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. 1971 May;21(5):907–915. doi: 10.1128/am.21.5.907-915.1971

Arylamidase of Cephalosporium acremonium and Its Specificity for Cephalosporin C

David W Dennen 1, Charles C Allen 1, Diane D Carver 1
PMCID: PMC377307  PMID: 5103343

Abstract

Three aggregational forms of arylamidase are produced by Cephalosporium acremonium. The exocellular enzyme, with an approximate molecular weight of 60,000, was purified 300-fold by diethylaminoethyl cellulose chromatography, gel filtration, and gel electrophoresis. With l-leucyl-β-naphthylamide as the substrate, the Km is 4.2 × 10−4m; the optimum pH, 7.7; and the temperature optimum, 35 C. The enzymatic hydrolysis of l-leucyl-β-naphthylamide is inhibited by a number of cephalosporins, whereas a variety of penicillins show no effect. Alternatively, the enzyme specifically catalyzes the β-lactam hydrolysis of a number of cephalosporins; a number of penicillins are resistant. The Km for cephalosporin C is 9.09 × 10−4m.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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