In enzymology, a 6-carboxyhexanoate—CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction
| 6-Carboxyhexanoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.14 | ||||||||
| CAS no. | 55467-50-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- ATP + 6-carboxyhexanoate + CoA AMP + diphosphate + 6-carboxyhexanoyl-CoA
The 3 substrates of this enzyme are ATP, 6-carboxyhexanoate, and CoA, whereas its 3 products are AMP, diphosphate, and 6-carboxyhexanoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6-carboxyhexanoyl-CoA synthetase, and pimelyl-CoA synthetase. This enzyme participates in biotin metabolism.
References
edit- Izumi Y, Morita H, Sato K, Tani Y, Ogata K (1972). "Synthesis of biotin-vitamers from pimelic acid and coenzyme A by cell-free extracts of various bacteria". Biochim. Biophys. Acta. 264 (1): 210–3. doi:10.1016/0304-4165(72)90133-x. PMID 4623286.
- Izumi Y, Morita H, Tani Y, Ogata K (1974). "The pimelyl-CoA synthetase responsible for the first step in biotin biosynthesis by microorganisms". Agric. Biol. Chem. 38 (11): 2257–2262. doi:10.1271/bbb1961.38.2257.
