Affiliation:
1. Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University, New York, New York 10461
Abstract
A mutant of
Gluconobacter cerinus
var.
ammoniacus
, IFO 3267, has been isolated which is deficient with respect to fructose 5-dehydrogenase, the enzyme catalyzing the oxidation of
d
-fructose to 5-keto-
d
-fructose (5 KF). Growth of this mutant on fructose as the sole carbon source was impaired unless the culture medium was supplemented with 5 KF. Significant randomization of the 1 and 6 positions of fructose has been reported previously for the wild-type organism during growth on this ketohexose. The pattern of
3
H incorporation into the C5 position of ribonucleic acid-ribose when the mutant was grown on [1-
3
H]fructose and [6-
3
H]fructose in the presence of 5 KF indicated that such randomization did not occur in this variant. The randomization observed in the wild type is, therefore, a consequence of the partial oxidation of fructose to the symmetrical 5 KF intermediate prior to its conversion to pentose. When the mutant was grown on [1-
3
H]fructose in the presence of unlabeled 5 KF, [5-
3
H]fructose appeared in the culture medium. Thus, 5 KF served as the oxidant for the nicotinamide adenine dinucleotide phosphate, reduced form, generated during growth on fructose.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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