Cobalt-factor II C20-methyltransferase
| Cobalt-factor II C20-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.151 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Cobalt-factor II C20-methyltransferase (EC 2.1.1.151) is an enzyme that catalyzes the 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
- ↑ 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.
- ↑ 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. Vol. 61. pp. 267–297. doi:10.1016/s0083-6729(01)61009-4. ISBN 9780127098616. PMID 11153269.
- ↑ Roessner CA, Huang KX, Warren MJ, Raux E, Scott AI (June 2002). "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. 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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