Author's Organization:Bio-Polymer Research Co., Ltd. Bio-Polymer Research Co., Ltd. Bio-Polymer Research Co., Ltd. Department of Biotechnology, Division of Agriculture and Life Sciences, The University of Tokyo Department of Biotechnology, Division of Agriculture and Life Sciences, The University of Tokyo:Department of Applied Biological Science, Nihon University
For characterization of the biosynthetic pathway of cellulose in a cellulose-producing Acetobacter xylinum strain BPR2001, the activities of several enzymes were measured. The activity of phosphoglucose isomerase catalyzing the conversion of fructose-6-phosphate into glucose-6-phosphate was greatly increased by fructose in the medium. The UDP-glucose pyrophosphorylase activity catalyzing the synthesis of UDP-glucose was very high in strain BPR2001, consistent with the idea that this is the key enzyme in cellulose biosynthesis. Strain BPR2001 was found to have a fructose-specific phosphoenolpyruvate-dependent phosphotransferase system (PTS).
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