Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine Synthetase, the Multienzyme Integrating the Four Primary Reactions in Beta-Lactam Biosynthesis, as a Model Peptide Synthetase

Biotechnology (N Y). 1993 Jul;11(7):807-10. doi: 10.1038/nbt0793-807.

Abstract

ACV synthetase forms the tripeptide precursor of penicillins and cephalosporins from alpha-aminoadipate, cysteine, and valine. Catalytic sites for substrate carboxyl activation as adenylates, peptide bond formations, epimerization and release of the tripeptide-thioester are integrated in multifunctional enzymes of 405 to 425 kD. These have been characterized from several pro- and eukaryotic beta-lactam producers. Implications of these results for the thio-template mechanism of peptide formation are discussed, as well as the use of this multienzyme as a model system for enzymatic peptide synthesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / biosynthesis*
  • Catalysis
  • Models, Chemical*
  • Molecular Sequence Data
  • Peptide Synthases / metabolism*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • beta-Lactams

Substances

  • Anti-Bacterial Agents
  • beta-Lactams
  • Peptide Synthases
  • alpha-aminoadipyl-cysteinyl-valine synthetase