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Protein kinases are enzymes that transfer phosphate groups to proteins in a reaction that requires ATP as a phosphate donor and enzyme catalyst. Serine-threonine kinases phosphorylate proteins on serine or threonine residues and tyrosine kinases phosphorylate proteins on tyrosine residues. Phosphorylation regulates the activity of certain proteins.

The kinase enzyme catalyses the transfer of the terminal phosphate group of ATP to the hydroxyl moiety in the amino acid residue. Phosphatases are enzymes which remove a phosphate group from a protein. These two enzymatic processes control protein activities in the cell and are involved in functions like responding to external stimuli. Kinases turn on protein function on and phosphatases turn proteins off. Most kinases promote cell proliferation, survival and migration when active or overexpressed and their malfunction is associated with cancer. Inherited mutations in kinases are associated with cancer.

Drug discovery

There are 538 kinases encoded in the human genome. The kinome of an organism is the complete set of protein kinases encoded by the genome. Since many kinases are associated with human cancer, they have become the second most targeted group of for cancer drugs. Synthetic and natural kinase inhibitors are therapeutic strategies for treating malignancies.

Synthetic biology

In the field of synthetic biology phosphorylation circuits have been engineered using phosphor-regulon motifs that act as biological switches which can change cell fate in yeast. Opto-kinases are optogenetics tools that allow the activation of inhibition of proteins kinases with light.


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