Applying structural transition theory to describe enzyme kinetics in heterogeneous systems

dc.creatorBispo, JAC
dc.creatorBonafe, CFS
dc.creatorSilva, MLC
dc.creatorAndrade, IHP
dc.creatorCarvalho, GBM
dc.date2014
dc.dateJUN
dc.date2014-07-30T13:49:24Z
dc.date2015-11-26T16:42:41Z
dc.date2014-07-30T13:49:24Z
dc.date2015-11-26T16:42:41Z
dc.date.accessioned2018-03-28T23:27:20Z
dc.date.available2018-03-28T23:27:20Z
dc.identifierJournal Of Mathematical Chemistry. Springer, v. 52, n. 6, n. 1497, n. 1513, 2014.
dc.identifier0259-9791
dc.identifier1572-8897
dc.identifierWOS:000335504100001
dc.identifier10.1007/s10910-014-0325-1
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/54813
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/54813
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1273339
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionEnzyme action was investigated by assuming the occurrence of different states of enzyme-substrate affinities. These states were considered to involve enzyme species with distinct abilities to form reaction product. The results obtained showed strong agreement with the experimental data for the action of peroxidase. This approach provides a powerful tool for predicting the kinetic behavior of other enzymatic processes in conditions not described before. An additional feature of this approach is the ability to characterize processes at any enzyme-substrate concentration ratio, including high enzyme-substrate ratios and enzyme inhibition by substrate or product. This proposal can also be used in systems with heterogeneity concerning the investigated enzyme.
dc.description52
dc.description6
dc.description1497
dc.description1513
dc.descriptionFundacao de Amparo a Pesquisa do Estado da Bahia (FAPESB)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Mathematical Chemistry
dc.relationJ. Math. Chem.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectEnzyme kinetics
dc.subjectHMM and MWC models
dc.subjectMichaelis-Menten kinetics
dc.subjectTwo-state model
dc.subjectMichaelis-menten Model
dc.subjectLigand-binding
dc.subjectLinked Functions
dc.subjectHemoglobin
dc.subjectPeroxidase
dc.subjectProteins
dc.subjectAssociation
dc.subjectDependence
dc.subjectSubstrate
dc.subjectSubunits
dc.titleApplying structural transition theory to describe enzyme kinetics in heterogeneous systems
dc.typeArtículos de revistas


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