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 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
References
- ^ 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
- Cobalt-precorrin+5A+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
