Precorrin-2 C20-methyltransferase
| 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 | ||||||||
| |||||||||
In enzymology, precorrin-2 C20-methyltransferase (EC 2.1.1.130) is an enzyme that catalyzes the chemical reaction
This methylation reaction converts precorrin-2 into precorrin-3A. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which gives S-adenosyl-L-homocysteine (SAH).[1][2]
The 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. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.[3]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2E0K and 2E0N.
References
- ^ Enzyme 2.1.1.130 at KEGG Pathway Database.
- ^ 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.
- ^ Battersby, Alan R. (2000). "Tetrapyrroles: The pigments of life: A Millennium review". Natural Product Reports. 17 (6): 507–526. doi:10.1039/B002635M. PMID 11152419.