Cobalt-precorrin 5A hydrolase
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| Cobalt-precorrin 5A hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.7.1.12 | ||||||||
| 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 5A hydrolase (EC 3.7.1.12), CbiG (gene)) is an enzyme with systematic name cobalt-precorrin 5A acylhydrolase.[1] This enzyme catalyses the following chemical reaction
- cobalt-precorrin-5A + H2O {\displaystyle \rightleftharpoons } cobalt-precorrin-5B + acetaldehyde + 2 H+
This enzyme hydrolyses the ring A acetate delta-lactone of cobalt-precorrin-5A and releases a two-carbon fragment from the macrocyclic corrin ring as acetaldehyde. This is part of the biosynthetic pathway to cobalamin (vitamin B12) in anaerobic bacteria such as Salmonella typhimurium and Bacillus megaterium .
See also
[edit ]References
[edit ]- ^ Kajiwara Y, Santander PJ, Roessner CA, Pérez LM, Scott AI (August 2006). "Genetically engineered synthesis and structural characterization of cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway to vitamin B12: definition of the roles of the CbiF and CbiG enzymes". Journal of the American Chemical Society. 128 (30): 9971–8. doi:10.1021/ja062940a. PMID 16866557.
External links
[edit ]- Cobalt-precorrin+5A+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
