A MOLECULAR-MODEL FOR CINNAMYL ALCOHOL-DEHYDROGENASE, A PLANT AROMATIC ALCOHOL-DEHYDROGENASE INVOLVED IN LIGNIFICATION

被引：46

作者：

MCKIE, JH

JAOUHARI, R

DOUGLAS, KT

GOFFNER, D

FEUILLET, C

GRIMAPETTENATI, J

BOUDET, AM

BALTAS, M

GORRICHON, L

机构：

[1] UNIV MANCHESTER,DEPT PHARM,MANCHESTER M13 9PL,LANCS,ENGLAND

[2] UNIV TOULOUSE 3,CTR BIOL & PHYSIOL VEGETALES,CNRS,URA 1457,F-31062 TOULOUSE,FRANCE

[3] UNIV TOULOUSE 3,CNRS,F-31062 TOULOUSE,FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1202卷 / 01期

基金：

英国惠康基金;

关键词：

ALCOHOL DEHYDROGENASE; LIGNIFICATION; MOLECULAR MODELING; DEHYDROGENASE; SEQUENCE HOMOLOGY; STRUCTURAL MODEL;

D O I：

10.1016/0167-4838(93)90063-W

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 plant aromatic alcohol dehydrogenase, cinnamyl alcohol dehydrogenase (CAD2 from Eucalyptus) was found by sequence analysis of its cloned gene to be homologous to a range of dehydrogenases including alcohol dehydrogenases, L-threonine-3-dehydrogenase, D-xylose reductase and sorbitol dehydrogenase. A homology model of CAD2 was built using the X-ray crystallographic coordinates of horse-liver alcohol dehydrogenase to provide the template, with additional modelling input from other analogous regions of structure from similar enzymes where necessary. The structural model thus produced rationalised the Zn-binding properties of CAD2, indicated the possession of a Rossmann fold (GXGXXG motif), and explained the class A stereospecificity (pro-R hydrogen removal from substrate alcohol) and aromatic substrate specificity of the enzyme. A range of potential ligands was designed based on the homology model and tested as inhibitors of CAD2 and horse liver alcohol dehydrogenase.

引用

页码：61 / 69

页数：9

共 40 条

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