title: Computational analysis of glycoside hydrolase family 1 specificities.
abstract: Glycoside hydrolase family 1 consists of beta-glucosidases, beta-galactosidases, 6-phospho-beta-galactosidases, myrosinases, and other enzymes having similar primary and tertiary structures but diverse specificities. Among these enzymes, beta-glucosidases hydrolyze cellobiose to glucose, and therefore they are key players in any cellulose to glucose process. All family members attack beta-glycosidic bonds between a pyranosyl glycon and an aglycon, but most have little specificity for the aglycon or for the bond configuration. Furthermore, glycon specificity is not absolute. Sixteen family members (six beta-glucosidases, two cyanogenic beta-glucosidases, one 6-phospho-beta-galactosidase, two myrosinases, and five beta-glycosidases) have known tertiary structures. We have used automated docking to computationally bind disaccharides with allopyranosyl, galactopyranosyl, glucopyranosyl, mannopyranosyl, 6-phosphogalactopyranosyl, and 6-phosphoglucopyranosyl glycons, all linked by beta-(1,2), beta-(1,3), beta-(1,4), and beta-(1,6)-glycosidic bonds to beta-glucopyranoside aglycons, along with beta-(1,1-thio)-allopyranosyl, -galactopyranosyl, -glucopyranosyl, and -mannopyranosyl) beta-glucopyranosides, into all of these structures to investigate the structural determinants of their enzyme specificities. The following are the eight active-site residues: Glu191, Thr194, Phe205, Asn285, Arg336, Asn376, Trp378, and Trp465 (Zea mays beta-glucosidase numbering), that control a significant amount of glycon specificity.
authors.affiliation: Department of Chemical and Biological Engineering, Iowa State University, Ames, IA 50011, USA.
authors.forename: Anthony D
authors.initials: AD
authors.lastname: Hill
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Reilly
mesh_terms: D000595:Amino Acid Sequence; D002236:Carbohydrate Conformation; D004187:Disaccharides / Q000737:chemistry* / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D004187:Disaccharides; D006026:Glycoside Hydrolases