In enzymology, a cobalt-factor II C20-methyltransferase (EC 2.1.1.151) is an enzyme that catalyzes the chemical reaction
| cobalt-factor II C20-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.151 | ||||||||
| 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 + cobalt-factor II S-adenosyl-L-homocysteine + cobalt-factor III
The two substrates of this enzyme are S-adenosyl methionine and cobalt-factor II; its two products are S-adenosylhomocysteine and cobalt-factor III.
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:cobalt-factor-II C20-methyltransferase. This enzyme is also called CbiL. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium.
See also
editReferences
edit- Spencer P, Stolowich NJ, Sumner LW, Scott AI (1998). "Definition of the redox states of cobalt-precorrinoids: investigation of the substrate and redox specificity of CbiL from Salmonella typhimurium". Biochemistry. 37 (42): 14917–27. doi:10.1021/bi981366f. PMID 9778368.
