Results 151 to 160 of about 10,058 (190)
Comparison of active site mutations at subsite + 2 of Anoxybacillus ayderensis A9 β-glucosidase for hydrolysis of pNPG and polydatin. [PDF]
BMC BiotechnolZada NS +8 more
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A snapshot into the uptake and utilization of potential oligosaccharide prebiotics by probiotic lactobacilli and bifidobacteria as accessed by transcriptomics, functional genomics, and recombinant protein characterization [PDF]
, 2012 Andersen, Joakim Mark
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Recent advances in S-palmitoylation and its emerging roles in human diseases. [PDF]
J Hematol OncolShang J, Ding M, Zhou X.
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Transcriptomic insights into arabinogalactan protein mechanism of action in galactosyltransferase octuple mutants. [PDF]
Front Plant SciAyorinde DA +2 more
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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 ...
J C, McLoughlin +2 more
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Journal of the American Chemical Society, 2017
The design of covalent inhibitors in glycoscience research is important for the development of chemical biology probes. Here we report the synthesis of a new carbocyclic mechanism-based covalent inhibitor of an α-glucosidase. The enzyme efficiently catalyzes its alkylation via either an allylic cation or a cationic transition state.
Saeideh Shamsi Kazem Abadi +5 more
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The design of covalent inhibitors in glycoscience research is important for the development of chemical biology probes. Here we report the synthesis of a new carbocyclic mechanism-based covalent inhibitor of an α-glucosidase. The enzyme efficiently catalyzes its alkylation via either an allylic cation or a cationic transition state.
Saeideh Shamsi Kazem Abadi +5 more
openaire +4 more sources
Biotechnology Advances, 2018
Glycoside hydrolase family 20 β-N-acetyl-d-hexosaminidases (GH20s) catalyze the hydrolysis of glycosidic linkages in glycans, glycoproteins and glycolipids. The diverse substrates of GH20s account for their various roles in many important bioprocesses, such as glycoprotein modification, glycoconjugate metabolism, gamete recognition and chitin ...
Tian Liu, Yanwei Duan, Qing Yang
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Glycoside hydrolase family 20 β-N-acetyl-d-hexosaminidases (GH20s) catalyze the hydrolysis of glycosidic linkages in glycans, glycoproteins and glycolipids. The diverse substrates of GH20s account for their various roles in many important bioprocesses, such as glycoprotein modification, glycoconjugate metabolism, gamete recognition and chitin ...
Tian Liu, Yanwei Duan, Qing Yang
openaire +4 more sources
Bioorganic Chemistry
Glycoside hydrolase family 20 (GH20) β-N-acetyl-d-hexosaminidase (Hex) catalyzes the cleavage of glycosidic linkages in glycans, glycolipids and glycoproteins, and is involved in glycoprotein modification, metabolism of glycoconjugate and the degradation of chitin in fungal cell walls and arthropod exoskeletons. GH84 O-β-N-acetyl-d-glucosaminidase (OGA)
Xi Jiang, Qing Yang
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Glycoside hydrolase family 20 (GH20) β-N-acetyl-d-hexosaminidase (Hex) catalyzes the cleavage of glycosidic linkages in glycans, glycolipids and glycoproteins, and is involved in glycoprotein modification, metabolism of glycoconjugate and the degradation of chitin in fungal cell walls and arthropod exoskeletons. GH84 O-β-N-acetyl-d-glucosaminidase (OGA)
Xi Jiang, Qing Yang
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Strategies for developing carbohydrates as glycoside hydrolase inhibitors
2020The cleavage of the glycosidic bond in glycoconjugates is an important activity in biological systems. The enzymes catalyzing this activity are termed as “glycoside hydrolases” (GH). About 1% of the genome in organisms are encoded by GHs. Researchers have put in tremendous amount of effort in understanding the mechanism of GHs and the effect of their ...
Radhika Thanvi +2 more
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