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Physiological roles of plant glycoside hydrolases
Planta, 2007The functions of plant glycoside hydrolases and transglycosidases have been studied using different biochemical and molecular genetic approaches. These enzymes are involved in the metabolism of various carbohydrates containing compounds present in the plant tissues. The structural and functional diversity of the carbohydrates implies a vast spectrum of
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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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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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Catalytic strategies of glycoside hydrolases [PDF]
, 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.
Petersen, Luis
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Glycoside hydrolases: Catalytic base/nucleophile diversity
Biotechnology and Bioengineering, 2010AbstractRecent studies have shown that a number of glycoside hydrolase families do not follow the classical catalytic mechanisms, as they lack a typical catalytic base/nucleophile. A variety of mechanisms are used to replace this function, including substrate‐assisted catalysis, a network of several residues, and the use of non‐carboxylate residues or ...
Thu V, Vuong, David B, Wilson
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Bifidobacterium glycoside hydrolases and (potential) prebiotics
Innovative Food Science and Emerging Technologies, 2008 Carbohydrates occur in food as natural constituents or are added as ingredients. In the last decade a number of novel dietary carbohydrates have been introduced as ingredients for food applications, responding to the growing awareness among consumers of ...
L A M van den Broek +1 more
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Twisting of glycosidic bonds by hydrolases
Carbohydrate Research, 2009Patterns of scissile bond twisting have been found in crystal structures of glycoside hydrolases (GHs) that are complexed with substrates and inhibitors. To estimate the increased potential energy in the substrates that results from this twisting, we have plotted torsion angles for the scissile bonds on hybrid Quantum Mechanics::Molecular Mechanics ...
Johnson, Glenn +3 more
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Formation of glycoside-hydrolases by oral streptococci
Archives of Oral Biology, 1973Abstract The formation of glycoside-hydrolases by oral streptococci grown in different substrates under different conditions was investigated. A proteose peptone medium was superior to brain-heart infusion broth and Todd-Hewitt broth for production of all enzymes.
C E, Nord +3 more
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Strategies for tailoring pH performances of glycoside hydrolases
Critical Reviews in Biotechnology, 2021Glycoside hydrolases (GHs) exhibit high activity and stability under harsh conditions, such as high temperatures and extreme pHs, given their wide use in industrial biotechnology. However, strategies for improving the acidophilic and alkalophilic adaptations of GHs are poorly summarized due to the complexity of the mechanisms of these adaptations. This
Shu-Fang, Li +3 more
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Hierarchical classification of glycoside hydrolases
Biochemistry (Moscow), 2011This 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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