title: Phenoxymethylpenicillin amidohydrolases from Penicillium chrysogenum.
abstract: A phenoxymethylpenicillin amidohydrolase which hydrolyses phenoxymethylpenicillin to 6-aminopenicillanic acid (6-APA) has been isolated from two species of Penicillium chrysogenum. The amidohydrolase had a molecular mass of approx. 42 kDa. Its activity with benzylpenicillin as substrate was only 1.5% of that with phenoxymethylpenicillin and it was inhibited by its products. No penicillin formation from 6-APA and phenoxyacetyl or phenylacetyl coenzyme A was observed. The enzyme is thus distinct from the phenylacetyl coenzyme A:6-APA acyltransferase, which also has amidohydrolase activity and is involved in the final stages of the biosynthesis of penicillins.
authors.affiliation: The Sir William Dunn School of Pathology, Oxford, UK.
authors.forename: P A
authors.initials: PA
authors.lastname: Whiteman
authors.forename: E P
authors.initials: EP
authors.lastname: Abraham
mesh_terms: D002511:Cephalosporins / Q000494:pharmacology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D008970:Molecular Weight; D010397:Penicillanic Acid / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology; D010399:Penicillin Amidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D010404:Penicillin V / Q000378:metabolism* / Q000494:pharmacology; D010408:Penicillium chrysogenum / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002511:Cephalosporins; D004791:Enzyme Inhibitors; D010397:Penicillanic Acid; C030735:7-aminocephalosporanic acid; C101921:phenoxymethylpenicillin amidohydrolase; D010399:Penicillin Amidase; C004408:aminopenicillanic acid; D010404:Penicillin V