[Fluorescence spectroscopy studies of interactions of leucyl-tRNA-synthetase with substrates].
Interactions of leucyl-tRNA synthetase with substrates were studied by fluorescence spectroscopy. The formation of enzyme-substrate complexes results in the quenching of protein fluorescence. The equilibrium binding constants were determined for L-leucine, ATP, tRNAleu and leucyladenylate. It is shown that the interaction of the enzyme with ATP or tRNAleu leads to 10-30-fold increase in the binding constants for subsequent interaction of the second substrate. The data obtained indicate to the cooperative interaction between ATP and tRNA binding sites.
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D005260:Female; D007700:Kinetics; D007930:Leucine; D007935:Leucine-tRNA Ligase / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000201:enzymology; D012346:RNA, Transfer, Amino Acyl; D013050:Spectrometry, Fluorescence; D046249:Transfer RNA Aminoacylation
D012346:RNA, Transfer, Amino Acyl; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases; D007935:Leucine-tRNA Ligase; D007930:Leucine
Izuchenie vzaimodeĭstviia leĭtsil-tRNK-sintetazy s substratami metodom fluorestsentnoĭ spektroskopii.