Abstract
A novel putative aldehyde dehydrogenase (ALDH) gene aldh1413 from Flammeovirga pacifica isolated from deep sea sediment was cloned, expressed, and characterized. The molecular weight of the ALDH1413 (479 amino acids) was estimated by SDS-PAGE to be 53 kDa. The optimum temperature and pH for ALDH1413 were 35°C and 9.0, respectively. In the presence of either NAD+ or NADP+, the enzyme could oxidize a number of aliphatic aldehydes, particularly C3-and C5-aliphatic aldehydes and aromatic aldehydes such as benzaldehyde, which indicates that the enzyme belongs to broad-specific (ALDH) superfamily. Steady-state kinetic study revealed that ALDH1413 had a KM value of 0.545 mM and a kcat value of 7.48 s−1 when propionaldehyde was used as the substrate. The Na+ could enhance ALDH1413 activity, which indicated it might be adapt to its habitat, marine environment.
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