Abstract
Maurer, P. R. (University of Otago Medical School, Dunedin, New Zealand) and R. D. Batt. Oxidation of polyols by Nocardia corallina. J. Bacteriol. 83:1131–1139. 1962.—Two diphosphopyridine nucleotide-linked polyol dehydrogenases were induced in Nocardia corallina strain S, and grown on either mannitol or sorbitol. One enzyme was labile and was specific for the conversion of sorbitol to d-fructose.
The second enzyme, which converted d-mannitol to d-fructose and, more slowly, d-arabitol to d-xylulose, was named the d-mannitol dehydrogenase. The configurations of the hydroxyl groups at carbons 2, 3, 4, and 5 of substrates for this enzyme were stereospecific. Formation of the enzyme was induced by d-mannitol and d-sorbitol but not by d-arabitol.
Extracts of cells grown on either mannitol or sorbitol catalyzed the oxidation of the reduced form of diphosphopyridine nucleotide in the presence of d-fructose and d-xylulose.
Cell suspensions of the organism oxidized mannitol, sorbitol, glycerol, inositol, and fructose but not dulcitol, d-arabitol, d-xylulose, or l-sorbose.
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Selected References
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