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Purification and Characterization of NAD(+)-Dependent Salicylaldehyde Dehydrogenase from Carbaryl-Degrading Pseudomonas sp Strain C6

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Title Purification and Characterization of NAD(+)-Dependent Salicylaldehyde Dehydrogenase from Carbaryl-Degrading Pseudomonas sp Strain C6
 
Creator SINGH, R
TRIVEDI, VD
PHALE, PS
 
Subject Aromatic aldehydes
Carbaryl metabolic pathway
Salicylaldehyde dehydrogenase
Kinetic characterization
Spectroscopic properties
AROMATIC-ALDEHYDES
NAPHTHALENE DEGRADATION
METHANOL DEHYDROGENASE
ALCOHOL-DEHYDROGENASE
ESCHERICHIA-COLI
ORNITHINE CARBAMOYLTRANSFERASE
ACINETOBACTER-CALCOACETICUS
BENZALDEHYDE DEHYDROGENASE
FORMALDEHYDE DEHYDROGENASE
THERMOTOLERANT BACILLUS
 
Description NAD(+)-dependent salicylaldehyde dehydrogenase (SALDH) which catalyzes the oxidation of salicylaldehyde to salicylate was purified form carbaryl-degrading Pseudomonas sp. strain C6. The enzyme was found to be a functional homotrimer (150 kDa) with subunit molecular mass of 50 kDa and contained calcium (1.8 mol/mol of enzyme). These properties were found to be unique. External addition of metal ions showed no effect on the activity and addition of chelators showed moderate inhibition of the activity. Potassium ions were found to enhance the activity significantly. SALDH showed higher affinity for salicylaldehyde (K-m=4.5 mu M) and accepts mono-as well as di-aromatic aldehydes; however it showed poor activity on aliphatic aldehydes. Chloro-/nitro-substituted benzaldehydes were potent substrate inhibitors as compared to benzaldehyde and 3-hydroxybenzaldehyde, while 2-naphthaldehyde and salicylaldehyde were moderate. The kinetic data revealed that SALDH, though having broad specificity, is more efficient for the oxidation of salicylaldehyde as compared to other aromatic aldehyde dehydrogenases which gives an advantage for Pseudomonas sp. strain C6 to bioremediate carbaryl and other aromatic aldehydes efficiently.
 
Publisher HUMANA PRESS INC
 
Date 2014-12-28T14:28:19Z
2014-12-28T14:28:19Z
2014
 
Type Article
 
Identifier APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 172(2)806-819
0273-2289
1559-0291
http://dx.doi.org/10.1007/s12010-013-0581-8
http://dspace.library.iitb.ac.in/jspui/handle/100/16753
 
Language English