Phosphorolytic Reaction of Cellvibrio gilvus Cellobiose Phosphorylase
スポンサーリンク
概要
- 論文の詳細を見る
Cellobiose phosphorylase was purified from Cellvibrio gilvus cells by the method reported previously with some modifications, and its kinetic properties were studied in detail. The initial velocity of the synthetic reaction was 1.4 times as fast as that of the phosphorolytic one. The equilibrium constant of the phosphorolysis was 0.32 at 37℃ and pH 7.0. No D-[U-^<14>C] glucose exchange reaction was observed in the absence of Pi. Kinetic studies on the phosphorolytic reaction showed that the reaction follows an ordered bi bi mechanism. These results make a sharp contrast to those of sucrose phosphorylase, which catalyzes fructose exchange reaction and follows a ping pong bi bi mechanism. Kinetic parameters were calculated as K_<mA>=2.6mM, K_<mB>=0.61 mM, and K_<iA>=6.8 mM (A, D-cellobiose ; B, Pi).
- 社団法人日本農芸化学会の論文
- 1992-04-23
著者
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Kitaoka Motomitsu
National Food Research Institute, National Agriculture and Food Research Organization
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Sawa T
Institute Of Microbial Chemistry
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Kitaoka M
Enzyme Laboratory National Food Research Institute
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Kitaoka M
Chubu Univ. Aichi Jpn
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Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute National Agriculture And Food Research Organizati
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Sasaki Takashi
National Food Research Institute
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Taniguchi Hajime
National Food Research Institute
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KITAOKA Motomitsu
Nippon Petrochemicals Co., Ltd.
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Kitaoka Motomitsu
Department Of Biological Chemistry Chubu University
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Taniguchi H
Yamaguchi Univ. Yamaguchi Jpn
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Taniguchi Hajime
National Food Research Insitute, Ministry of Agricultuer, Forestry and Fisheries
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