Enzymatic Characteristics of Cellobiose Phosphorylase from <I>Ruminococcus albus</I> NE1 and Kinetic Mechanism of Unusual Substrate Inhibition in Reverse Phosphorolysis
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概要
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Cellobiose phosphorylase (CBP) catalyzes the reversible phosphorolysis of cellobiose to produce α-D-glucopyranosyl phosphate (Glc1<I>P</I>) and D-glucose. It is an essential enzyme for the metabolism of cello-oligosaccharides in a ruminal bacterium, <I>Ruminococcus albus</I>. In this study, recombinant <I>R. albus</I> CBP (RaCBP) produced in <I>Escherichia coli</I> was characterized. It showed highest activity at pH 6.2 at 50 °C, and was stable in a pH range of 5.5–8.8 and at below 40 °C. It phosphorolyzed only cellobiose efficiently, and the reaction proceeded through a random-ordered bi bi mechanism, by which inorganic phosphate and cellobiose bind in random order and D-glucose is released before Glc1<I>P</I>. In the synthetic reaction, RaCBP showed highest activity to D-glucose, followed by 6-deoxy-D-glucose. D-Mannose, 2-deoxy-D-glucose, D-glucosamine, D-xylose, 1,5-anhydro-D-glucitol, and gentiobiose also served as acceptors, although the activities for them were much lower than for D-glucose. D-Glucose acted as a competitive-uncompetitive inhibitor of the reverse synthetic reaction, which bound not only the Glc1<I>P</I> site (competitive) but also the ternary enzyme-Glc1<I>P</I>-D-glucose complex (uncompetitive).
著者
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MATSUI Hirokazu
Research Faculty of Agriculture, Hokkaido University
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Mori Haruhide
Research Faculty Of Agriculture Hokkaido University
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Saburi Wataru
Research Faculty Of Agriculture Hokkaido University
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Morimoto Naoki
Research Faculty Of Agriculture Hokkaido University
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TAGUCHI Hidenori
Research Faculty of Agriculture, Hokkaido University
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Hamura Ken
Research Faculty Of Agriculture Hokkaido University
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Abe Shotaro
Research Faculty Of Agriculture Hokkaido University
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