@inbook {16738,
	title = {Carbohydrases},
	booktitle = {The Encyclopedia of Catalysis},
	year = {2010},
	publisher = {John Wiley and Sons},
	organization = {John Wiley and Sons},
	edition = {2nd},
	address = {New York},
	abstract = {<p>The enzymes that catalyze the synthesis and degradation of oligo- and polysaccharides are among the most important in the biosphere, because of the key role they play in the global carbon cycle. Thanks to a long and rich history of scientific study, the catalytic mechanisms of the glycoside hydrolases and transglycosylases are generally well understood in terms of enzyme-substrate interactions and transition state structure. Recent structure-function studies of polysaccharide lyases have also begun to unravel the secrets of catalysis in these distinct classes of carbohydrate-active enzymes. Built upon a firm understanding of enzyme structure and mechanism, an impressive number of technological applications highlight the prowess of these biological catalysts.</p>},
	keywords = {biomass, carbohydrate binding module (CBM), CAZy, glycosidase, glycoside hydrolase, GLYCOSYL-ENZYME INTERMEDIATE, polysaccharide lyase, TRANSGLYCOSYLATION},
	doi = {10.1002/0471227617.eoc037},
	author = {Brumer, Harry},
	editor = {Istv{\'a}n T. Horv{\'a}th}
}
@article {2682,
	title = {Construction of protected hydroxylated pyrrolidines using nitrogen-centered radical cyclizations},
	journal = {Chemical Communications},
	number = {38},
	year = {2009},
	note = {ISI Document Delivery No.: 498CXTimes Cited: 3Cited Reference Count: 41Zhai, Huimin Zlotorzynska, Maria Sammis, Glenn},
	pages = {5716-5718},
	type = {Article},
	abstract = {Nitrogen-centered radical cyclizations onto silyl enol ethers were utilized for the syntheses of protected polyhydroxylated pyrrolidines 2-hydroxymethyl-3-hydroxypyrrolidine and 1,4-dideoxy-1,4-imino-L-ribitol.},
	keywords = {1, 4-DIDEOXY-1, 4-IMINO-L-RIBITOL, ADDITIONS, AMINYL RADICALS, GENERATION, glycosidase, inhibitors, NATURAL OCCURRENCE, ring expansion, ROUTE, STRAIGHTFORWARD SYNTHESIS, THERAPEUTIC APPLICATIONS},
	isbn = {1359-7345},
	url = {<Go to ISI>://000270115300013},
	author = {Zhai, H. M. and Zlotorzynska, M. and Sammis, G.}
}
@article {713,
	title = {Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens},
	journal = {Carbohydrate Research},
	volume = {338},
	number = {5},
	year = {2003},
	note = {ISI Document Delivery No.: 645XBTimes Cited: 6Cited Reference Count: 38},
	month = {Feb},
	pages = {415-421},
	type = {Article},
	abstract = {The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate omicron-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pK(a) values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an similar to 10-fold higher k(cat)/K-m value with this substrate at pH 6 and 40 degreesC, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. (C) 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {bacillus xylanase, CIRCULANS XYLANASE, CLASSIFICATION, electrostatic, extremophile, glycosidase, GLYCOSYL-ENZYME INTERMEDIATE, HYDROLASES, interactions, NMR ASSIGNMENTS, pH-dependent mechanism, PK(A), PROTEIN, STABILITY, THERMOSTABILITY},
	isbn = {0008-6215},
	url = {<Go to ISI>://000181004800004},
	author = {Poon, D. K. Y. and Webster, P. and Withers, S. G. and McIntosh, L. P.}
}
@article {5228,
	title = {Synthesis of 2,6-dideoxy-2-fluoro-6-[F-18]-fluoro-beta-D-glucopyranosyl fluoride (2,6FGF) as a potential imaging probe for glucocerebrosidase},
	journal = {Journal of Labelled Compounds \& Radiopharmaceuticals},
	volume = {44},
	number = {5},
	year = {2001},
	note = {ISI Document Delivery No.: 420VMTimes Cited: 4Cited Reference Count: 8},
	month = {Apr},
	pages = {385-394},
	type = {Article},
	abstract = {We have previously synthesized 2-deoxy-2-[F-18]-fluoro-beta -mannosyl [F-18]-fluoride and shown that it behaves as a mechanism-based inhibitor of Agrobacterium sp. beta -glucosidase. In-vivo experiments indicate that this compound undergoes partial hydrolysis to produce 2-deoxy-2-fluoro-mannose, which can become phosphorylated and trapped within the cell. We now report the synthesis of another 2-fluoro glycoside which is F-18-labelled at the 6 position so that the label cannot be lost during such glycoside hydrolysis and which, further, cannot be phosphorylated. The mechanism-based glycosidase inhibitor 2,6-dideoxy-2-fluoro-6-[F-18]-fluoro-beta -D-glucopyranosyl fluoride (2,6FGF) was synthesized in 69\% overall chemical yield and in 9\% radiochemical yield (decay corrected) as a potential imaging probe for glycosidase.},
	keywords = {2-fluoro-glucose, fluorine-18, Gaucher{\textquoteright}s disease, glycosidase, PET},
	isbn = {0362-4803},
	url = {<Go to ISI>://000168026000009},
	author = {Wong, A. W. and Adam,Michael J. and Withers, S. G.}
}
@article {4667,
	title = {Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase},
	journal = {Biochemistry},
	volume = {38},
	number = {17},
	year = {1999},
	note = {ISI Document Delivery No.: 193YMTimes Cited: 122Cited Reference Count: 50},
	month = {Apr},
	pages = {5346-5354},
	type = {Article},
	abstract = {The 1.8 Angstrom resolution structure of the glycosyl-enzyme intermediate formed on the retaining beta-1,4-xylanase from Bacillus circulans has been determined using X-ray crystallographic techniques. The 2-fluoro-xylose residue bound in the -1 subsite adopts a B-2,B-5 (boat) conformation, allowing atoms C5, O5, C1, and C2 of the sugar to achieve coplanarity as required at the oxocarbenium ion-like transition states of the double-displacement catalytic mechanism. Comparison of this structure to that of a mutant of this same enzyme noncovalently complexed with xylotetraose [Wakarchuk et al. (1994) Protein Sci. 3, 467-475] reveals a number of differences beyond the distortion of the sugar moiety. Most notably, a bifurcated hydrogen bond interaction is formed in the glycosyl-enzyme intermediate involving H-eta of Tyr69, the endocyclic oxygen (O5) of the xylose residue in the -1 subsite, and O-epsilon 2 of the catalytic nucleophile, Glu78. To gain additional understanding of the role of Tyr69 at the active site of this enzyme, we also determined the 1.5 Angstrom resolution structure of the catalytically inactive Tyr69Phe mutant. Interestingly, no significant structural perturbation due to the loss of the phenolic group is observed. These results suggest that the interactions involving the phenolic group of Tyr69, O5 of the proximal saccharide, and Glu78 O-epsilon 2 important for the catalytic mechanism of this enzyme, and it is proposed that, through charge redistribution, these interactions serve to stabilize the oxocarbenium-like ion of the transition state. Studies of the covalent glycosyl-enzyme intermediate of this xylanase also provide insight into specificity, as contacts with C5 of the xylose moiety exclude sugars with hydroxymethyl substituents, and the mechanism of catalysis, including aspects of stereoelectronic theory as applied to glycoside hydrolysis.},
	keywords = {ACTIVE-SITE RESIDUES, BACILLUS-CIRCULANS XYLANASE, beta-glucosidase, CELLULOMONAS-FIMI, glycosidase, IDENTIFICATION, LEAVING GROUP, MECHANISM, REACTION COORDINATE, TRICHODERMA-REESEI},
	isbn = {0006-2960},
	url = {<Go to ISI>://000080165400009},
	author = {Sidhu, G. and Withers, S. G. and Nguyen, N. T. and McIntosh, L. P. and Ziser, L. and Brayer, G. D.}
}
@article {4197,
	title = {Mechanisms of cellulases and xylanases},
	journal = {Biochemical Society Transactions},
	volume = {26},
	number = {2},
	year = {1998},
	note = {ISI Document Delivery No.: ZT170Times Cited: 22Cited Reference Count: 24664th Meeting of the Biochemical-SocietyDEC 15-17, 1997READING, ENGLANDBiochem Soc},
	month = {May},
	pages = {156-160},
	type = {Proceedings Paper},
	keywords = {ACID-SEQUENCE SIMILARITIES, ACTIVE-SITE, BACILLUS-CIRCULANS XYLANASE, CLASSIFICATION, ENZYME, FAMILIES, GLUCOSIDASE, glycosidase, GLYCOSYL HYDROLASES, HYDROLYSIS, nucleophile},
	isbn = {0300-5127},
	url = {<Go to ISI>://000074056400019},
	author = {Birsan, C. and Johnson, P. and Joshi, M. and MacLeod, A. and McIntosh, L. and Monem, V. and Nitz, M. and Rose, D. R. and Tull, D. and Wakarchuck, W. W. and Wang, Q. and Warren, R. A. J. and White, A. and Withers, S. G.}
}
