skip to main content
Idioma:

Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis

Andújar-Sánchez, Montserrat ; Martínez-Rodríguez, Sergio ; Heras-Vázquez, Francisco Javier Las ; Clemente-Jiménez, Josefa María ; Rodríguez-Vico, Felipe ; Jara-Pérez, Vicente

Biochimica et biophysica acta. Proteins and proteomics, 2006-02, Vol.1764 (2), p.292-298 [Periódico revisado por pares]

Elsevier B.V

Texto completo disponível

Citações Citado por
  • Título:
    Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis
  • Autor: Andújar-Sánchez, Montserrat ; Martínez-Rodríguez, Sergio ; Heras-Vázquez, Francisco Javier Las ; Clemente-Jiménez, Josefa María ; Rodríguez-Vico, Felipe ; Jara-Pérez, Vicente
  • Assuntos: Binding ; Escherichia coli ; Hydantoin racemase ; Inhibition ; Mutagenesis ; Sinorhizobium meliloti ; Thermodynamic parameter
  • É parte de: Biochimica et biophysica acta. Proteins and proteomics, 2006-02, Vol.1764 (2), p.292-298
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: Hydantoin racemase enzyme together with a stereoselective hydantoinase and a stereospecific d-carbamoylase guarantee the total conversion from d,l-5-monosubstituted hydantoins with a low velocity of racemization, to optically pure d-amino acids. Hydantoin racemase from Sinorhizobium meliloti was expressed in Escherichia coli. Calorimetric and fluorescence experiments were then carried out to obtain the thermodynamic binding parameters, Δ G, Δ H and Δ S for the inhibitors l- and d-5-methylthioethyl-hydantoin. The number of active sites is four per enzyme molecule (one per monomer), and the binding of the inhibitor is entropically and enthalpically favoured under the experimental conditions studied. In order to obtain information about amino acids involved in the active site, four different mutants were developed in which cysteines 76 and 181 were mutated to Alanine and Serine. Their behaviour shows that these cysteines are essential for enzyme activity, but only cysteine 76 affects the binding to these inhibitors.
  • Editor: Elsevier B.V
  • Idioma: Inglês
Voltar para lista de resultados
Ir para página anteriorAnterior Resultado  9 AvançarIr para próxima página

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.