Evolution of polysaccharide hydrolase substrate specificity. Three-dimensional structure of two plant beta-glucan endohydrolases with distinct substrate specificities. Varghese, J.N., Garrett, T.P.J., Colman, P.M., Chen, L., HøJ, P.B. Glutamic acid 274 is the nucleophile in the active site of a “retaining” exoglucanase from Cellulomonas fimi. Tull, D., Withers, S.G., Gilkes, N.R., Kilburn, D.G., Warren, R.A.J. Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites. Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi.

Crystal structure, at 2.6 Å resolution, of the Streptomyces lividans xylanase A, a member of the F family of β-1,4-D-glycanases. Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: Two conformational states in the active site. Structure and function of endoglucanase V. The catalytic domain of endoglucanase A from Clostridium cellulolyticum - Effects of arginine-79 and histidine-122 mutations on catalysis. Cellulase EGZ of Erwinia chrysanthemi: structural organization and importance of His 98 and Glu 133 residues for catalysis. Py, B., Bortoli-German, I., Haiech, J., Chippaux, M. Site-directed mutagenesis of conserved residues in Clostridium thermocellum endoglucanase CelC. Glu 280 is the nucleophile in the active site of Clostridium thermocellum CelC, a family A endo-β-1,4-glucanase. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution using amino acid sequence data. Stereoselective hydrolysis catalyzed by related β-1,4-glucanases and β-1,4-xylanases. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. A classification of glycosyl hydrolases based on amino acid sequence similarities. Domains in microbial β-1,4-glycanases: Sequence conservation, function, and enzyme families. Gilkes, N.R., Henrissat, B., Kilburn, D.G., Miller, R.C., Jr & Warren, R.A.J.

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