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Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase.
Fourmy, D; Mechulam, Y; Brunie, S; Blanquet, S; Fayat, G.
Afiliação
  • Fourmy D; Laboratoire de Biochimie, Unité de Recherche Associée 240 du Centre National de la Recherche Scientifique, Ecole Polytechnique, Palaiseau, France.
FEBS Lett ; 292(1-2): 259-63, 1991 Nov 04.
Article em En | MEDLINE | ID: mdl-1959615
Comparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the occurrence of a few conserved motifs, having a possible functional significance. The role of one of these motifs, centered at position 300 in the E. coli enzyme sequence, was assayed by the use of site-directed mutagenesis. Substitution of the His301 or Trp305 residues by Ala resulted in a large decrease in methionine affinity, whereas the change of Val298 into Ala had only a moderate effect. The catalytic rate of the enzyme was unimpaired by these substitutions. It is concluded that the above conserved amino-acid region is located at or close to the amino-acid binding pocket of methionyl-tRNA synthetase.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Escherichia coli / Metionina / Metionina tRNA Ligase Tipo de estudo: Diagnostic_studies Idioma: En Revista: FEBS Lett Ano de publicação: 1991 Tipo de documento: Article País de afiliação: França
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Escherichia coli / Metionina / Metionina tRNA Ligase Tipo de estudo: Diagnostic_studies Idioma: En Revista: FEBS Lett Ano de publicação: 1991 Tipo de documento: Article País de afiliação: França