Protein kinases catalyze the transfer of the ?-phosphoryl group
of ATP to serine, threonine, and tyrosine residues in proteins, a
process essential for cell signaling. Although there may be as many
as 2000 kinases in the human genome, the organization of the
residues in the active sites of these enzymes is essentially the same
(conserved).1 Even after many structural and kinetic measurements,
there is still considerable controversy regarding the role of these
residues in the enzyme mechanism.
Revised: April 7, 2011 |
Published: July 23, 2003
Citation
Valiev M., R. Kawai, J.A. Adams, and J.H. Weare. 2003.The Role of the Putative Catalytic Base in the Phosphoryl Transfer Reaction in a Protein Kinase: First Principles Calculations.Journal of the American Chemical Society 125, no. 33:9926-9927.