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 language | English |
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Pages (from-to) | 807-810 |
Number of pages | 4 |
Journal | Bio/Technology |
Volume | 11 |
Issue number | 7 |
DOIs | |
State | Published - Jul 1993 |
Externally published | Yes |