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Uroporphyrinogen-III C-methyltransferase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Name | Uroporphyrinogen-III C-methyltransferase |
| EC_number | 2.1.1.107 |
| CAS_number | 125752-76-3 |
Uroporphyrinogen-III C-methyltransferase (), 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. This enzyme catalyses the following overall 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). These reactions are part of the biosynthetic pathway to cobalamin (vitamin B12) in both anaerobic and aerobic bacteria.
References
References
- (1990). "Uroporphyrinogen-III methylase catalyzes the enzymatic-synthesis of sirohydrochlorin-II and sirohydrochlorin-IV by a clockwise mechanism". J. Am. Chem. Soc..
- (February 1990). "The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase". The Biochemical Journal.
- (May 2002). "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase". The EMBO Journal.
- {{KEGG enzyme. 2.1.1.107
- (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports.
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