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

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 multifuncti...

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Bibliographic Details
Published inBio/technology (New York, N.Y. 1983) Vol. 11; no. 7; pp. 807 - 810
Main Authors Aharonowitz, Y, Bergmeyer, J, Cantoral, J M, Cohen, G, Demain, A L, Fink, U, Kinghorn, J, Kleinkauf, H, MacCabe, A, Palissa, H
Format Journal Article
LanguageEnglish
Published United States 01.07.1993
Subjects
Amino Acid Sequence
Anti-Bacterial Agents - biosynthesis
beta-Lactams
Catalysis
Models, Chemical
Molecular Sequence Data
Peptide Synthases - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0733-222X
1087-0156
1546-1696
DOI:10.1038/nbt0793-807