Nucleotide Binding by the Epidermal Growth Factor Receptor Protein-tyrosine Kinase TRINITROPHENYL-ATP AS A SPECTROSCOPIC PROBE
作者： Kunrong Cheng , John G. Koland
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摘要: The nucleotide binding properties of the epidermal growth factor (EGF) receptor protein-tyrosine kinase were investigated with fluorescent analog 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate (TNP-ATP). TNP-ATP was found to be an active substrate for autophosphorylation reaction recombinant EGF domain (TKD). Whereas Vmax TNP-ATP-dependent approximately 200-fold lower than that ATP, Km this similar observed ATP. also shown inhibitor ATP-dependent and phosphorylation reactions TKD. Spectroscopic studies demonstrated both a high affinity TKD markedly enhanced fluorescence bound analog. enzyme-bound attenuated in presence which enabled determination dissociation constants ATP Mn2+ complex A truncated form lacking C-terminal exhibited TNP-ATP, indicated occupied peptide site modulated substrates.
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