Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli.
The penicillin G acylase genes from the Proteus rettgeri wild type and from a hyperproducing mutant which is resistant to succinate repression were cloned in Escherichia coli K-12. Expression of both wild-type and mutant P. rettgeri acylase genes in E. coli K-12 was independent of orientation in the cloning vehicle and apparently resulted from recognition in E. coli of the P. rettgeri promoter sequences. The P. rettgeri acylase was secreted into the E. coli periplasmic space and was composed of subunits electrophoretically identical to those made in P. rettgeri. Expression of these genes in E. coli K-12 was not repressed by succinate as it is in P. rettgeri. Instead, expression of the enzymes was regulated by glucose catabolite repression.
D000581:Amidohydrolases / Q000235:genetics*; D003001:Cloning, Molecular; D004794:Enzyme Repression; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D005947:Glucose / Q000494:pharmacology; D010399:Penicillin Amidase / Q000096:biosynthesis / Q000235:genetics*; D011401:Promoter Regions, Genetic; D011511:Proteus / Q000201:enzymology / Q000235:genetics*; D013386:Succinates / Q000494:pharmacology; D019802:Succinic Acid
D013386:Succinates; D019802:Succinic Acid; D000581:Amidohydrolases; D010399:Penicillin Amidase; D005947:Glucose