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Metabolism of Gentiobiose in Aerobacter aerogenes

Department of Biochemistry, Michigan State University, East Lansing, Michigan 48823

ABSTRACT

Cleavage of gentiobiose in cell extracts of gentiobiose-grown Aerobacter aerogenes was dependent on the presence of adenosine 5'-triphosphate (ATP). The enzymes that participate in the overall reaction were shown to be a ß-glucoside kinase, which catalyzes the phosphorylation of gentiobiose with ATP to form gentiobiose monophosphate [6-O-phosphoryl-ß-D-glucopyranosyl-(1 6)-D-glucose], and a phospho-ß-glucosidase, which catalyzes the hydrolytic cleavage of gentiobiose monophosphate to form equimolar amounts of D-glucose and D-glucose 6-phosphate. Although the ß-glucoside kinase was previously shown to catalyze the phosphorylation of many ß-glucosides that serve as growth substrates (i.e., gentiobiose, cellobiose, cellobiitol, salicin, arbutin, methyl ß-D-glucoside, and phenyl ß-D-glucoside), mutant analysis and induction studies indicate that it functions only in the metabolism of gentiobiose, cellobiose, and cellobiitol.