[Interaction between tRNA-recognizing sites of phenylalanyl-tRNA synthetase from Escherichia coli MRE-600].
Modification of phenylalanyl-tRNA synthetase by N-Br-Ac-[14C]Phe-tRNAPhe results in two products, one being stable in alkaline conditions and the other being instable. The instable product is formed in the presence of an equimolar excess of the reagent over the enzyme while the stable one--in the presence of a tenfold excess. The experimental results are described by a kinetic model which takes into account the existence of two routes of modification of product formation. The first route is from the complex containing one molecule of the reagent and the other from the complex containing two molecules of the reagent. It is assumed that the presence of the molecule of the reagent in one center of the dimeric enzyme induces a change in the acceptor point of the other center, which leads to local conformational changes of the enzyme molecule interacting with the substrate analogue.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008433:Mathematics; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000494:pharmacology*
D012346:RNA, Transfer, Amino Acyl; C032617:tRNA, N-bromoacetylphenylalanine-; D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase
Vzaimodeĭstvie tRNK-uznaiushchikh uchastkov v fenilalanil-tRNK-sintetaze iz Escherichia coli MRE-600.