Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating)
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| Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.196 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) (EC 2.1.1.196, CbiT) is an enzyme with systematic name S-adenosyl-L-methionine:precorrin-7 C15-methyltransferase (C12-decarboxylating).[1][2] This enzyme catalyses the following chemical reaction
This enzyme catalyses both methylation at C-15 and decarboxylation of the C-12 acetate side chain of cobalt-precorrin-7 in the anaerobic pathway[3] of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.
See also[edit]
References[edit]
- ^ Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF (November 2002). "The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase". Structure. 10 (11): 1475–87. doi:10.1016/S0969-2126(02)00876-6. PMID 12429089.
- ^ Santander PJ, Kajiwara Y, Williams HJ, Scott AI (February 2006). "Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway". Bioorganic & Medicinal Chemistry. 14 (3): 724–31. doi:10.1016/j.bmc.2005.08.062. PMID 16198574.
- ^ R. Caspi (2013-09-25). "Pathway: adenosylcobalamin biosynthesis I (anaerobic)". MetaCyc Metabolic Pathway Database. Retrieved 2020-04-24.
External links[edit]
- Cobalt-precorrin-7+(C15)-methyltransferase+(decarboxylating) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
