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Catalytic strategies of glycoside hydrolases
2018Glycoside hydrolases (GHs) are enzymes that catalyze the hydrolysis of the glycosidic bond between two carbohydrate residues or a carbohydrate unit linked to a non-carbohydrate aglycon unit. Despite years of research dedicated to GHs, there are still several mechanistic details, relevant for individual GH enzymes, that remain to be investigated.
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Structural and sequence-based classification of glycoside hydrolases
Current Opinion in Structural Biology, 1997The diversity of oligo- and polysaccharides provides an abundance of biological roles for these carbohydrates. The enzymes hydrolysing these compounds, the glycoside hydrolases, therefore mediate a wealth of biological functions. Glycoside hydrolases fall into a number of sequence-based families.
Henrissat, Bernard, Davies, G.
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Purification of some glycoside hydrolases by affinity chromatography
Carbohydrate Research, 1977Two glycoproteins have been isolated from the cell walls of baker's yeast. One is a glucan-protein complex which has been partially characterised as having a branched carbohydrate structure composed of chains of (1 leads to 3)-linked beta-D-glucosyl residues, some of which are attached by (1 leads to 6)-linkages to the main chain.
Michael Edward, Robert J. Sturgeon
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A GLYCOSIDE-HYDROLASE INHIBITOR IN TREATMENT OF DUMPING SYNDROME
The Lancet, 1979BAY g 5421, a glycoside-hydrolase inhibitor, produced symptomatic improvement in ten patients with the dumping syndrome. 100 mg BAY g 5421, given before a 50 g sucrose meal, produced pronounced attenuation of both hyperglycaemic and hypoglycaemic phases of plasma glucose levels; and it greatly reduced the rise in plasma levels of gastric inhibitory ...
M.J. Alam +2 more
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Modeling catalytic reaction mechanisms in glycoside hydrolases
Current Opinion in Chemical Biology, 2019Modeling catalysis in carbohydrate-active enzymes is a daunting challenge because of the high flexibility and diversity of both enzymes and carbohydrates. Glycoside hydrolases (GHs) are an illustrative example, where conformational changes and subtle interactions have been shown to be critical for catalysis.
Lluís Raich +3 more
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Cln5 is secreted and functions as a glycoside hydrolase in Dictyostelium
Cellular Signalling, 2018Ceroid lipofuscinosis neuronal 5 (CLN5) is a member of a family of proteins that are linked to neuronal ceroid lipofuscinosis (NCL). This devastating neurological disorder, known commonly as Batten disease, affects all ages and ethnicities and is currently incurable. The precise function of CLN5, like many of the NCL proteins, remains to be elucidated.
Robert J. Huber +1 more
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Glycoside hydrolases and glycosyltransferases: families and functional modules
Current Opinion in Structural Biology, 2001The past year has witnessed the expected increase in the number of solved structures of glycoside hydrolases and glycosyltransferases, and their constitutive modules. These structures show that, while glycoside hydrolases display an extraordinary variety of folds, glycosyltransferases and carbohydrate-binding modules appear to belong to a much smaller ...
Bernard Henrissat, Yves Bourne
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Phylogenetic analysis of family 6 glycoside hydrolases
Biopolymers, 2005AbstractMultiple sequence alignment separates members of glycoside hydrolase Family 6 into eight subfamilies: one of mainly actinobacterial endoglucanases (EGs), one of ascomycotal EGs, one of chytridiomycotal EGs and cellobiohydrolases (CBHs), one of actinobacterial and proteobacterial CBHs, one of chytridiomycotal CBHs, two of ascomycotal CBHs, and ...
Anthony D. Hill +4 more
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Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles
2001Publisher Summary Glycoside hydrolases and glycosyltransferases are widespread groups of carbohydrate-active enzymes present in virtually all organisms and are involved, respectively, in the hydrolysis and in the biosynthesis of glycosidic bonds between carbohydrates or between a carbohydrate and a noncarbohydrate moiety.
Bernard Henrissat, Pedro M. Coutinho
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Immunization with Dextransucrases and Glycosidic Hydrolases
Journal of Dental Research, 1972Arthur N. Bahn +2 more
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