cellulase has been researched along with isofagomine* in 3 studies
3 other study(ies) available for cellulase and isofagomine
| Article | Year |
|---|---|
A potential fortuitous binding of inhibitors of an inverting family GH9 β-glycosidase derived from isofagomine.
Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site. Topics: Alicyclobacillus; Cellulase; Enzyme Inhibitors; Glycoside Hydrolases; Imino Pyranoses; Models, Molecular; Protein Binding | 2011 |
Distortion of a cellobio-derived isofagomine highlights the potential conformational itinerary of inverting beta-glucosidases.
A cellobio-derived isofagomine glycosidase inhibitor (Ki approximately 400 nM) displays an unusual distorted 2,5B (boat) conformation upon binding to cellobiohydrolase Cel6A from Humicola insolens, highlighting the different conformational itineraries used by various glycosidases, with consequences for the design of therapeutic agents. Topics: Ascomycota; beta-Glucosidase; Cellobiose; Cellulase; Cellulose 1,4-beta-Cellobiosidase; Glycoside Hydrolases; Imino Pyranoses; Models, Molecular; Piperidines; Protein Conformation; Substrate Specificity | 2003 |
Direct observation of the protonation state of an imino sugar glycosidase inhibitor upon binding.
Glycosidases are some of the most ubiquitous enzyme in nature. Their biological significance, coupled to their enormous catalytic prowess derived from tight binding of the transition state, is reflected in their importance as therapeutic targets. Many glycosidase inhibitors are known. Imino sugars are often potent inhibitors, yet many facets of their mode of action, such as their degree, if any, of transition-state "mimicry" and their protonation state when bound to the target glycosidase remain unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in complex with a cellobio-derived isofagomine in conjunction with the pH dependence of Ki and kcat/KM reveals that this compound binds as a protonated sugar. Surprisingly, both the enzymatic nucleophile and the acid/base are unprotonated in the complex. Topics: Bacillus; Binding Sites; Cellulase; Enzyme Inhibitors; Hydrogen-Ion Concentration; Imino Pyranoses; Kinetics; Oligosaccharides; Piperidines; Protons | 2003 |