Biology:8-amino-7-oxononanoate synthase
| 8-amino-7-oxononanoate synthase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.3.1.47 | ||||||||
| CAS number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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 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
- "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. October 1968. doi:10.1128/JB.96.4.1291-1297.1968. PMID 4879561.
- "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. November 1998. doi:10.1006/jmbi.1998.2086. PMID 9813126.
- "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. January 1999. doi:10.1046/j.1432-1327.1999.00006.x. PMID 9914476.
- "Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies". Biochemistry 39 (3): 516–28. January 2000. doi:10.1021/bi991620j. PMID 10642176.
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