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Calbiochem Information
Signal Transduction Resource
Protein Kinase Activators
 
 
Protein phosphorylation corresponds to one of the most important molecular mechanisms by which extracellular signals produce their biological responses in cells. Stimulation of protein kinases is considered to be one of the most common activation mechanism in signal transduction systems. Protein phosphorylation systems are composed of at least three components: (a) phosphoproteins, that alter their properties during phosphorylation-dephosphorylation; (b) protein kinases, that transfer a phosphate group from ATP to specific serine, threonine, or tyrosine residues on proteins; and (c) protein phosphotases, that dephosphorylate the phosphoproteins, thereby restoring the particular protein phosphorylation system to its basal stage. The eukaryotic protein kinases constitute one of the largest superfamilies of homologous proteins that are related by virtue of their catalytic domains. Most related protein kinases are specific for either serine/threonine or tyrosine phosphorylation. At least three principal mechanisms have been proposed for the activation of various protein kinases. Figure 17 outlines some of the major pathways involved in the regulatory mechanisms. Many substrates are known to undergo phosphorylation by multiple protein kinases. Most protein kinases possess a 30 - 32 kDa catalytic domain that is well conserved throughout the phylogeny. A considerable amount of information on primary sequence of the catalytic domains of various protein kinases has been published. These sequences share a large number of residues involved in ATP binding, catalysis, and maintenance of structural integrity. Protein kinases have a latent catalytic activity and removal of the inhibitory constraints induces activation of the enzyme.
 
 
PKA Activators
 
PKC Activators
 
PKG Activators
 
 
Related Links
PTK Interactive Pathway™
PKC Interactive Pathway™ & Products

MAPK Interactive Pathway™

Akt Interactive Pathway™
Phosphorylation/Dephosphorylation Inhibitors