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Arylamidase of Cephalosporium acremonium and Its Specificity for Cephalosporin C

机译：顶头孢霉的丙烯酰胺酶及其对头孢菌素C的特异性

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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.
机译：顶头孢霉产生三种聚集形式的芳酰胺酶。通过二乙氨基乙基纤维素色谱，凝胶过滤和凝胶电泳将分子量约为60,000的胞外酶纯化300倍。以1-亮氨酰-β-萘酰胺为底物，Km为4.2×10 -4m。最佳pH值为7.7;头孢菌素抑制了l-亮氨酰-β-萘酰胺的酶水解，而各种青霉素则没有作用。或者，该酶特异性催化许多头孢菌素的β-内酰胺水解。许多青霉素具有抗性。头孢菌素C的Km为9.09×10？4m。

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