Results 21 to 30 of about 3,083 (198)
Two distinct catalytic pathways for GH43 xylanolytic enzymes unveiled by X-ray and QM/MM simulations
Nature Communications, 2021 Family 43 glycoside hydrolases (GH43) are involved in the breakdown of hemicellulose. Functional, structural and computational characterization of a GH43 enzyme, including a snapshot of an active Michaelis complex, reveal the hydrolysis mechanism and ...
Mariana A. B. Morais +9 more
doaj +1 more source
Structure of a member of glycoside hydrolase family 61: are these true glycoside hydrolases? [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2008 n ...
Lo Leggio, L. +7 more
openaire +2 more sources
Annotation and comparative analysis of the glycoside hydrolase genes in
BMC Genomics, 2010 Background Glycoside hydrolases cleave the bond between a carbohydrate and another carbohydrate, a protein, lipid or other moiety. Genes encoding glycoside hydrolases are found in a wide range of organisms, from archea to animals, and are relatively ...
Wu Jiajie +5 more
doaj +1 more source
Functional exploration of the glycoside hydrolase family GH113 [PDF]
PLOS ONE, 2022 β-Mannans are a heterogeneous group of polysaccharides with a common main chain of β-1,4-linked mannopyranoside residues. The cleavage of β-mannan chains is catalyzed by glycoside hydrolases called β-mannanases. In the CAZy database, β-mannanases are grouped by sequence similarity in families GH5, GH26, GH113 and GH134.
Couturier, Marie +7 more
openaire +5 more sources
Detecting and identifying glycoside hydrolases using cyclophellitol-derived activity-based probes
, 2022 The ability to detect active enzymes in a complex mixture of folded proteins (e.g., secretome, cell lysate) generally relies on observations of catalytic ability, necessitating the development of an activity assay that is compatible with the sample and ...
Overkleeft, H.S. +5 more
core +2 more sources
Frontiers in Microbiology, 2016 The detailed lifestyle of microorganisms in deep-sea brine environments remains largely unexplored. Using a carefully calibrated genome binning approach, we reconstructed partial to nearly-complete genomes of 51 microorganisms in biofilms from the Thuwal
Weipeng Zhang +6 more
doaj +1 more source
Engineering the stability and the activity of a glycoside hydrolase [PDF]
Protein Engineering Design and Selection, 2010 Glycosidases, the enzymes responsible in nature for the catabolism of carbohydrates, are well-studied catalysts widely used in industrial biotransformations and oligosaccharide synthesis, which are also attractive targets for drug development. Glycosidases from hyperthermophilic organisms (thriving at temperatures > 85 °C) are also interesting models ...
CobucciPonzano Beatrice +3 more
openaire +4 more sources
, 2020 Lignocellulolytic and chitinolytic glycoside hydrolases are commonly used enzymes in commercial processes and thus are well documented for their vital role in agriculture, textile, paper, food, biofuel and healthcare sectors. Ongoing research is targeted
Chawade, Aakash, +2 more
core +1 more source
Disaccharide phosphorylases: Structure, catalytic mechanisms and directed evolution
Synthetic and Systems Biotechnology, 2021 Disaccharide phosphorylases (DSPs) are carbohydrate-active enzymes with outstanding potential for the biocatalytic conversion of common table sugar into products with attractive properties. They are modular enzymes that form active homo-oligomers. From a
Shangshang Sun, Chun You
doaj +1 more source
Allylic Carbocyclic Inhibitors Covalently Bind Glycoside Hydrolases [PDF]
, 2023 Allylic cyclitols were investigated as covalent inhibitors of glycoside hydrolases by chemical, enzymatic, proteomic, and computational methods. This approach was inspired by the C7 cyclitol natural product streptol glucoside, which features a potential ...
Tatyana D. Grayfer (1415323) +11 more
core +2 more sources