| Literature DB >> 8373826 |
J H McKie1, R Jaouhari, K T Douglas, D Goffner, C Feuillet, J Grima-Pettenati, A M Boudet, M Baltas, L Gorrichon.
Abstract
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.Entities:
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Year: 1993 PMID： 8373826 DOI： 10.1016/0167-4838(93)90063-w
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002