Glycosidase mechanisms: anatomy of a finely tuned catalyst.

By David L. Zechel and, S. Withers. 1999

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Citations in the corpus

Dissecting enzyme function with microfluidic-based deep mutational scanning (2015, background): “We hypothesize that N307 may act to shift the pKa of the general acid/base, which is crucial for the pKa-cycling mechanism of most retaining glycosidases (19).”
Xylanases, xylanase families and extremophilic xylanases. (2005, background): “[52] Zechel, D.”
Chitin Metabolism in Insects (2012, background): “Mechanistically, chitinases of family 18 hydrolyze chitin with retention of the anomeric configuration at the cleavage site, involving a double-displacement mechanism where a substrate-assisted catalysis occurs (Tomme et al., 1995; Henrissat, 1999; Zechel and Withers, 2000; Brameld et al., 2002).”
A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. (2001, background): “Numerous reviews of their structure, function and catalytic mechanisms are available (Sinnott, 1990; McCarter and Withers, 1994; Davies and Henrissat, 1995; Zechel and Withers, 2000).”
α-l-Arabinofuranosidases: the potential applications in biotechnology (2006, background): “Like other glycoside hydrolases, a-L-AFases mediate glycosidic bond cleavage via acid/base-assisted catalysis employing two major mechanisms, giving rise to either an overall retention or an inversion of the anomeric configuration [26, 136].”
β-Xylosidases from filamentous fungi: an overview (2010, background): “In the second step (deglycosylation), the acid–base catalytic group deprotonates the incoming water molecule, which then attacks at the anomeric center of the substrate while displacing the sugar (Davies et al. 1998; Zechel and Withers 2000).”
Microbial β-Glucosidase: Sources, Production and Applications (2017, background): “In the deglycosylation step, a water molecule attacks enzyme-glycosyl intermediate to displace the catalytic nucleophile from the glucose with basic assistance of the catalytic acid/base [109,110,111].”
Cloning of β-Primeverosidase from Tea Leaves, a Key Enzyme in Tea Aroma Formation1 (2002, background): “Glycosyl hydrolases in family 1 are known to be retaining glycosidases, which catalyze the hydrolysis of the substrates with retaining the anomeric configuration by a double-displacement mechanism through a glucosyl-enzyme covalent intermediate (Zechel and Withers, 2000).”