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...
Main Authors: | , , |
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Format: | Article |
Language: | English |
Published: |
"Alexandru Ioan Cuza" University of Iași
2010-12-01
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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 |
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. |
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ISSN: | 1582-3571 2248-3276 |