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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Chemical influences on the specificity of tyrosine phosphorylation.

Biological tyrosine phosphorylation has become an extensively studied reaction. Little, however, is known of the chemistry involved. The acetylation of the tyrosyl phenolic hydroxyl group by N-acetylimidazole was studied as a model acylation reaction over the pH range 7.5-9. 5. The reactivities of tyrosine and 3-fluorotyrosine were compared. The ratio of reactivities, kappa F-Tyr/kappa Tyr, decreases with increasing pH. Extrapolation to the state in which equivalent concentrations of the two derivatives exist indicates that, consistent with Brønsted theory, tyrosine is 17 times more reactive than fluorotyrosine. No reactivity was observed with tetrafluorotyrosine, 3-nitrotyrosine, or 3,5-dinitrotyrosine. A peptide containing fluorotyrosine was synthesized and compared with the tyrosine-containing peptide as a substrate for the insulin receptor/tyrosine kinase. In both the presence and absence of insulin, the tyrosine peptide was phosphorylated with higher Vm and Km values than the fluorotyrosine peptide was. These results suggest that ionization of the tyrosyl hydroxyl group has an effect on both the chemical and enzymatic reactivities of the tyrosyl residue in acylation reactions. A model is suggested in which deprotonation of the acceptor occurs upon binding of the substrate to the kinase and implicates a role for the substrate site microenvironment in defining substrate specificity.[1]

References

  1. Chemical influences on the specificity of tyrosine phosphorylation. Martin, B.L., Wu, D., Jakes, S., Graves, D.J. J. Biol. Chem. (1990) [Pubmed]
 
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