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The genes encoding NAD+ -dependent alanine dehydrogenases (AlaDHs) (EC1.4.1.1 ) from the Antarctic bacterial organismsShewanella sp. strain Ac10 (SheAlaDH) andCarnobacterium sp. strain St2 (CarAlaDH) were cloned and expressed inEscherichia coli . Of all of the AlaDHs that have been sequenced, SheAlaDH exhibited the highest level of sequence similarity to the AlaDH from the gram-negative bacteriumVibrio proteolyticus (VprAlaDH). CarAlaDH was most similar to AlaDHs from mesophilic and thermophilicBacillus strains. SheAlaDH and CarAlaDH had features typical of cold-adapted enzymes; both the optimal temperature for catalytic activity and the temperature limit for retaining thermostability were lower than the values obtained for the mesophilic counterparts. Thek cat /Km value for the SheAlaDH reaction was about three times higher than thek cat /Km value for VprAlaDH, but it was much lower than thek cat /Km value for the AlaDH fromBacillus subtilis . Homology-based structural models of various AlaDHs, including the two psychrotrophic AlaDHs, were constructed. The thermal instability of SheAlaDH and CarAlaDH may result from relatively low numbers of salt bridges in these proteins.

applied and environmental microbiology

Cold-Adapted Alanine Dehydrogenases from Two Antarctic Bacterial Strains: Gene Cloning, Protein Characterization, and Comparison with Mesophilic and Thermophilic Counterparts