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Influence of Molecular Structures of Substrates and Analogues on Taka-amylase A Catalyzed Hydrolyses:I. Effect of Chain Length of Linear Substrates
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- NITTA Yasunori
- The Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
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- MIZUSHIMA Minoru
- The Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
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- HIROMI Keitaro
- The Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
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- ONO Sôzaburo
- The Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
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Description
1) Hydrolyses of linear maltodextrins (DP 2--DPn 117) catalyzed by crystalline Taka-amylase A [EC 3. 2. 1. 1] were studied at pH 5.3 and 25°C to determine the rate parameter for each substrate.<br> 2) Michaelis constant, Km (in moler basis), decreased with increasing chain length (n) of glucose unit. Turnover number, V/(E)0, increased with chain length up to n=7 and became practically constant for n more than 7, which suggests that the specificity region of Taka-amylase A spans about 7 glucose units.<br> 3) The dependence of Km and V/(E)0 on chain length of substrate was interpreted in terms of the probability of formation of productive and nonproductive ES-complexes. Based on the assumption that the breakdown rate constant in productive ES-complex, kint, is constant irrespective of chain length of substrate and binding mode, magnitudes of subsite affinities (in free energy units) in the active site were evaluated from the values of V/Km (E)0 for various substrates. Results suggested the presence of a distortion in the productive ES complex.
Journal
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- J Biochem (Tokyo)
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J Biochem (Tokyo) 69 (3), 567-576, 1971
The Japanese Biochemical Society
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Details 詳細情報について
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- CRID
- 1570291228197499520
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- NII Article ID
- 130003538473
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- ISSN
- 0021924X
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- Text Lang
- en
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- Data Source
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- CiNii Articles