Purification and Characterization of NAD(+)-Dependent Salicylaldehyde Dehydrogenase from Carbaryl-Degrading Pseudomonas sp Strain C6
DSpace at IIT Bombay
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Title |
Purification and Characterization of NAD(+)-Dependent Salicylaldehyde Dehydrogenase from Carbaryl-Degrading Pseudomonas sp Strain C6
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Creator |
SINGH, R
TRIVEDI, VD PHALE, PS |
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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 |
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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.
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Publisher |
HUMANA PRESS INC
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Date |
2014-12-28T14:28:19Z
2014-12-28T14:28:19Z 2014 |
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Type |
Article
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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 |
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Language |
English
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