Comparison of the ATP-[32P]pyrophosphate exchange reactions catalysed by native (two-site) and chemically modified (one-site) tryptophanyl-tRNA synthetase.
Explore the source record for details and available documents.
Adenosine Triphosphate↗
Biomedical subjects
V V Zinoviev
Publications and source records attributed to V V Zinoviev.
Interaction of aminoacyl-tRNA synthetases and tRNA: positive and negative cooperativity of their active centres.
The influence of tRNA on the kinetics of PP-ATP exchange and aminoacyl-tRNA formation catalysed by leucyl-, phenylalanyl-, and tryptophanyl-tRNA synthetases has been investigated. These enzymes were chosen because they belong to three main classes of quaternary structure alpha1, alpha2beta2 and alpha2, respectively. The present paper shows that the investigated synthetases manifest kinetic cooperativity of the active centres which is negative in the case of AAA formation and positive in the case of leucyl- and tryptophanyl-tRNA synthesis. The obtained data were interpreted with the aid of the trigger model of the enzyme.
Adenosine Triphosphate↗
Kinetic parameters of tryptophan: tRNA ligase catalyzed ATP-(32P) pyrophosphate exchange as an approach to extimation of the order of substrate binding.
Explore the source record for details and available documents.
Adenosine Triphosphate↗