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Hierarchical classification of glycoside hydrolases

Biochemistry (Moscow), 2011
This review deals with structural and functional features of glycoside hydrolases, a widespread group of enzymes present in almost all living organisms. Their catalytic domains are grouped into 120 amino acid sequence-based families in the international classification of the carbohydrate-active enzymes (CAZy database).
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Bioprospecting Metagenomics for New Glycoside Hydrolases

2012
To efficiently deconstruct recalcitrant plant biomass to fermentable sugars in industrial processes, biocatalysts of higher performance and lower cost are required. The genetic diversity found in the metagenomes of natural microbial biomass decay communities may harbor such enzymes.
Jack, Gilbert   +5 more
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Diversity of phosphorylases in glycoside hydrolase families

Applied Microbiology and Biotechnology, 2015
Phosphorylases are useful catalysts for the practical preparation of various sugars. The number of known specificities was 13 in 2002 and is now 30. The drastic increase in available genome sequences has facilitated the discovery of novel activities.
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GLYCOSIDE HYDROLASES IN APLYSIA FASCIATA: ANALYSIS AND APPLICATIONS

Biotechnology and Genetic Engineering Reviews, 2008
Glycosylation is considered to be an important reaction for the chemical modification of compounds with useful biological activities. Glycoside hydrolases are biotechnologically attractive enzymes which can be used in synthetic reactions for assembling glycosidic linkages with absolute stereoselectivity at an anomeric centre.
A Trincone   +3 more
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Structural and sequence-based classification of glycoside hydrolases

Current Opinion in Structural Biology, 1997
The 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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Modeling catalytic reaction mechanisms in glycoside hydrolases

Current Opinion in Chemical Biology, 2019
Modeling 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.
Joan, Coines   +2 more
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Cln5 is secreted and functions as a glycoside hydrolase in Dictyostelium

Cellular Signalling, 2018
Ceroid 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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Family 4 glycoside hydrolases are special: The first β-elimination mechanism amongst glycoside hydrolases

Biocatalysis and Biotransformation, 2006
The glycoside hydrolases are a large group of enzymes that can be grouped into two major mechanistic classes based upon the stereochemical outcome of catalysis: retention and inversion of sugar anomeric configuration. Both mechanisms involve nucleophilic displacement at the anomeric center, and both proceed via positively charged oxocarbenium ion-like ...
Vivian L Y. Yip, Stephen G. Withers
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Catalytic strategies of glycoside hydrolases

2018
Glycoside 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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Immunization with Dextransucrases and Glycosidic Hydrolases

Journal of Dental Research, 1972
J A, Hayashi, I L, Shklair, A N, Bahn
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