Biology:Uroporphyrinogen-III C-methyltransferase
| Uroporphyrinogen-III C-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.107 | ||||||||
| CAS number | 125752-76-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Uroporphyrinogen-III C-methyltransferase (EC 2.1.1.107), uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase.[1][2][3] This enzyme catalyses the following overall chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme catalyses two methylation reactions. The first reaction converts uroporphyrinogen III into precorrin-1 and the second forms dihydrosirohydrochlorin (precorrin-2). In both cases the methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine (SAH).[4] These reactions are part of the biosynthetic pathway to cobalamin (vitamin B12) in both anaerobic and aerobic bacteria.[5]
See also
References
- ↑ "Uroporphyrinogen-III methylase catalyzes the enzymatic-synthesis of sirohydrochlorin-II and sirohydrochlorin-IV by a clockwise mechanism". J. Am. Chem. Soc. 112: 5343–5345. 1990. doi:10.1021/ja00169a048.
- ↑ "The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase". The Biochemical Journal 265 (3): 725–9. February 1990. doi:10.1042/bj2650725. PMID 2407234.
- ↑ "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase". The EMBO Journal 21 (9): 2068–75. May 2002. doi:10.1093/emboj/21.9.2068. PMID 11980703.
- ↑ Enzyme 2.1.1.107 at KEGG Pathway Database.
- ↑ Battersby, Alan R. (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports 17 (6): 507–526. doi:10.1039/b002635m. PMID 11152419.
External links
- Uroporphyrinogen-III+C-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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