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Binding of β-D-glucosides and β-D-mannosides by rice and barley β-D-glycosidases with distinct substrate specificities

AuthorsKuntothom, T.; Raab, M.; Tvaroska, I.; Fort, S.; Pengthaisong, S.; Cañada, F. Javier CSIC ORCID ; Calle Jiménez, Luis Pablo CSIC; Jiménez-Barbero, Jesús CSIC ORCID; Ketudat Cairns, J. R.; Hrmova, M,
Issue Date12-Oct-2010
PublisherAmerican Chemical Society
CitationBiochemistry, 49 (40) : 8779-93 (2010)
AbstractBinding of β-d-Glucosides and β-d-Mannosides by Rice and Barley β-d-Glycosidases with Distinct Substrate SpecificitiesAbstractFull Text HTMLHi-Res PDF[4702 KB]PDF w/ Links[1269 KB]Supporting Info -> PDFbi101112c_si_001.pdf (116.23 kb)FiguresCiting ArticlesTeerachai Kuntothom‡#, Michal Raab#§, Igor Tvaroška§, Sebastien Fort, Salila Pengthaisong‡, Javier Cañada, Luis Calle, Jesús Jiménez-Barbero, James R. Ketudat Cairns‡, and Maria Hrmova*@● ‡ School of Biochemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, Thailand § Department of Structure and Function of Saccharides, Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Bratislava, Slovak Republic Centre de Recherches sur les Macromolecules Vegetales, Grenoble, France Centro de Investigaciones Biológicas, CSIC, Madrid, Spain @ Australian Centre for Plant Functional Genomics, University of Adelaide, Glen Osmond, Australia. Biochemistry, 2010, 49 (40), pp 8779–8793 DOI: 10.1021/bi101112c Publication Date (Web): September 8, 2010 Copyright © 2010 American Chemical Society *To whom correspondence should be addressed. Telephone: +61 8 8303 7160. Fax: +61 8 8303 7102. E-mail: maria.hrmova@adelaide.edu.au., #These authors made equal contributions to this work. , Current address: Department of Chemistry, Mahasarakham University, Mahasarakham, Thailand. , ●Also affiliated with Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic. † Funding Statement This work was supported by grants from the Australian Research Council to M.H. and from the Thailand Research Fund (BRG5080007) to J.R.K.C. T.K. was sponsored by The Institute for the Promotion of Teaching Science and Technology of Thailand. M.R. and I.T. are thankful for support from the Science and Technology Assistance Agency under Contract APVV-0607-07. J.C., L.C., and J.J.-B. thank the Ministerio de Ciencia e Innovacion for support (CTQ2009-08536). Section:EnzymesAbstractPredominantly, rice Os3BGlu7 operates as a β-d-glucosidase (EC, while barley HvBII acts as a β-d-mannosidase (EC Saturation transfer difference nuclear magnetic resonance (STD NMR) and transferred nuclear Overhauser effect (trNOE) spectroscopy in conjunction with quantum mechanics/molecular mechanics (QM/MM) modeling and docking at the 6-31+G* level were used to investigate binding of S- and O-linked gluco- and manno-configured aryl-β-d-glycosides to Os3BGlu7 and HvBII. Kinetic analyses with 4-nitrophenyl β-d-thioglucoside (4NP-S-Glc) and 4-nitrophenyl β-d-thiomannoside (4NP-S-Man) indicated that the inhibitions were competitive with apparent Ki constants of 664 and 710 μM for Os3BGlu7 and 95 and 266 μM for HvBII, respectively. The STD NMR and trNOESY experiments revealed that 4NP-S-Glc and 4NP-S-Man bound weakly in 4C1 conformations to Os3BGlu7; 4NP-S-Glc adopted 3S5 (B3,O) or 1S3 (1,4B) conformations, and 4NP-S-Man preferred 4C1 geometry, when bound to HvBII. The QM modeling and docking, based on GLIDE scores, predicted that 4NP-O-Glc, 4NP-O-Man, and 4NP-S-Man bound preferentially in 1S3 geometries to both enzymes, contrary to 4NP-S-Glc that could also adopt a 4C1 conformation, although in a “flipped-down” ring position. The experimental and computational data suggested that in glycoside recognition and substrate specificity of Os3BGlu7 and HvBII, a combination of the following determinants is likely to play key roles: (i) the inherent conformational and spatial flexibilities of gluco- and manno-configured substrates in the enzymes’ active sites, (ii) the subtle differences in the spatial disposition of active site residues and their capacities to form interactions with specific groups of substrates, and (iii) the small variations in the charge distributions and shapes of the catalytic sites.
Description15 páginas, 9 figuras, 2 tablas -- PAGS nros. 8779-8793
Publisher version (URL)http://dx.doi.org/10.1021/bi101112c
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