Search Results - "Warren, R.Antony J."

Engineering of a thioglycoligase: randomized mutagenesis of the acid–base residue leads to the identification of improved catalysts by Müllegger, Johannes, Jahn, Michael, Chen, Hong-Ming, Warren, R.Antony J., Withers, Stephen G.

“…Thioglycoligases are recently introduced variants of retaining glycosidases in which the acid–base catalyst has been mutated, rendering them capable of…”
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Fusion to an endoglucanase allows alkaline phosphatase to bind to cellulose by Greenwood, Jeffrey M., Gilkes, Neil R., Kilburn, Douglas G., Miller, Robert C., Warren, R.Antony J.

“…Endoglucanase CenA of Cellulomonas fimi comprises an N-terminal cellulose-binding domain and a C-terminal catalytic domain joined together by a sequence of 23…”
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Characterization and affinity applications of cellulose-binding domains by Tomme, Peter, Boraston, Al, McLean, Brad, Kormos, Jeff, Creagh, A.Louise, Sturch, Ken, Gilkes, Neil R., Haynes, Charles A., Warren, R.Antony J., Kilburn, Douglas G.

“…Cellulose-binding domains (CBDs) are discrete protein modules found in a large number of carbohydrolases and a few nonhydrolytic proteins. To date, almost 200…”
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Structure and Ligand Binding of Carbohydrate-binding Module CsCBM6-3 Reveals Similarities with Fucose-specific Lectins and “Galactose-binding” Domains by Boraston, Alisdair B, Notenboom, Valerie, Warren, R.Antony J, Kilburn, Douglas G, Rose, David R, Davies, Gideon

“…Carbohydrate-binding polypeptides, including carbohydrate-binding modules (CBMs) from polysaccharidases, and lectins, are widespread in nature. Whilst CBMs are…”
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The E358S mutant of Agrobacterium sp. β-glucosidase is a greatly improved glycosynthase by Mayer, Christoph, Zechel, David L., Reid, Stephen P., Warren, R.Antony J., Withers, Stephen G.

“…Glycosynthases are nucleophile mutants of retaining glycosidases that catalyze the glycosylation of sugar acceptors using glycosyl fluoride donors, thereby…”
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Affinity electrophoresis for the identification and characterization of soluble sugar binding by carbohydrate-binding modules by Tomme, Peter, Boraston, Alisdair, Kormos, Jeffery M, Warren, R.Antony J, Kilburn, Douglas G

“…Affinity electrophoresis was used to identify and quantify the interaction of carbohydrate-binding modules (CBMs) with soluble polysaccharides. Association…”
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Mannanase Man26A from Cellulomonas fimi has a mannan-binding module by Stoll, Dominik, Boraston, Alisdair, Stålbrand, Henrik, McLean, Bradley W., Kilburn, Douglas G., Warren, R.Antony J.

“…A modular mannanase (Man26A) from the bacterium Cellulomonas fimi contains a mannan-binding module (Man26Abm) that binds to soluble but not to insoluble…”
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Mannanase Man26A from Cellulomonas fimi has a mannan-binding module by Stoll, D, Boraston, A, Stalbrand, H, McLean, B.W, Kilburn, D.G, Warren, R.A.J

“…A modular mannanase (Man26A) from the bacterium Cellulomonas fimi contains a mannan-binding module (Man26Abm) that binds to soluble but not to insoluble…”
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The identification of the catalytic nucleophiles of two β-galactosidases from glycoside hydrolase family 35 by Blanchard, Jan E, Gal, Laurent, He, Shouming, Foisy, Janine, Warren, R.Antony J, Withers, Stephen G

“…The β-galactosidases from Xanthomonas manihotis (β-Gal Xmn) and Bacillus circulans (β-Gal-3 Bcir) are retaining glycosidases that hydrolyze glycosidic bonds…”
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Enhancement of the Endo-β-1,4-glucanase Activity of an Exocellobiohydrolase by Deletion of a Surface Loop (∗) by Meinke, Andreas, Damude, Howard G., Tomme, Peter, Kwan, Emily, Kilburn, Douglas G., Miller, Robert C., Warren, R.Antony J., Gilkes, Neil R.

“…In the commonly accepted mechanism for enzymatic hydrolysis of cellulose, endo-β-1,4-glucanases randomly cleave glucosidic bonds within glucan polymers,…”
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A streptavidin-cellulose-binding domain fusion protein that binds biotinylated proteins to cellulose by Le, K D, Gilkes, N R, Kilburn, D G, Miller, Jr, R C, Saddler, J N, Warren, R A

“…A fusion protein, Sta-CBDCex, which comprises streptavidin with a cellulose-binding domain (CBDCex) fused to its C terminus, was produced in the cytoplasm of…”
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Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the bacterium Cellulomonas fimi by Bedarkar, S, Gilkes, N R, Kilburn, D G, Kwan, E, Rose, D R, Miller, Jr, R C, Warren, R A, Withers, S G

“…Single crystals of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the cellulolytic bacterium Cellulomonas fimi, have been…”
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