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J. Biochem, 1989, Vol. 106, No. 1 126-132
© 1989 Japanese Biochemical Society

research-article

Monkey Liver Indanol Dehydrogenase. Purification, Properties, and Kinetic Mechanism1

Akira Hara, Kouji Mouri, Makoto Nakagawa, Mitsuhiro Nakamura, Toshihiro Nakayama, Kazuya Matsuura and Hideo Sawada2

Department of Biochemistry, Gifu Pharmaceutical University Gifu, Gifu 502

2To whom correspondence should be addressed.

Indanol dehydrogenase was purified to apparent homogeneity from monkey liver cytosol. The enzyme was a monomer with a molecular weight of 36, 000 and pi of 8.7. The amino acid composition was determined. The enzyme oxidized alicyclic alcohols including trans-dihydrodiols of benzene and naphthalene in the presence of both NADP+ and NAD+ and reduced several xenobiotic carbonyl compounds in the presence of NADPH, the 4-pro-R hydrogen atom of which was transferred to the substrate. The results of fluorometric binding and kinetic studies are consistent with an ordered sequential mechanism with NADP+ binding first. The enzyme was inhibited competitively versus NADP+ and un-competitively versus 1-indanol not only by cheiating agents such as 1, 10-phenanthroline and 2, 2 -bipyridine but also by a nonchelating isomer, 4, 4'-bipyridine, which suggests hydrophobic interaction of the aromatic compounds with the enzyme, which did not contain zinc. The enzyme was also inhibited by Cibacron blue dye, synthetic estrogens, and {delta}4–3-ketosteroids. The inhibition by Cibacron blue was competitive versus NADP+ and noncompetitive versus 1-indanol, whereas those by hexestrol, medroxyprogesterone acetate, and progesterone were uncompetitive versus NADP+ and competitive versus 1-indanol, corraborating the ordered addition of the coenzyme prior to 1-indanol.

1This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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