Structure and Catalytic Implications of Taka-Amylase A

Y. Matsuura, M. Kusunoki, M. Kakudo
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引用次数: 13

Abstract

Taka-amylase has a (αβ)8 barrel structure and the active site is located at the C-terminal end of a β-strand as reported earlier. In this paper, we describe about the direction of substrate amylose binding with respect to the barrel structure. A possible mechanism of hydrolysis is also proposed, in which Glu 230, Asp 297 and Asp 206 located near the active site are essentially involved.
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塔卡淀粉酶A的结构及其催化意义
taka -淀粉酶具有(αβ)8桶状结构,活性位点位于β链的c端。在本文中,我们描述了相对于桶状结构的底物直链淀粉结合的方向。本文还提出了一种可能的水解机制,其中位于活性位点附近的Glu 230、Asp 297和Asp 206主要参与了水解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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