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J Bacteriol. 1968 March; 95(3): 932-936
Copyright © 1968 American Society for Microbiology. All Rights Reserved.
1 Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01002
ABSTRACT
The incubation of Aerobacter aerogenes PRL-R3 with ribitol resulted in the induction of ribitol dehydrogenase and D-ribulokinase, coordinately controlled enzymes of the pathway of ribitol catabolism. A dehydrogenase-negative mutant was unable to induce D-ribulokinase activity following incubation with ribitol. Similar experiments using a kinase-negative mutant resulted in normal induction of ribitol dehydrogenase, as compared to the wild-type PRL-R3 strain. Constitutive or induced cells for L-fucose isomerase were capable of catalyzing the isomerization of D-arabinose to D-ribulose. In contrast to the experiments using ribitol as the substrate, the isomerization of D-arabinose resulted in the induction of D-ribulokinase with dehydrogenase-negative cells. These data indicated that D-ribulose, rather than ribitol, acts as the inducer of the enzymes for ribitol degradation.
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