Affiliation:
1. 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-C
14
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 (NADPH
2
) and
d
-xylulose with reduced nicotinamide adenine dinucleotide (NADH
2
). 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 NADH
2
was purified 33-fold and characterized as a xylitol (→
d
-xylulose) dehydrogenase. Similarly, an enzyme reducing
d
-ribulose with NADPH
2
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 NADPH
2
-linked
d
-arabitol (→
d
-ribulose) dehydrogenase.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference33 articles.
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