Results 121 to 130 of about 5,356 (159)
Journal of Applied Glycoscience (1999), 2011 Azasugars are known as potent inhibitors of glycoside hydrolases. In this study, we examined the inhibition of Cellvibrio gilvus cellobiose phosphorylase (CBP) by four azasugars (isofagomine, 1-deoxynojirimycin, castanospermine and calystegine B2) and a non-azasugar (glucono-1,5-lactone).
Shinya Fushinobu +2 more
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
openaire +2 more sources
Bioscience, Biotechnology and BiochemistryAbstract Glycoside hydrolase family 65 (GH65) includes glycoside hydrolases active on various α-glucosides. We previously demonstrated that the GH65 enzyme from Flavobacterium johnsoniae (FjGH65A) is a kojibiose hydrolase and determined its 3-dimensional structure. In this study, the effects of glucosidase inhibitors on FjGH65A and their
Shuntaro Nakamura +2 more
exaly +3 more sources
ACS Catalysis, 2022
In this study, we look at how a catalytically efficient α-galactosidase stabilizes transition state (TS) charge delocalization for substrate hydrolysis. We then assess whether covalent inhibition of the enzyme by three types of mechanism-based covalent inhibitors occurs via similar modes of TS stabilization.
Oluwafemi Akintola +2 more
exaly +3 more sources
In this study, we look at how a catalytically efficient α-galactosidase stabilizes transition state (TS) charge delocalization for substrate hydrolysis. We then assess whether covalent inhibition of the enzyme by three types of mechanism-based covalent inhibitors occurs via similar modes of TS stabilization.
Oluwafemi Akintola +2 more
exaly +3 more sources
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
openaire +1 more source
The Synthesis of a New Class of Potential Inhibitors for Glycoside Hydrolases†
Journal of Carbohydrate Chemistry, 2005Some attempts toward the synthesis of novel inhibitors of glycosyl transferases are described. More successfully, the synthesis of an activated cyclopropacyclohexene and an amide and an amine of a cyclopropa‐fused pyranose are described. None of these three novel compounds proved to be a significant inhibitor of a retaining α‐glucosidase from barley. †
Robert Stick, Keith Stubbs
openaire +1 more source
Mechanism‐Based Inhibitors to Probe Transitional States of Glycoside Hydrolases
2006Recent structural and kinetic studies indicate that glycosidases (glycoside hydrolases) change the peripheral structure of their catalytic sites dynamically to trim glycan structures. Inhibitors that label specific amino acid residues in the active site of these enzymes based on its mechanism of action are powerful tools to probe such a hidden ...
Hiroshi, Hinou +2 more
openaire +2 more sources
The Synthesis of Some Epoxyalkyl b-C-Glycosides as Potential Inhibitors of b-Glucan Hydrolases
Australian Journal of Chemistry, 1997The treatment of tetra-O-benzyl-D-glucono-1,5-lactone with various alkenylmagnesium halides gave the intermediate lactols which, upon reduction (Et3SiH/BF3) and protecting group manipulation, yielded alkenyl tetra-O-acetyl-β-D-C-glucopyranosides in good yield.
Best, W.M. +4 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
exaly +3 more sources
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
exaly +3 more sources
Australian Journal of Chemistry, 2007
While isofagomine and noeuromycin have previously been demonstrated to be effective inhibitors of a range of exo-acting glycosidases, they are usually only very weak inhibitors of endo-glycosidases. However, the disaccharide-like 3- and 4-O-ß-d-glucopyranosylisofagomines have proven to be strong inhibitors of these endo-acting enzymes that utilize ...
Peter J. Meloncelli +6 more
openaire +1 more source
While isofagomine and noeuromycin have previously been demonstrated to be effective inhibitors of a range of exo-acting glycosidases, they are usually only very weak inhibitors of endo-glycosidases. However, the disaccharide-like 3- and 4-O-ß-d-glucopyranosylisofagomines have proven to be strong inhibitors of these endo-acting enzymes that utilize ...
Peter J. Meloncelli +6 more
openaire +1 more source