8-amino-7-oxononanoate synthase
8-amino-7-oxononanoate synthase | |||||||||
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Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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
Thus, the two
.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. 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. 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. 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. PMID 10642176.