Article
Structural basis for the inhibition of 1,3-1,4-β-D-glucanase by noncompetitive calcium ion and competitive Tris inhibitors.
Biochemical and biophysical research communications - 15 Apr 2011
Tsai Li-Chu, Hsiao Ching-Hua, Liu Wen-Yan, Yin Li-Ming, Shyur Lie-Fen
Abstract excerpt
In this paper, we determine the mutant W203F structure of TFsβ-glucanase, which contains aromatic residue Trp203 at the active site of the enzyme. Residue Trp203 is stacked with the glucose product of cellotriose. Further analysis reveals that two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of Glu56 and Glu60, was found at the position...
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