Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/13518
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dc.contributor.authorHrmova, M.en
dc.contributor.authorDe Gori, R.en
dc.contributor.authorSmith, B.en
dc.contributor.authorFairweather, J.en
dc.contributor.authorDriguez, H.en
dc.contributor.authorVarghese, J.en
dc.contributor.authorFincher, G.en
dc.date.issued2002en
dc.identifier.citationPlant Cell, 2002; 14(5):1033-1052en
dc.identifier.issn1040-4651en
dc.identifier.issn1532-298Xen
dc.identifier.urihttp://hdl.handle.net/2440/13518-
dc.description.abstractFamily 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.statementofresponsibilityMaria Hrmova, Ross De Gori, Brian J. Smith, Jon K. Fairweather, Hugues Driguez, Joseph N. Varghese, and Geoffrey B. Fincheren
dc.language.isoenen
dc.publisherAmer Soc Plant Physiologistsen
dc.subjectPlants; 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 Dataen
dc.titleStructural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolasesen
dc.typeJournal articleen
dc.identifier.rmid0020020858en
dc.identifier.doi10.1105/tpc.010442en
dc.identifier.pubid60117-
pubs.library.collectionAgriculture, Food and Wine publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
dc.identifier.orcidHrmova, M. [0000-0002-3545-0605]en
Appears in Collections:Agriculture, Food and Wine publications

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