Review

Yair Aharonowitz, Jürgen Bergmeyer, Jesus M. Cantoral, Gerald Cohen, Arnold L. Demain, Uwe Fink, Jim Kinghorn, Horst Kleinkauf, Andrew MacCabe, Harriet Palissa, Eva Pfeifer, Torsten Schwecke, Henk van Liempt, Hans von Döhren*, Saul Wolfe, Jinyou Zhang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

ACV Synthetase forms the tripeptide precursor of penicillins and cephalosporins from a-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 Iactam 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.

Original languageEnglish
Pages (from-to)807-810
Number of pages4
JournalBio/Technology
Volume11
Issue number7
DOIs
StatePublished - Jul 1993
Externally publishedYes

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