Understanding Protein Kinases: Critical Regulators of Biological Processes in Health and Disease

Enzymes that modify protein groups by the transfer of a phosphate group

Kinase

Enzymes that modify protein groups by the transfer of a phosphate group are called protein kinases. These enzymes are responsible for phosphorylation, a common post-translational modification where a phosphate group is added to a protein molecule. Phosphorylation plays a critical role in regulating biological pathways and processes, including cell division, metabolism, gene expression, and signal transduction.

Protein kinases use ATP as a source of phosphate and catalyze the transfer of the phosphate group from ATP to specific amino acid residues within the target protein. The most common amino acids that are phosphorylated are serine, threonine, and tyrosine, although other amino acids such as histidine and aspartic acid can also be phosphorylated in some cases.

There are over 500 different protein kinases in humans, each with specific target substrates and biological functions. The dysregulation of protein kinase activity has been implicated in many diseases, including cancer, diabetes, and neurodegenerative disorders. As such, protein kinases have become an important target for drug development, and many kinase inhibitors are currently in clinical use or under development for the treatment of various diseases.

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