Biology:Cobalt-factor II C20-methyltransferase
| Cobalt-factor II C20-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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Cobalt-factor II C20-methyltransferase (EC 2.1.1.151) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
This is a methylation reaction in which cobalt-precorrin-2 is converted to cobalt-precorrin-2. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Salmonella typhimurium.[1][2]
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.[3] This enzyme is also called CbiL. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium.[4][5][6]
See also
- Cobalamin biosynthesis
- Precorrin-2 C20-methyltransferase for enzyme that gives the same reaction in aerobic organisms
References
- ↑ "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. 1998. doi:10.1021/bi981366f. PMID 9778368.
- ↑ 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.
- ↑ Enzyme 2.1.1.151 at KEGG Pathway Database.
- ↑ Roessner, Charles A.; Santander, Patricio J.; Scott, A.Ian (2001). "Multiple biosynthetic pathways for vitamin B12: Variations on a central theme". Cofactor Biosynthesis. Vitamins & Hormones. 61. pp. 267–297. doi:10.1016/s0083-6729(01)61009-4. ISBN 9780127098616.
- ↑ "Isolation and characterization of 14 additional genes specifying the anaerobic biosynthesis of cobalamin (vitamin B12) in Propionibacterium freudenreichii (P. shermanii)". Microbiology 148 (Pt 6): 1845–1853. June 2002. doi:10.1099/00221287-148-6-1845. PMID 12055304.
- ↑ Frank, S.; Brindley, A.A.; Deery, E.; Heathcote, P.; Lawrence, A.D.; Leech, H.K.; Pickersgill, R.W.; Warren, M.J. (2005). "Anaerobic synthesis of vitamin B12: Characterization of the early steps in the pathway". Biochemical Society Transactions 33 (4): 811–814. doi:10.1042/BST0330811. PMID 16042604.
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