8-amino-7-oxononanoate synthase
In enzymology, a 8-amino-7-oxononanoate synthase (EC 2.3.1.47) is an enzyme that catalyzes the chemical reaction
- 6-carboxyhexanoyl-CoA + L-alanine 8-amino-7-oxononanoate + CoA + CO2
| 8-amino-7-oxononanoate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.47 | ||||||||
| CAS no. | 9075-61-0 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are 6-carboxyhexanoyl-CoA and L-alanine, whereas its 3 products are 8-amino-7-oxononanoate, CoA, and CO2.
This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 6-carboxyhexanoyl-CoA:L-alanine C-carboxyhexanoyltransferase (decarboxylating). Other names in common use include 7-keto-8-aminopelargonic acid synthetase, 7-keto-8-aminopelargonic synthetase, and 8-amino-7-oxopelargonate synthase.
References
Further reading
- Eisenberg MA, Star C (October 1968). "Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs". Journal of Bacteriology. 96 (4): 1291–7. doi:10.1128/JB.96.4.1291-1297.1968. PMC 252447. PMID 4879561.
- Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L (November 1998). "The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme". Journal of Molecular Biology. 284 (2): 401–19. doi:10.1006/jmbi.1998.2086. PMID 9813126.
- Ploux O, Breyne O, Carillon S, Marquet A (January 1999). "Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies". European Journal of Biochemistry. 259 (1–2): 63–70. doi:10.1046/j.1432-1327.1999.00006.x. PMID 9914476.
- Webster SP, Alexeev D, Campopiano DJ, Watt RM, Alexeeva M, Sawyer L, Baxter RL (January 2000). "Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies". Biochemistry. 39 (3): 516–28. doi:10.1021/bi991620j. PMID 10642176.