[Review] Crystal Structure Analysis of β-Amylase/Saccharide Complexes Measured at Different pH and Room Temperature.

  • Mikami Bunzo
    Laboratory of Metabolic Science of Forest Plants and Microorganisms, Division of Diagnostics and Control of the Humanosphere, Research Institute for Sustainable Humanosphere, Kyoto University Structural Energy Bioscience Research Section, Division of Advanced Energy Utilization, Institute of Advanced Energy, Kyoto University
  • Adachi Motoyasu
    Institute for Quantum Life Science, National Institute for Quantum and Radiological Science and Technology
  • Mizutani Kimihiko
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • Takahashi Nobuyuki
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • Kang You-Na
    Laboratory of Food Quality Design and Development, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University
  • Hirata Akira
    Laboratory of Food Quality Design and Development, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University
  • Yamane Aiko
    Laboratory of Food Quality Design and Development, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University
  • Saka Naoki
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • Kawamura Hirokazu
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • Hou Xueni
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University
  • Mori Kotaro
    Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University

Bibliographic Information

Other Title
  • 【総説:応用糖質科学シンポジウム】 非凍結結晶を用いたβ-アミラーゼと基質アナログ複合体構造のpH変化の解析

Abstract

<p>凍結結晶法によるX線結晶構造解析では凍結の影響や凍結保護剤の問題があり,結晶中での酵素の構造変化を正しく評価することは困難である.酵素と基質(基質アナログ)複合体のpH変化による構造変化を調べることは,酵素反応前後の構造変化を捉えることに繋がる.著者らはβ-アミラーゼの酵素反応機構を明らかにするために本酵素の基質アナログであるグルコース,マルトースと基質であるマルトペンタオースを用いて,野生型酵素と変異体酵素について非凍結結晶の結晶中でのpH変化による複合体構造の変化を追跡した.その結果,触媒残基の二つのGlu残基(酸触媒残基であるGlu186と塩基触媒残基であるGlu380)の解離が酵素と基質の構造変化に大きく関わり,本酵素反応を高効率化していることを明らかにした.</p>

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