Artículos de revistas
Applying structural transition theory to describe enzyme kinetics in heterogeneous systems
Registro en:
Journal Of Mathematical Chemistry. Springer, v. 52, n. 6, n. 1497, n. 1513, 2014.
0259-9791
1572-8897
WOS:000335504100001
10.1007/s10910-014-0325-1
Autor
Bispo, JAC
Bonafe, CFS
Silva, MLC
Andrade, IHP
Carvalho, GBM
Institución
Resumen
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) 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. 52 6 1497 1513 Fundacao de Amparo a Pesquisa do Estado da Bahia (FAPESB) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)