Affiliation:
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
21 articles.
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