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The D-sorbitol dehydrogenase gene, sldA, and an upstream gene, sldB, encoding a hydrophobic polypeptide, SldB, of Gluconobacter suboxydans IFO 3255 were disrupted in a check of their biological functions. The bacterial cells with the sldA gene disrupted did not produce L-sorbose by oxidation of D-sorbitol in resting-cell reactions at pHs 4.5 and 7.0, indicating that the dehydrogenase was the main D-sorbitol-oxidizing enzyme in this bacterium. The cells did not produce D-fructose from D-mannitol or dihydroxyacetone from glycerol. The disruption of the sldB gene resulted in undetectable oxidation of D-sorbitol, D-mannitol, or glycerol, although the cells produced the dehydrogenase. The cells with the sldB gene disrupted produced more of what might be signal-unprocessed SldA than the wild-type cells did. SldB may be a chaperone-like component that assists signal processing and folding of the SldA polypeptide to form active D-sorbitol dehydrogenase.

bioscience, biotechnology, and biochemistry

Main Polyol Dehydrogenase of<i>Gluconobacter suboxydans</i>IFO 3255, Membrane-bound<scp>D</scp>-Sorbitol Dehydrogenase, That Needs Product of Upstream Gene,<i>sldB</i>, for Activity

Main Polyol Dehydrogenase ofGluconobacter suboxydansIFO 3255, Membrane-boundD-Sorbitol Dehydrogenase, That Needs Product of Upstream Gene,sldB, for Activity