Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/54813
Type: Artigo de periódico
Title: Applying structural transition theory to describe enzyme kinetics in heterogeneous systems
Author: Bispo, JAC
Bonafe, CFS
Silva, MLC
Andrade, IHP
Carvalho, GBM
Abstract: Enzyme 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.
Subject: Enzyme kinetics
HMM and MWC models
Michaelis-Menten kinetics
Two-state model
Country: EUA
Editor: Springer
Rights: fechado
Identifier DOI: 10.1007/s10910-014-0325-1
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

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