Precorrin-4 C11-methyltransferase
| 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 | ||||||||
| |||||||||
In enzymology, a precorrin-4 C11-methyltransferase (EC 2.1.1.133) is an enzyme that catalyzes the chemical reaction
- 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.
