In- silico identification of key residues for shifting the coenzyme specificity of an aldehyde-dehidrogenase

The aldehyde dehydrogenase enzyme coded by the pAO1 megaplasmid of A. nicotinovorans has an 35% identity at the sequence level with the succinic-semialdehyde dehydrogenase from E. coli, the latter being a suitable template for homology modeling experiments. The computer generated model of AlDH helpe...

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Bibliographic Details
Main Authors: Marius Mihasan, Vlad Artenie, Zenovia Olteanu
Format: Article
Language:English
Published: "Alexandru Ioan Cuza" University of Iași 2010-12-01
Series:Analele Ştiinţifice Ale Universităţii Alexandru Ioan Cuza din Iași,Sectiunea II A : Genetica si Biologie Moleculara
Online Access:http://www.gbm.bio.uaic.ro/index.php/gbm/article/view/833
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Summary:The aldehyde dehydrogenase enzyme coded by the pAO1 megaplasmid of A. nicotinovorans has an 35% identity at the sequence level with the succinic-semialdehyde dehydrogenase from E. coli, the latter being a suitable template for homology modeling experiments. The computer generated model of AlDH helped at identifying the residues implicated in catalysis (C266, E232, R143, Q266, S423) as well as in co-enzyme specificity (K158, Ser161, G215). Several single mutants were constructed and docked with NAD+ and NADP+ in an attempt to identify the key residues for shifting the NAD/NADP preference of the pAO1 coded enzyme.
ISSN:1582-3571
2248-3276