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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