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PubMed · 6805183

Penicillin amidase from Proteus rettgeri.

M Robak·A Szewczuk
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Abstract

1. Penicillin amidase from Proteus rettgeri was purified 580-fold by a four-step chromatographic procedure. Titration with phenylmethanesulphonyl fluoride showed that the purified preparation contains 53% of the enzyme. 2. The molecular weight of the amidase was found to be 65.000. The enzyme is strongly inhibited by N-bromosuccinimide and zinc ions. It hydrolyses penicillins, cephalosporins and some synthetic substrates, and in addition it catalyses synthesis of ampicillin from methyl ester of phenylglycine and 6-aminopenicillanic acid. 3. The immobilized amidase obtained by copolymerization of the chemically modified enzyme with acrylamide was applied for preparative hydrolysis of benzylpenicillin.

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AmidohydrolasesBacteriaMetalsMolecular WeightPenicillin AmidasePenicillin GPenicillin VProteusSubstrate SpecificityTime FactorsJournal Article

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M Robak, A Szewczuk. 1981. Penicillin amidase from Proteus rettgeri.. https://pubmed.ncbi.nlm.nih.gov/6805183/

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