Identity of dimeric dihydrodiol dehydrogenase as NADP+-dependent D-xylose dehydrogenase in pig liver

被引：17

作者：

Aoki, S ^{[1
]}

Ishikura, S ^{[1
]}

Asada, Y ^{[1
]}

Usami, N ^{[1
]}

Hara, A ^{[1
]}

机构：

[1] Gifu Pharmaceut Univ, Biochem Lab, Gifu 5028585, Japan

来源：

CHEMICO-BIOLOGICAL INTERACTIONS | 2001年 / 130卷 / 1-3期

关键词：

dihydrodiol dehydrogenase; D-xylose dehydrogenase; novel protein family;

D O I：

10.1016/S0009-2797(00)00307-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Dimeric dihydrodiol dehydrogenases (DDs, EC 1.3.1.20), which oxidize trans-dihydrodiols of aromatic hydrocarbons to the corresponding catechols, have been molecularly cloned from human intestine, monkey kidney, pig liver, dog liver, and rabbit lens. A comparison of the sequences with the DNA sequences in databases suggested that dimeric DDs constitute a novel protein family with 20 gene products. In addition, it was found that dimeric DD oxidizes several pentoses and hexoses: and the specificity resembles that of NADP(+)-dependent D-xylose dehydrogenase (EC 1.1.1.179) of pig liver. The inhibition of D-xylose dehydrogenase activity in the extracts of monkey kidney, dog liver and pig liver, its co-purification with dimeric DD activity from pig liver, and kinetic analysis of the D-xylose reduction by pig dimeric DD indicated that the two enzymes are the same protein. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：775 / 784

页数：10

共 22 条

[1] Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases [J].