Main ethanol metabolizing alcohol dehydrogenases (ADH I and ADH IV): biochemical functions and the physiological manifestation

被引：18

作者：

Ashmarin, IP ^{[1
]}

Danilova, RA ^{[1
]}

Obukhova, MF ^{[1
]}

Moskvitina, TA ^{[1
]}

Prosorovsky, VN ^{[1
]}

机构：

[1] Moscow State Univ, Inst Biomed Chem, Moscow, Russia

来源：

FEBS LETTERS | 2000年 / 486卷 / 01期

关键词：

alcohol dehydrogenase; retinol; steroid; craving for ethanol; acetaldehyde; lipid peroxidation; xenobiotic;

D O I：

10.1016/S0014-5793(00)02229-8

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：

The range of the biochemical reactions which can be catalyzed by ADH I and ADH IV is extremely wide. The most characterized functions of these enzymes are protection against excess endogenous acetaldehyde, products of lipid peroxidation, exogenous alcohols and some xenobiotics. It was found also that ADH I and ADH IV are important members of the enzyme system synthesizing retinoic acid (especially during embryogenesis), They can oxidize some steroids and participate in bioamine and prostaglandin metabolism but so far the extent of their contribution to the latter processes is under discussion. Recent data suggest a correlation between the activity of ADH I in some organs and fine physiological processes including behavior regulation and craving for alcohol in albino rats. (C) 2000 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.

引用

页码：49 / 51

页数：3

共 30 条

[1] Alcohol dehydrogenase of human and rat blood vessels - Role in ethanol metabolism [J].