Studies on the biosynthesis of carbapenem antibiotics. III. Enzymological characterization of the L-amino acid acylase activity of A933 acylase.
A933 acylase, which is involved in exchange of the pantothenyl substituent of OA-6129 carbapenems with acetyl CoA, was characterized as an L-amino acid acylase with a molecular weight of 100,000 (+/- 8,000) and a pI value of 5.1. The highest L-amino acid acylase activity of A933 acylase was observed at 37 degrees C and pH 7 approximately 7.5 for N-chloroacetyl-L-phenylalanine. Unlike other amino acid acylases, A933 acylase was severely inhibited by cobalt ions and p-chloromercuribenzoate. The acylase also showed peptidase activity with some di- and tripeptides. A protein fraction with A933 L-amino acid acylase activity from blocked mutant 1501 lacked OA-6129A-depantothenylating activity.
D000581:Amidohydrolases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000145:classification; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D009154:Mutation; D009842:Oligopeptides / Q000378:metabolism; D013696:Temperature; D013845:Thienamycins / Q000096:biosynthesis* / Q000378:metabolism
D008670:Metals; D009842:Oligopeptides; D013845:Thienamycins; C016883:PS 5; C036497:OA 6129A; D000581:Amidohydrolases