Affiliation:
1. Instituto de Investigación de Ciencias Biológicas, Department of Biochemistry, Montevideo, Uruguay
Abstract
The utilization of
d
-mannitol,
d
-arabitol, and
d
-sorbitol by
Rhizobium meliloti
was studied in extracts from mannitol-grown cells. Two different polyol dehydrogenases were induced by any of these polyols: (i) a nicotinamide adenine dinucleotide (NAD)-arabitol dehydrogenase and (ii) a NAD-sorbitol dehydrogenase, whereas polyol phosphate dehydrogenases were absent.
d
-Arabitol dehydrogenase was observed to act on both
d
-arabitol and
d
-mannitol, but
d
-sorbitol dehydrogenase acted specifically on
d
-sorbitol.
d
-Arabitol was oxidized to
d
-xylulose,
d
-mannitol and
d
-sorbitol were oxidized to
d
-fructose. An adenosine triphosphate-linked hexokinase which acts on
d
-fructose and absence of hexose isomerase were also detected in this organism.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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