title: [Tyrosyl-tRNA-synthetase from bovine liver. Functional role of histidine residues].
abstract: A specific chemical modification of histidyl residues in tyrosyl-tRNA synthetase by diethyl pyrocarbonate was performed. It is shown that five of sixteen histidyl residues can react with diethyl pyrocarbonate in the native conditions. Modification of two histidyl residues per dimer results in the inactivation of tyrosyl-tRNA synthetase in both steps of the tRNATyr aminoacylation. All substrates protect tyrosyl-tRNA synthetase against inactivation with diethyl pyrocarbonate, the most effective protector being combination of ATP and tyrosine. Histidyl residues of tyrosyl-tRNA synthetase are suggested to be involved in the catalytic mechanism of aminoacylation of tRNATyr.
authors.forename: D V
authors.initials: DV
authors.lastname: Gnatenko
authors.forename: A I
authors.initials: AI
authors.lastname: Korneliuk
authors.forename: G Kh
authors.initials: GKh
authors.lastname: Matsuka
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002417:Cattle; D004047:Diethyl Pyrocarbonate / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D007700:Kinetics; D013057:Spectrum Analysis; D013379:Substrate Specificity; D014448:Tyrosine-tRNA Ligase / Q000378:metabolism*
chemical_list: D006639:Histidine; D000255:Adenosine Triphosphate; D014448:Tyrosine-tRNA Ligase; D004047:Diethyl Pyrocarbonate
vernacular_title: Tirozil-tRNK-sintetaza iz pecheni byka. Izuchenie funktsional'noĭ roli ostatkov gistidina.