Roskoski, Robert, Jr. Blue Ridge Institute for Medical Research, Horse Shoe, North Carolina.
- Protein kinase genes
- Serine/threonine protein kinases
- Tyrosine protein kinases
- Protein phosphatases
- Drug targets
- Links to Primary Literature
- Additional Readings
One of a family of enzymes that exert regulatory effects on a variety of cellular functions, as well as malignant transformation, by adding a phosphate group to proteins according to the equation (ATP represents adenosine triphosphate, ADP represents adenosine diphosphate, and OH is a hydroxyl group attached to an amino acid residue.) Based upon the nature of the phosphorylated OH group, these enzymes are classified as serine/threonine protein kinases and tyrosine protein kinases, where serine, threonine, and tyrosine are amino acid residues found in proteins. Furthermore, there is a small group of dual-specificity kinases, which closely resemble serine/threonine kinases, that catalyze the phosphorylation of both threonine and tyrosine on target proteins. The ratio of phosphoserine/phosphothreonine/phosphotyrosine in proteins from animal cells is about 3000/300/1. Despite the scarcity of tyrosine protein phosphate, it plays a paramount role in cell physiology.
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