Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway.

ABSTRACT: Salicylaldehyde (SAL) dehydrogenase (SALD) is responsible for the oxidation of SAL to salicylate using nicotinamide adenine dinucleotide (NAD⁺) as a cofactor in the naphthalene degradation pathway. We report the use of a protein sequence similarity network to make functional inferences about SALDs. Network and phylogenetic analyses indicated that SALDs and the homologues are present in bacteria and fungi. The key residues in SALDs were analyzed by evolutionary methods and a molecular simulation analysis. The results showed that the catalytic residue is most highly conserved, followed by the residues binding NAD⁺ and then the residues binding SAL. A molecular simulation analysis demonstrated the binding energies of the amino acids to NAD⁺ and/or SAL and show

SUBMITTER: Jia B 

PROVIDER: S-EPMC5324060 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature