Reversibility of the epidermal growth factor receptor self-phosphorylation reaction. Evidence for formation of a high energy phosphotyrosine bond.
作者： L Hubler , G N Gill , P J Bertics
DOI: 10.1016/S0021-9258(18)94223-7
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摘要: Abstract The reversibility of the epidermal growth factor (EGF) receptor self-phosphorylation reaction was studied using highly purified from A431 human epidermoid carcinoma cells. Self-phosphorylation is inhibited by product ADP in a dose-dependent manner exhibiting an IC50 approximately 2 microM. In addition, phosphorylated EGF can be rapidly dephosphorylated presence ADP. dephosphorylation results equimolar production ATP and loss phosphate receptor. reverse dependent on time t1/2 15 s Km(ADP) = 0.40 +/- 0.14 effectively exogenous peptide substrate for forward reaction, i.e., src-peptide (a synthetic corresponding to one sites p60v-src). This suggests that intrinsic equilibrium constant, K, estimated 0.5-1.6 kinetic reactant/product concentration analyses. Assuming standard free energy change, delta G0, hydrolysis -9.5 kcal/mol, observed G0 phosphotyrosine bond calculated -9 -10 kcal/mol. These indicate which appears important regulation function, readily reversible formed this relatively high energy.
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