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dc.contributor.authorGreanggrai Hommalaien_US
dc.contributor.authorStephen G. Withersen_US
dc.contributor.authorWatchalee Chuenchoren_US
dc.contributor.authorJames R Ketudat Cairnsen_US
dc.contributor.authorJisnuson Svastien_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThe University of British Columbiaen_US
dc.contributor.otherSuranaree University of Technologyen_US
dc.date.accessioned2018-08-24T01:41:30Z-
dc.date.available2018-08-24T01:41:30Z-
dc.date.issued2007-07-01en_US
dc.identifier.citationGlycobiology. Vol.17, No.7 (2007), 744-753en_US
dc.identifier.issn14602423en_US
dc.identifier.issn09596658en_US
dc.identifier.other2-s2.0-34447309082en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34447309082&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/24173-
dc.description.abstractRice BGlu1 β-glucosidase is a glycosyl hydrolase family 1 enzyme that acts as an exoglucanase on β-(1,4)- and short β-(1,3)-linked gluco-oligosaccharides. Mutations of BGlu1 β-glucosidase at glutamate residue 414 of its natural precursor destroyed the enzyme's catalytic activity, but the enzyme could be rescued in the presence of the anionic nucleophiles such as formate and azide, which verifies that this residue is the catalytic nucleophile. The catalytic activities of three candidate mutants, E414G, E414S, and E414A, in the presence of the nucleophiles were compared. The E414G mutant had approximately 25- and 1400-fold higher catalytic efficiency than E414A and E414S, respectively. All three mutants could catalyze the synthesis of mixed length oligosaccharides by transglucosylation, when α-glucosyl fluoride was used as donor and pNP-cellobioside as acceptor. The E414G mutant gave the fastest transglucosylation rate, which was approximately 3- and 19-fold faster than that of E414S and E414A, respectively, and gave yields of up to 70-80% insoluble products with a donor-cceptor ratio of 5:1.13C-NMR, methylation analysis, and electrospray ionization-mass spectrometry showed that the insoluble products were β-(1,4)-linked oligomers with a degree of polymerization of 5 to at least 11. The BGlu1 E414G glycosynthase was found to prefer longer chain length oligosaccharides that occupy at least three sugar residue-binding subsites as acceptors for productive transglucosylation. This is the first report of a β-glucansynthase derived from an exoglycosidase that can produce long-chain cello-oligosaccharides, which likely reflects the extended oligosaccharide-binding site of rice BGlu1 β-glucosidase. © The Author 2007.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34447309082&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleEnzymatic synthesis of cello-oligosaccharides by rice BGlu1 β-glucosidase glycosynthase mutantsen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1093/glycob/cwm039en_US
Appears in Collections:Scopus 2006-2010

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