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
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 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. This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1BS0, 1DJ9, 1DJE, and 2G6W.
References
- Eisenberg MA, Star C (1968). "Synthesis of 7-Oxo-8-Aminopelargonic Acid, a Biotin Vitamer, in Cell-free Extracts of Escherichia coli Biotin Auxotrophs". J. Bacteriol. 96 (4): 1291–7. PMC 252447. PMID 4879561.
- L; Alexeeva, M; Baxter, RL; Campopiano, DJ; Webster, SP; Sawyer, L (1998). "The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme". J. Mol. Biol. 284 (2): 401–19. doi:10.1006/jmbi.1998.2086. PMID 9813126.
- Ploux O, Breyne O, Carillon S, Marquet A (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". Eur. J. Biochem. 259 (1–2): 63–70. doi:10.1046/j.1432-1327.1999.00006.x. PMID 9914476.
- Baxter RL; Alexeev, D; Campopiano, DJ; Watt, RM; Alexeeva, M; Sawyer, L; Baxter, RL (2000). "Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies". Biochemistry. 39 (3): 516–28. doi:10.1021/bi991620j. PMID 10642176.
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