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KMID : 0380219990320020127
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 2 p.127 ~ p.132
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Biochemical Properties of NAD(P)H-Quinone Oxidoreductase from Saccharomyces cerevisiae
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Kim Kyung-Soon
Suk Hee-Won
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Abstract
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The NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified from S. cerevisiae. The native molecular weight of the enzyme is approximately 111 kDa and is composed of five identical subunits with molecular weights of 22 kDa each. The optimum pH of the enzyme is pH 6.0 with 1,4-benzoquinone as a substrate. The apparent km for 1,4-benzoquinone and 1,4- naphthoquinone are 1.3 mM and 14.3μM, respectively. Its activity is greatly inhibited by Cu2+ and Hg2+ ions, nitrofurantoin, dicumarol, and Cibacron blue 3GA. The purified NAD(P)H-quinone oxidoreductase was found capable of reducing aromatic nitroso compounds as well as a variety of quinones, and can utilize either NADH or NADPH as a source of reducing equivalents. The nitroso reductase activity of the purified NAD(P)H-quinone oxidoreductase is strongly inhibited by dicumarol.
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KEYWORD
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NAD(P)H-quinone oxidoreductase, S. cerevisiae
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