N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase

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In enzymology, a N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase (EC 6.3.2.26) is an enzyme that catalyzes the chemical reaction

3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H₂O $\rightleftharpoons$ 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine

The 5 substrates of this enzyme are ATP, L-2-aminohexanedioate, L-cysteine, L-valine, and H₂O, whereas its 3 products are AMP, diphosphate, and [[N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine]].

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming, valine-inverting). Other names in common use include L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase, ACV synthetase, and L-alpha-aminoadipyl-cysteinyl-valine synthetase. This enzyme participates in penicillin and cephalosporin biosynthesis.

[edit] References

IUBMB entry for 6.3.2.26
BRENDA references for 6.3.2.26 (Recommended.)
PubMed references for 6.3.2.26
PubMed Central references for 6.3.2.26
Google Scholar references for 6.3.2.26
Byford MF, Baldwin JE, Shiau CY, Schofield CJ (1997). "The Mechanism of ACV Synthetase". Chem. Rev. 97: 2631–2650. doi:10.1021/cr960018l. PMID 11851475.
Theilgaard HB, Kristiansen KN, Henriksen CM, Nielsen J (Pt 1). "Purification and characterization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Penicillium chrysogenum". Biochem. J. 327: 185–91. PMID 9355751.