Summary
In enzymology, a precorrin-4 C11-methyltransferase (EC 2.1.1.133) is an enzyme that catalyzes the chemical reaction
| precorrin-4 C11-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.133 | ||||||||
| 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 | ||||||||
| |||||||||
- S-adenosyl-L-methionine + precorrin-4 S-adenosyl-L-homocysteine + precorrin-5
The two substrates of this enzyme are S-adenosyl methionine and precorrin 4; its two products are S-adenosylhomocysteine and precorrin 5.
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 C11 methyltransferase. Other names in common use include precorrin-3 methylase, and CobM. It 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 1CBF and 2CBF.
References edit
- Thibaut D, Debussche L (1990). "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid". J. Bacteriol. 172 (10): 5980–90. doi:10.1128/jb.172.10.5980-5990.1990. PMC 526920. PMID 2211521.
- Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM (1993). "Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium". J. Bacteriol. 175 (11): 3303–16. doi:10.1128/jb.175.11.3303-3316.1993. PMC 204727. PMID 8501034.
