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J Bacteriol. 1965 May; 89(5): 1186-1194
Copyright © 1965 American Society for Microbiology. All Rights Reserved.

Enzymatic Basis for D-Arabitol Production by Saccharomyces rouxii¹

^a Department of Biochemistry, Michigan State University, East Lansing, Michigan

ABSTRACT

INGRAM, JORDAN M. (Michigan State University, East Lansing), AND W. A. WOOD. Enzymatic basis for D-arabitol production by Saccharomyces rouxii. J. Bacteriol. 89:1186–1194. 1965.—The enzymatic steps in D-arabitol synthesis by Saccharomyces rouxii were studied. The fermentation of D-glucose-6-C¹⁴ gave rise to D-arabitol labeled at C-5; D-ribose of ribonucleic acid had the same isotope pattern. Crude extracts were able to reduce D-ribulose with reduced nicotinamide adenine dinucleotide phosphate (NADPH₂) and D-xylulose with reduced nicotinamide adenine dinucleotide (NADH₂). These extracts also oxidized D-arabitol with nicotinamide adenine dinucleotide phosphate and xylitol with nicotinamide adenine dinucleotide. No reduction of D-ribulose-5-phosphate or D-xylulose-5-phosphate was observed. An enzyme which reduced D-xylulose with NADH₂ was purified 33-fold and characterized as a xylitol ( D-xylulose) dehydrogenase. Similarly, an enzyme reducing D-ribulose with NADPH₂ was purified 12-fold and characterized as a D-arabitol ( D-ribulose) dehydrogenase. Alkaline and acid phosphatases were purified 50- and 40-fold, respectively, and their specificities were determined. Only the acid phosphatase had detectable activity on D-ribulose-5-phosphate. The data support the postulate that D-arabitol arises by dephosphorylation of D-ribulose-5-phosphate and reduction of D-ribulose by a NADPH₂-linked D-arabitol ( D-ribulose) dehydrogenase.

¹ Contribution No. 3520 of the Michigan Agricultural Experiment Station.

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