Article
Positioning the acid/base catalyst in a glycosidase: studies with Bacillus circulans xylanase.
Biochemistry - 25 Feb 1997
Lawson S L, Wakarchuk W W, Withers S G
Abstract excerpt
The mechanism of action employed by a glycosidase is dictated, in part, by the distance between the two catalytic carboxylic acids. In the retaining endo-beta-1,4-xylanase from Bacillus circulans, this critical distance (approximately 5.5 A) has been altered by mutagenesis of the putative acid/base catalyst Glu172. An increase in the separation (Glu172Asp) resulted in a 400-fold decrease in the k(cat) value for...
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