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|dc.contributor.author||De Gori, R.||en|
|dc.identifier.citation||Plant Cell, 2002; 14(5):1033-1052||en|
|dc.description.abstract||Family 3 β-D-glucan glucohydrolases are distributed widely in higher plants. The enzymes catalyze the hydrolytic removal of β-D-glucosyl residues from nonreducing termini of a range of β-D-glucans and β-D-oligoglucosides. Their broad specificity can be explained by x-ray crystallographic data obtained from a barley β-D-glucan glucohydrolase in complex with nonhydrolyzable S-glycoside substrate analogs and by molecular modeling of enzyme/substrate complexes. The glucosyl residue that occupies binding subsite -1 is locked tightly into a fixed position through extensive hydrogen bonding with six amino acid residues near the bottom of an active site pocket. In contrast, the glucosyl residue at subsite +1 is located between two Trp residues at the entrance of the pocket, where it is constrained less tightly. The relative flexibility of binding at subsite +1, coupled with the projection of the remainder of bound substrate away from the enzyme's surface, means that the overall active site can accommodate a range of substrates with variable spatial dispositions of adjacent β-D-glucosyl residues. The broad specificity for glycosidic linkage type enables the enzyme to perform diverse functions during plant development.||en|
|dc.description.statementofresponsibility||Maria Hrmova, Ross De Gori, Brian J. Smith, Jon K. Fairweather, Hugues Driguez, Joseph N. Varghese, and Geoffrey B. Fincher||en|
|dc.publisher||Amer Soc Plant Physiologists||en|
|dc.subject||Plants; Glucans; Glycoside Hydrolases; Glucosidases; beta-Glucosidase; Glucan Endo-1,3-beta-D-Glucosidase; Cellobiose; Disaccharides; Trisaccharides; Phylogeny; Binding Sites; Amino Acid Sequence; Carbohydrate Sequence; Protein Binding; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Kinetics; Catalysis; Models, Molecular; Molecular Sequence Data||en|
|dc.title||Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases||en|
|pubs.library.collection||Agriculture, Food and Wine publications||en|
|dc.identifier.orcid||Hrmova, M. [0000-0002-3545-0605]||en|
|Appears in Collections:||Agriculture, Food and Wine publications|
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