. [PubMed
]
- Brenner DA, Didier JM, Frasier F, Christensen SR, Evans GA, Dailey HA: A molecular defect in human protoporphyria. Am J Hum Genet. 1992 Jun;50(6):1203-10. [PubMed
]
- Sarkany RP, Alexander GJ, Cox TM: Recessive inheritance of erythropoietic protoporphyria with liver failure. Lancet. 1994 Jun 4;343(8910):1394-6. [PubMed
]
- Imoto S, Tanizawa Y, Sato Y, Kaku K, Oka Y: A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria. Br J Haematol. 1996 Jul;94(1):191-7. [PubMed
]
- Rufenacht UB, Gouya L, Schneider-Yin X, Puy H, Schafer BW, Aquaron R, Nordmann Y, Minder EI, Deybach JC: Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria. Am J Hum Genet. 1998 Jun;62(6):1341-52. [PubMed
]
- Gouya L, Schneider-Yin X, Rufenacht U, Herrero C, Lecha M, Mascaro JM, Puy H, Deybach JC, Minder EI: Mutations in the ferrochelatase gene of four Spanish patients with erythropoietic protoporphyria. J Invest Dermatol. 1998 Sep;111(3):406-9. [PubMed
]
- Schneider-Yin X, Gouya L, Dorsey M, Rufenacht U, Deybach JC, Ferreira GC: Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria. Blood. 2000 Aug 15;96(4):1545-9. [PubMed
]
- Rufenacht UB, Gregor A, Gouya L, Tarczynska-Nosal S, Schneider-Yin X, Deybach JC: New missense mutation in the human ferrochelatase gene in a family with erythropoietic protoporphyria: functional studies and correlation of genotype and phenotype. Clin Chem. 2001 Jun;47(6):1112-3. [PubMed
]
- Poh-Fitzpatrick MB, Wang X, Anderson KE, Bloomer JR, Bolwell B, Lichtin AE: Erythropoietic protoporphyria: altered phenotype after bone marrow transplantation for myelogenous leukemia in a patient heteroallelic for ferrochelatase gene mutations. J Am Acad Dermatol. 2002 Jun;46(6):861-6. [PubMed
]
- Wiman A, Floderus Y, Harper P: Novel mutations and phenotypic effect of the splice site modulator IVS3-48C in nine Swedish families with erythropoietic protoporphyria. J Hum Genet. 2003;48(2):70-6. [PubMed
]
- Whatley SD, Mason NG, Khan M, Zamiri M, Badminton MN, Missaoui WN, Dailey TA, Dailey HA, Douglas WS, Wainwright NJ, Elder GH: Autosomal recessive erythropoietic protoporphyria in the United Kingdom: prevalence and relationship to liver disease. J Med Genet. 2004 Aug;41(8):e105. [PubMed
]
- Aurizi C, Schneider-Yin X, Sorge F, Macri A, Minder EI, Biolcati G: Heterogeneity of mutations in the ferrochelatase gene in Italian patients with erythropoietic protoporphyria. Mol Genet Metab. 2007 Apr;90(4):402-7. Epub 2006 Dec 29. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13086 |
| Enzyme 4 Name |
cDNA FLJ76483, highly similar to Homo sapiens ferrochelatase |
| Enzyme 4 Synonyms |
- protoporphyria
- FECH, mRNA
- Ferrochelatase
- Protoporphyria, isoform CRA_a
|
| Enzyme 4 Gene Name |
FECH |
| Enzyme 4 Protein Sequence |
>cDNA FLJ76483, highly similar to Homo sapiens ferrochelatase
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLV
WQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKEC
GVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTS
QQL
|
| Enzyme 4 Number of Residues |
423 |
| Enzyme 4 Molecular Weight |
47863 |
| Enzyme 4 Theoretical pI |
8.91 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Coenzyme transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158259335  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8KA72  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8KA72_HUMAN  |
| Enzyme 4 PDB ID |
1HRK  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK292937  |
| Enzyme 4 GeneCard ID |
A8KA72  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
14933 |
| Enzyme 5 Name |
Ferrochelatase |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
Not Available |
| Enzyme 5 Protein Sequence |
>Ferrochelatase
LGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQ
KRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPEIQEQY
RRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLE
RAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILK
ELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQS
KVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVE
NIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
|
| Enzyme 5 Number of Residues |
420 |
| Enzyme 5 Molecular Weight |
47488.3 |
| Enzyme 5 Theoretical pI |
8.53 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- ferrochelatase activity
- lyase activity
|
| Process |
- heme biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in ferrochelatase activity |
| Enzyme 5 Specific Function |
Catalyzes the ferrous insertion into protoporphyrin IX |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
62897941  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q53FU1  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q53FU1_HUMAN  |
| Enzyme 5 PDB ID |
1HRK  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1263 bp
CTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGCGATCCGCTG
GCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCAGCTGCAGCG
GCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTTCAACCGCAG
AAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAAACTCTTGGA
GATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACACTTCCTATT
CAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCGAGATTCAAGAGCAGTAC
CGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGAGAGGGCATG
GTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTATATTGGATTT
CGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGATGGCCTAGAA
AGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGCAGCAGCTTA
AATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAGTGGAGCACT
ATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCATATTCTAAAG
GAACTGGACCATTTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTTTCTGCTCAC
TCACTGCCCATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGCGCCACT
GTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGGCAATCC
AAGGTTGGTCCAATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGGCTTTGT
GAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCATATTGAA
ACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGAGTTGAA
AACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTGGCCGAC
TTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTGAGCTGT
CCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAGCAGCTG
TGA
|
| Enzyme 5 GenBank Gene ID |
AK223190  |
| Enzyme 5 GeneCard ID |
Not Available |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
HGNC:3647  |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
Not Available |
| Enzyme 5 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
14936 |
| Enzyme 6 Name |
Ferrochelatase |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
Not Available |
| Enzyme 6 Protein Sequence |
>Ferrochelatase
MCSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQ
EQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERD
GLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADH
ILKELDHFPLERSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVW
QSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECG
VENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQ
QL
|
| Enzyme 6 Number of Residues |
422 |
| Enzyme 6 Molecular Weight |
47680.5 |
| Enzyme 6 Theoretical pI |
8.59 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- ferrochelatase activity
- lyase activity
|
| Process |
- heme biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in ferrochelatase activity |
| Enzyme 6 Specific Function |
Catalyzes the ferrous insertion into protoporphyrin IX |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
54696780  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q5TZY0  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
Q5TZY0_HUMAN  |
| Enzyme 6 PDB ID |
1HRK  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1269 bp
ATGTGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGAAGCCGAAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAA
ACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACA
CTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAA
GAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGA
GAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACAGCCCCTCACAAATACTAT
ATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGAT
GGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGC
AGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAG
TGGAGCACTATTGACAGGTGGCCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCAT
ATTCTAAAGGAACTGGACCATTTTCCACTTGAGAGAAGCGAGGTGGTCATTCTGTTTTCT
GCTCACTCACTGCCGATGTCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGC
GCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGG
CAATCCAAGGTTGGTCCGATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGG
CTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCAT
ATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGA
GTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTG
GCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTG
AGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAG
CAGCTGTAG
|
| Enzyme 6 GenBank Gene ID |
BT019959  |
| Enzyme 6 GeneCard ID |
Not Available |
| Enzyme 6 GenAtlas ID |
Not Available |
| Enzyme 6 HGNC ID |
HGNC:3647  |
| Enzyme 6 Chromosome Location |
Not Available |
| Enzyme 6 Locus |
Not Available |
| Enzyme 6 SNPs |
Not Available |
| Enzyme 6 General References |
Not Available |
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
14937 |
| Enzyme 7 Name |
Ferrochelatase |
| Enzyme 7 Synonyms |
Not Available |
| Enzyme 7 Gene Name |
DKFZp686P18130 |
| Enzyme 7 Protein Sequence |
>Ferrochelatase
MAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQKRKP
KTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIG
GGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIA
FTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDH
FPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGP
MPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRR
AESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL
|
| Enzyme 7 Number of Residues |
416 |
| Enzyme 7 Molecular Weight |
47131.9 |
| Enzyme 7 Theoretical pI |
8.78 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- ferrochelatase activity
- lyase activity
|
| Process |
- heme biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in ferrochelatase activity |
| Enzyme 7 Specific Function |
Catalyzes the ferrous insertion into protoporphyrin IX |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
33096717  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q7KZA3  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
Q7KZA3_HUMAN  |
| Enzyme 7 PDB ID |
1HRK  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1251 bp
ATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGCGATCCGCTGGCATCCAGCAGC
TGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCAGCTGCAGCGGCCGTCACCACA
GAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTTCAACCGCAGAAGAGGAAGCCG
AAAACTGGAATATTAATGCTAAACATGGGAGGCCCTGAAACTCTTGGAGATGTTCACGAC
TTCCTTCTGAGACTCTTCTTGGACCGAGACCTCATGACACTTCCTATTCAGAATAAGCTG
GCACCATTCATCGCCAAACGCCGAACCCCCAAGATTCAAGAGCAGTACCGCAGGATTGGA
GGCGGATCCCCCATCAAGATATGGACTTCCAAGCAGGGAGAGGGCATGGTAAAGCTGCTG
GATGAATTGTCCCCCAACACAGCCCCTCACAAATACTATATTGGATTTCGGTACGTCCAT
CCTTTAACAGAAGAAGCAATTGAAGAGATGGAGAGAGATGGCCTAGAAAGGGCTATTGCT
TTCACACAGTATCCACAGTACAGCTGCTCCACCACAGGCAGCAGCTTAAATGCCATTTAC
AGATACTATAATCAAGTGGGACGGAAGCCCACGATGAAGTGGAGCACTATTGACAGGTGG
CCCACACATCACCTCCTCATCCAGTGCTTTGCAGATCATATTCTAAAGGAACTGGACCAT
TTTCCACTTGAGAAGAGAAGCGAGGTGGTCATTCTGTTTTCTGCTCACTCACTGCCGATG
TCTGTGGTCAACAGAGGCGACCCATATCCTCAGGAGGTAAGCGCCACTGTCCAAAAAGTC
ATGGAAAGGCTGGAGTACTGCAACCCCTACCGACTGGTGTGGCAATCCAAGGTTGGTCCG
ATGCCCTGGTTGGGTCCTCAAACAGACGAATCTATCAAAGGGCTTTGTGAGAGGGGGAGG
AAGAATATCCTCTTGGTTCCGATAGCATTTACCAGTGACCATATTGAAACGCTGTATGAG
CTGGACATCGAGTACTCTCAAGTTTTAGCCAAGGAGTGTGGAGTTGAAAACATCAGAAGA
GCTGAGTCTCTTAATGGAAATCCATTGTTCTCTAAGGCCCTGGCCGACTTGGTGCATTCA
CACATCCAGTCAAACGAGCTGTGTTCCAAGCAGCTGACCCTGAGCTGTCCGCTCTGTGTC
AATCCTGTCTGCAGGGAGACTAAATCCTTCTTCACCAGCCAGCAGCTGTGA
|
| Enzyme 7 GenBank Gene ID |
BX571744  |
| Enzyme 7 GeneCard ID |
DKFZp686P18130  |
| Enzyme 7 GenAtlas ID |
DKFZp686P18130  |
| Enzyme 7 HGNC ID |
HGNC:3647  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
14938 |
| Enzyme 8 Name |
Ferrochelatase |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
Not Available |
| Enzyme 8 Protein Sequence |
>Ferrochelatase
MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQV
QPQKRYESNIRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKR
RTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAI
EEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWSTHHLLI
QCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYC
NPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQ
VLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRET
KSFFTSQQL
|
| Enzyme 8 Number of Residues |
429 |
| Enzyme 8 Molecular Weight |
48614.5 |
| Enzyme 8 Theoretical pI |
8.90 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- ferrochelatase activity
- lyase activity
|
| Process |
- heme biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in ferrochelatase activity |
| Enzyme 8 Specific Function |
Catalyzes the ferrous insertion into protoporphyrin IX |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
- protoheme + 2 H+ = protoporphyrin + Fe2+ [RN:R00310]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
21751005  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q8NAN0  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
Q8NAN0_HUMAN  |
| Enzyme 8 PDB ID |
1HRK  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1290 bp
ATGCGTTCACTCGGCGCAAACATGGCTGCGGCCCTGCGCGCCGCGGGCGTCCTGCTCCGC
GATCCGCTGGCATCCAGCAGCTGGAGGGTCTGTCAGCCATGGAGGTGGAAGTCAGGTGCA
GCTGCAGCGGCCGTCACCACAGAAACAGCCCAGCATGCCCAGGGTGCAAAACCTCAAGTT
CAACCGCAGAAGAGGTATGAGTCTAACATCAGGAAGCCGAAAACTGGAATATTAATGCTA
AACATGGGAGGCCCTGAAACTCTTGGAGATGTTCACGACTTCCTTCTGAGACTCTTCTTG
GACCGAGACCTCATGACACTTCCTATTCAGAATAAGCTGGCACCATTCATCGCCAAACGC
CGAACCCCCAAGATTCAAGAGCAGTACCGCAGGATTGGAGGCGGATCCCCCATCAAGATA
TGGACTTCCAAGCAGGGAGAGGGCATGGTGAAGCTGCTGGATGAATTGTCCCCCAACACA
GCCCCTCACAAATACTATATTGGATTTCGGTACGTCCATCCTTTAACAGAAGAAGCAATT
GAAGAGATGGAGAGAGATGGCCTAGAAAGGGCTATTGCTTTCACACAGTATCCACAGTAC
AGCTGCTCCACCACAGGCAGCAGCTTAAATGCCATTTACAGATACTATAATCAAGTGGGA
CGGAAGCCCACGATGAAGTGGAGCACTATTGACAGGTGGTCCACACATCACCTCCTCATC
CAGTGCTTTGCAGATCATATTCTAAAGGAACTGGACCATTTTCCACTTGAGAAGAGAAGC
GAGGTGGTCATTCTGTTTTCTGCTCACTCACTGCCCATGTCTGTGGTCAACAGAGGCGAC
CCATATCCTCAGGAGGTAAGCGCCACTGTCCAAAAAGTCATGGAAAGGCTGGAGTACTGC
AACCCCTACCGACTGGTGTGGCAATCCAAGGTTGGTCCGATGCCCTGGTTGGGTCCTCAA
ACAGACGAATCTATCAAAGGGCTTTGTGAGAGGGGGAGGAAGAATATCCTCTTGGTTCCG
ATAGCATTTACCAGTGACCATATTGAAACGCTGTATGAGCTGGACATCGAGTACTCTCAA
GTTTTAGCCAAGGAGTGTGGAGTTGAAAACATCAGAAGAGCTGAGTCTCTTAATGGAAAT
CCATTGTTCTCTAAGGCCCTGGCCGACTTGGTGCATTCACACATCCAGTCAAACGAGCTG
TGTTCCAAGCAGCTGACCCTGAGCTGTCCGCTCTGTGTCAATCCTGTCTGCAGGGAGACT
AAATCCTTCTTCACCAGCCAGCAGCTGTGA
|
| Enzyme 8 GenBank Gene ID |
AK092416  |
| Enzyme 8 GeneCard ID |
Not Available |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
HGNC:3647  |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
Not Available |
| Enzyme 8 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 8 Metabolite References |
Not Available |