The enantioselectivity of quinohaemoprotein alcohol dehydrogenases: mechanistic and structural aspects

被引：21

作者：

Jongejan, A ^{[1
]}

Machado, SS ^{[1
]}

Jongejan, JA ^{[1
]}

机构：

[1] Delft Univ Technol, Dept Biotechnol, Kluyver Lab, NL-2628 BC Delft, Netherlands

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 8卷 / 1-3期

关键词：

pyrroloquinoline quinone; quinohaemoprotein; alcohol dehydrogenase; enantioselective oxidation; chiral alcohols; kinetics; mechanism; structure; molecular modeling; review;

D O I：

10.1016/S1381-1177(99)00063-6

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：

Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, isolated from Acetobacter, Gluconobacter and Comamonas species show appreciable enantioselectivity in the oxidation of chiral primary and secondary alcohols. Current views of the structural and mechanistic factors of importance for the understanding of the enantioselective performance of these enzymes are reviewed. Structural properties of QH-ADH, Type I, from C. testosteroni, and QH-ADH, Type II, from A. pasteurianus have been deduced from homology modeling studies based on the X-ray crystallographic data available for PQQ-containing quinoprotein methanol dehydrogenases, MDHs. Mechanisms that have been proposed for quino(haemo)protein alcohol dehydrogenase-catalyzed substrate oxidation are discussed in relation to the constraints set by the observed enantioselectivity. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：121 / 163

页数：43

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