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dc.creatorDusan, Velickovic
dc.creatorNenad, Milosavic
dc.creatorDejan, Bezbradica
dc.creatorBihelović, Filip
dc.creatorSegal, Ann Marie
dc.creatorŠegan, Dejan M.
dc.creatorTrbojević-Ivić, Jovana
dc.creatorAleksandra, Dimitrijevic
dc.date.accessioned2018-11-22T00:28:17Z
dc.date.available2018-11-22T00:28:17Z
dc.date.issued2014
dc.identifier.issn0175-7598
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1797
dc.description.abstractOur investigation of the catalytic properties of Saccharomyces cerevisiae alpha-glucosidase (AGL) using hydroxybenzyl alcohol (HBA) isomers as transglucosylation substrates and their glucosides in hydrolytic reactions demonstrated interesting findings pertaining to the aglycon specificity of this important enzyme. AGL specificity increased from the para(p)- to the ortho(o)-HBA isomer in transglucosylation, whereas such AGL aglycon specificity was not seen in hydrolysis, thus indicating that the second step of the reaction (i.e., binding of the glucosyl acceptor) is rate-determining. To study the influence of substitution pattern on AGL kinetics, we compared AGL specificity, inferred from kinetic constants, for HBA isomers and other aglycon substrates. The demonstrated inhibitory effects of HBA isomers and their corresponding glucosides on AGL-catalyzed hydrolysis of p-nitrophenyl a-glucoside (PNPG) suggest that HBA glucosides act as competitive, whereas HBA isomers are noncompetitive, inhibitors. As such, we postulate that aromatic moieties cannot bind to an active site unless an enzyme-glucosyl complex has already formed, but they can interact with other regions of the enzyme molecule resulting in inhibition.en
dc.publisherSpringer, New York
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsrestrictedAccess
dc.sourceApplied Microbiology and Biotechnology
dc.subjectAglycon specificityen
dc.subjectalpha-glucosidaseen
dc.subjectTransglucosylation kineticsen
dc.subjectHydrolysis kineticsen
dc.subjectSubstrate inhibitionen
dc.subjectHydroxybenzyl alcoholen
dc.titleThe specificity of alpha-glucosidase from Saccharomyces cerevisiae differs depending on the type of reaction: hydrolysis versus transglucosylationen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСегал, Aнн Марие; Ненад, Милосавиц; Дејан, Безбрадица; Дејан, Сеган; Aлександра, Димитријевиц; Дусан, Велицковиц; Трбојевић-Ивић, Јована; Бихеловић, Филип;
dc.citation.volume98
dc.citation.issue14
dc.citation.spage6317
dc.citation.epage6328
dc.identifier.wos000338237400013
dc.identifier.doi10.1007/s00253-014-5587-9
dc.citation.other98(14): 6317-6328
dc.citation.rankM21
dc.identifier.pmid24682477
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84903612924
dc.identifier.rcubKon_2680


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