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Precorrin-2 C20-methyltransferase 
Summary
In enzymology, a precorrin-2 C20-methyltransferase (EC 2.1.1.130) is an enzyme that catalyzes the chemical reaction
| precorrin-2 C20-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.130 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- S-adenosyl-L-methionine + precorrin-2 S-adenosyl-L-homocysteine + precorrin-3A
The two substrates of this enzyme are S-adenosyl methionine and precorrin 2 and its two products are S-adenosylhomocysteine and precorrin 3A.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:precorrin-4 C20-methyltransferase and another names in common use is CobI. The enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also edit
Structural studies edit
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E0K and 2E0N.
References edit
- Stolowich NJ, Iida K, Scott AI (1992). "Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis. Identification of the 11-methyl and 20-methyl transferases of corrin biosynthesis". FEBS Lett. 301 (1): 73–8. doi:10.1016/0014-5793(92)80213-Z. PMID 1451790. S2CID 20198692.
- Anousis N, Stolowich NJ, Holderman MT, Scott AI (1995). "Overexpression in Escherichia coli of 12 vitamin B12 biosynthetic enzymes". Protein Expr. Purif. 6 (2): 155–63. doi:10.1006/prep.1995.1019. PMID 7606163.
- Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F (1993). "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". J. Bacteriol. 175 (22): 7430–40. doi:10.1128/jb.175.22.7430-7440.1993. PMC 206888. PMID 8226690.
