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Stereospecificity of trans-dihydrodiol oxidation by dimeric and monomeric dihydrodiol dehydrogenases from mammalian tissues.
J Biochem. 1994 Mar; 115(3):493-6.JB

Abstract

The stereochemical course in the enzymatic oxidation of trans-dihydrodiols of benzene and naphthalene by dimeric dihydrodiol dehydrogenase of monkey kidney was compared with that by monomeric dihydrodiol dehydrogenase of rat liver. The monkey kidney and rat liver enzymes each oxidized about half of the racemic dihydrodiol of benzene added to the reaction mixture, but almost all the substrate was disappeared in the reaction mixture containing both enzymes. The CD spectra of the unreacted dihydrodiols of benzene and naphthalene in reaction mixtures containing the rat liver enzyme showed the negative sign of Cotton effect, while those in reaction mixtures containing the monkey kidney enzyme gave the positive sign of Cotton effect. Thus, the monkey kidney dimeric enzyme selectively oxidized (-)-[1R,2R]-dihydrodiols of aromatic hydrocarbons, in contrast to the stereo-specificity of the rat liver enzyme for the (+)-[1S,2S]-isomers. The (+)-[1S,2S]- and (-)-[1R,2R]-dihydrodiols of benzene were separately prepared from the racemic form by using the two enzymes, and were used as substrates to determine the stereospecificity of dihydrodiol dehydrogenases from other mammalian tissues. The dimeric enzymes from pig liver and rabbit lens also exhibited specificity for the (-)-isomer, which was opposite to that of the monomeric enzymes from human and mouse liver, although aldehyde reductase and aldose reductase oxidized both (+)- and (-)-isomers.

Authors+Show Affiliations

Biochemistry Laboratory, Gifu Pharmaceutical University.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8056762

Citation

Yamaguchi, S, et al. "Stereospecificity of Trans-dihydrodiol Oxidation By Dimeric and Monomeric Dihydrodiol Dehydrogenases From Mammalian Tissues." Journal of Biochemistry, vol. 115, no. 3, 1994, pp. 493-6.
Yamaguchi S, Inazu A, Deyashiki Y, et al. Stereospecificity of trans-dihydrodiol oxidation by dimeric and monomeric dihydrodiol dehydrogenases from mammalian tissues. J Biochem. 1994;115(3):493-6.
Yamaguchi, S., Inazu, A., Deyashiki, Y., Nakayama, T., Sato, K., Miyabe, Y., & Hara, A. (1994). Stereospecificity of trans-dihydrodiol oxidation by dimeric and monomeric dihydrodiol dehydrogenases from mammalian tissues. Journal of Biochemistry, 115(3), 493-6.
Yamaguchi S, et al. Stereospecificity of Trans-dihydrodiol Oxidation By Dimeric and Monomeric Dihydrodiol Dehydrogenases From Mammalian Tissues. J Biochem. 1994;115(3):493-6. PubMed PMID: 8056762.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stereospecificity of trans-dihydrodiol oxidation by dimeric and monomeric dihydrodiol dehydrogenases from mammalian tissues. AU - Yamaguchi,S, AU - Inazu,A, AU - Deyashiki,Y, AU - Nakayama,T, AU - Sato,K, AU - Miyabe,Y, AU - Hara,A, PY - 1994/3/1/pubmed PY - 1994/3/1/medline PY - 1994/3/1/entrez SP - 493 EP - 6 JF - Journal of biochemistry JO - J. Biochem. VL - 115 IS - 3 N2 - The stereochemical course in the enzymatic oxidation of trans-dihydrodiols of benzene and naphthalene by dimeric dihydrodiol dehydrogenase of monkey kidney was compared with that by monomeric dihydrodiol dehydrogenase of rat liver. The monkey kidney and rat liver enzymes each oxidized about half of the racemic dihydrodiol of benzene added to the reaction mixture, but almost all the substrate was disappeared in the reaction mixture containing both enzymes. The CD spectra of the unreacted dihydrodiols of benzene and naphthalene in reaction mixtures containing the rat liver enzyme showed the negative sign of Cotton effect, while those in reaction mixtures containing the monkey kidney enzyme gave the positive sign of Cotton effect. Thus, the monkey kidney dimeric enzyme selectively oxidized (-)-[1R,2R]-dihydrodiols of aromatic hydrocarbons, in contrast to the stereo-specificity of the rat liver enzyme for the (+)-[1S,2S]-isomers. The (+)-[1S,2S]- and (-)-[1R,2R]-dihydrodiols of benzene were separately prepared from the racemic form by using the two enzymes, and were used as substrates to determine the stereospecificity of dihydrodiol dehydrogenases from other mammalian tissues. The dimeric enzymes from pig liver and rabbit lens also exhibited specificity for the (-)-isomer, which was opposite to that of the monomeric enzymes from human and mouse liver, although aldehyde reductase and aldose reductase oxidized both (+)- and (-)-isomers. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/8056762/Stereospecificity_of_trans_dihydrodiol_oxidation_by_dimeric_and_monomeric_dihydrodiol_dehydrogenases_from_mammalian_tissues_ L2 - https://joi.jlc.jst.go.jp/JST.Journalarchive/biochemistry1922/115.493?lang=en&from=PubMed DB - PRIME DP - Unbound Medicine ER -