Article
Mutations on aromatic residues of the active site to alter selectivity of the Sulfolobus solfataricus maltooligosyltrehalose synthase.
Journal of agricultural and food chemistry - 17 May 2006
Fang Tsuei-Yun, Tseng Wen-Chi, Chung Yao-Te, Pan Ching-Hsing
Abstract excerpt
Mutations Y290F, Y367F, F405Y, and Y409F located near subsite +1 were constructed in maltooligosyltrehalose synthase (MTSase) to alter the selectivity of the enzyme. These mutations were designed to evaluate the effects of hydrophobic interactions and/or hydrogen bondings on transglycosylation and side hydrolysis reactions. The catalytic efficiencies of Y290F MTSase for hydrolysis and transglycosylation reactions...
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