Subsite Structure of Exo-1, 4-β-Glucosidase from Acetobacter xylinum BPR2001
スポンサーリンク
概要
- 論文の詳細を見る
The Michaelis constant(K_m)and molecular activity(k_0)of an exo-1, 4-β-glucosidase(EC3. 2. 1. 74)from Acetobacter xylinum subsp. sucrofermentans BPR2001 for hydrolysis of cello-oligosaccharides(G2-G6)were determined by steady-state kinetic analysis. The 1/K_m and k_0 values for G2 were much lower than those for G3-G6. The enzyme was competitively inhibited by glucono-δ-lactone and conduritol-β epoxide. Based on the theory of Hiromi et al. (Biochim. Biophys. Acta, 302 : 362-375, 1973), the subsite affinities(A_i=1-6)and the intrinsic hydrolysis rate constant for substrate linkage in a productive complex(k_<int>of the enzyme were kinetically estimated: A_1=2.46kcal/mol, A_2=-0.44kcal/mol, A_3=3.70kcal/mol, A_4=0.33kcal/mol, A_5=0.27kcal/mol, A_6=0.06kcal/mol, and k_<int>=33.4S^<-1>. The subsite affinities were different from thos for the β-glucosidase from Aspergillus niger and for the exo-1, 4-β-glucosidase from Torulopsis wickerhamii, in that the A_2 value for the Acetobacter enzyme was negative. These results suggest that the enzyme possesses subsite affinities which have never previously been reported among exo-type glucosidase.
- 社団法人日本生物工学会の論文
- 1998-06-25
著者
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Tahara N
Wood Research Institute Kyoto University
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Nakai Tomonori
Wood Research Inst. Kyoto Univ.
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YANO HISATO
Bio-Polymer Research Co. Ltd.,
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YOSHINAGA FUMIHIRO
Bio-Polymer Research Co. Ltd.,
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TAHARA NAOKI
Bio-Polymer Research Co., Ltd.
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Yano Hisato
Bio-polymer Research Co. Ltd. Ksp R&d Business-park Bldg
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Yoshinaga F
Bio-polymer Research Co. Ltd.
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Yoshinaga Fumihiro
Bio-polymer Research Co. Ltd.
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Yano Hisato
Bio-Polymer Research Co. Ltd. , KSP R&D Business-Park Bldg
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