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Cobalt-precorrin-5B (C1)-methyltransferase
| Field | Value |
|---|---|
| Name | Cobalt-precorrin-5B (C1)-methyltransferase |
| EC_number | 2.1.1.195 |
Cobalt-precorrin-5B (C1)-methyltransferase (), cobalt-precorrin-6A synthase, CbiD (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:cobalt-precorrin-5B (C1)-methyltransferase. This enzyme catalyses the following chemical reaction
: cobalt-precorrin-5B + S-adenosyl-L-methionine \rightleftharpoons cobalt-precorrin-6A + S-adenosyl-L-homocysteine
This enzyme catalyses the C-1 methylation of cobalt-precorrin-5B in the anaerobic pathway of adenosylcobalamin biosynthesis in bacteria such as Salmonella typhimurium, Bacillus megaterium, and Propionibacterium freudenreichii subsp. shermanii.
References
References
- (December 2000). "The enigma of cobalamin (Vitamin B12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway". The Journal of Biological Chemistry.
- (April 2005). "Genetically engineered production of 1-desmethylcobyrinic acid, 1-desmethylcobyrinic acid a,c-diamide, and cobyrinic acid a,c-diamide in Escherichia coli implies a role for CbiD in C-1 methylation in the anaerobic pathway to cobalamin". The Journal of Biological Chemistry.
- R. Caspi. (2013-09-25). "Pathway: adenosylcobalamin biosynthesis I (anaerobic)". MetaCyc Metabolic Pathway Database.
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