title: [Stabilization of the transition state in the active center of aminoacyl-tRNA-synthetase].
abstract: The mechanism for transition state stabilization in the activation of amino acids by aminoacyl-tRNA synthetases is proposed. We carried out a quantum mechanical study on system modelling the attack of the amino acid carboxylate on the alpha-phosphate group of ATP. The activation barrier is reduced by improved hydrogen binding between a phosphoryl oxygen atom and a proton donor group of the enzyme. The relative stabilization of the transition state is found to be about 8 kcal/mol. On the basis of results obtained for the reaction in gas phase, in aqueous solution and in the active site the nature of the enzyme catalysis is discussed.
authors.forename: A A
authors.initials: AA
authors.lastname: Voĭtiuk
authors.forename: A A
authors.initials: AA
authors.lastname: Blizniuk
authors.forename: O I
authors.initials: OI
authors.lastname: Lavrik
mesh_terms: D000604:Amino Acyl-tRNA Synthetases; D001665:Binding Sites; D011487:Protein Conformation
chemical_list: D000604:Amino Acyl-tRNA Synthetases
vernacular_title: Stabilizatsiia perekhodnogo sostoianiia v aktivnom tsentre aminoatsil-tRNK-sintetaz.