Studies on the biosynthesis of carbapenem antibiotics. II. Isolation and functions of a specific acylase involved in the depantothenylation of the OA-6129 compounds.
A specific acylase designated A933 acylase was isolated and purified to 90% protein homogeneity from Streptomyces fulvoviridis A933 17M9 which produces PS-5, epithienamycins A and C and MM 17880 together with minor carbapenem analogs, penicillin N and cephamycin C. This enzyme was found to catalyze the depantothenylation of OA-6129 carbapenems; the acyl exchange of OA-6129 carbapenems with acyl CoA's; the deacetylation of N-acetyl-L-amino acids; and the acylation of NS-5 and 6-aminopenicillanate with acyl CoA's, whereas the deacetylation of PS-5 and N-acetyl-D-amino acids; and the deacylation of benzylpenicillin and cephalosporin C were not observed. Similar enzyme activities were also detected in Streptomyces cattleya, Streptomyces cremeus subsp. auratilis and Streptomyces argenteolus which are all carbapenem producers.
D000214:Acyl Coenzyme A / Q000378:metabolism; D000215:Acylation; D000581:Amidohydrolases / Q000302:isolation & purification* / Q000494:pharmacology; D013302:Streptomyces / Q000201:enzymology*; D013845:Thienamycins / Q000378:metabolism*
D000214:Acyl Coenzyme A; D013845:Thienamycins; C036499:OA 6129C; C036497:OA 6129A; C036498:OA 6129B(1); D000581:Amidohydrolases; C019665:amidase