Detail of "13253-44-6"

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Properties of dihydropyrimidinase in intact cells of Pseudomonas putida

Properties of dihydropyrimidinase in intact cells of Pseudomonas putida. Sun, Wanru (Inst. Microbiol., Acad. 13253-44-6 and 616-03-5 are also occured in this study. Sin., Beijing, Peop. Rep. China). Weishengwu Xuebao, 23(3), 257-64 (Chinese) 1983. CODEN: WSHPA8. ISSN: 0001-6209. DOCUMENT TYPE: Journal CA Section: 10 (Microbial Biochemistry) Section cross-reference(s): 7 The substrate specificity of dihydropyrimidinase in P. putida cells for hydantoin derivs. was highest for 5-phenylhydantoin followed in order by 5-methylthioethylhydantoin, 5-methylhydantoin, and 5-isobutylhydantoin. Whereas the optimum pH for the reactions varies with the substrate, the optimum temp. is similar for all substrates. The enzyme activity is strongly inhibited by Ag+, Cu2+, and Zn2+, as well as by chelating agents. The enzyme activity was decreased by ~70% by addn. of EDTA, but >90% of the activity was recovered when Fe2+ was added. The Km values of the enzyme for 5-phenylhydantoin, 5-methylthioethylhydantoin, and 5-methylhydantoin were 1.61 ′ 10-2, 2.08 ′ 10-2, and 1.61 ′ 10-1M, resp. .