NADH-dependent cinerulose reductase in rat liver microsomes. |
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| Authors: | T Komiyama T Oki T Inui T Takeuchi H Umezawa |
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| Institution: | 1. Central Research Labolatories, Sanraku-Ocean Co., Ltd., 4-9-1, Johnan, Fujisawa 251 Japan;2. Institute of Microbial Chemistry, 3-14-23, Kamiosaki, Shinagawa-ku, Tokyo 141, Japan |
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| Abstract: | In the course of studies on the metabolism of a new antitumor anthracycline antibiotic, aclacinomycin A, the new keto reductase which catalyzes the reduction of keto group of L-cinerulose of aclacinomycin A to L-rhodinose was found in rat liver microsomal membrane. The enzyme requires NADH for the reduction and showed optimum pH at 7.0. Km value for aclacinomycin A, 2.1 × 10?5 M and the concentration of NADH need to half maximal activity, 6.2 × 10?5 M were obtained. The activity was potently inhibited by detergents, such as Triton X-100, sodium deoxycholate and sodium dodecyl sulfate. |
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