Acceptor-dependent regioselectivity of glycosynthase reactions by Streptomyces E383A β-glucosidase

…, M Saura-Valls, X Pérez, M Conti, A Planas

Index: Faijes, Magda; Saura-Valls, Marc; Perez, Xavi; Conti, Marta; Planas, Antoni Carbohydrate Research, 2006 , vol. 341, # 12 p. 2055 - 2065

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Citation Number: 33

Abstract

The nonnucleophilic mutant E383A β-glucosidase from Streptomyces sp. has proven to be an efficient glycosynthase enzyme, catalyzing the condensation of α-glucosyl and α- galactosyl fluoride donors to a variety of acceptors. The enzyme has maximal activity at 45° C, and a pH-dependence reflecting general base catalysis with an apparent kinetic pKa of 7.2. The regioselectivity of the new glycosidic linkage depends unexpectedly on the ...

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