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J Bacteriol. 1971 January; 105(1): 232-240
Copyright © 1971 American Society for Microbiology. All Rights Reserved.
1 Department of Biochemistry, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104
ABSTRACT
A biochemical and genetic analysis of D-mannitol metabolism in Salmonella typhimurium indicates that D-mannitol is phosphorylated by the phosphoenolpyruvate-dependent phosphotransferase system. D-Mannitol-1-phosphate is converted to D-fructose-6-phosphate by mannitol-1-phosphate dehydrogenase. Two classes of mannitol mutants are described. Both map at about 115 min on the Salmonella chromosome. Mutants missing mannitol-1-phosphate dehydrogenase activity are mannitol sensitive; i.e., either growth is inhibited or the cells are lysed in the presence of mannitol. In a strain missing adenyl cyclase activity, the mannitol genes require exogenous cyclic adenosine-3',5'-monophosphate for expression.
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