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Results 1 - 9 of 9
EC Number
General Information
network and phylogenetic analyses indicated that salicylaldehyde dehydrogenases (SALDs) and the homologues are present in bacteria and fungi, phylogenetic tree, distribution, and evolution of SALD, overview. Key residues in SALDs are analyzed by evolutionary methods and a molecular simulation analysis. The catalytic residue is most highly conserved, followed by the residues binding NAD+ and then the residues binding salicylaldehyde, molecular simulation analysis
site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis. Cys284 is positioned close to both NAD+ and SAL, implicating it as a potentially important residue
mineralization of naphthalene, detoxification of salicylaldehyde
NahF catalyzes the last reaction in the conversion of naphthalene to salicylate
pathway for the degradation of carbaryl via gentisate, overview. Various enzymes are involved in the metabolic pathway, including salicylaldehyde dehydroganse
the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway
substrate binding induces a conformational change
physiological function
salicylaldehyde dehydrogenase is responsible for the oxidation of salicylaldehyde to salicylate using NAD+ as a cofactor in the naphthalene degradation pathway
physiological function
the enzyme catalyzes the oxidation of salicylaldehyde to salicylate in the carbaryl-degrading Pseudomonas sp. strain C6
Results 1 - 9 of 9