Kinase enzyme

Kinase enzymes are a broad class of enzymes that catalyze the transfer of phosphate groups from high-energy donor molecules (mainly ATP) to specific substrates—a process known as phosphorylation[5][7]. Protein kinases, a major subclass, phosphorylate proteins on serine, threonine, tyrosine, or dual-specificity residues and are extensively involved in the regulation of signaling pathways that control cell growth, survival, differentiation, apoptosis, metabolism, and immune responses[7][2][5]. Dysregulation of kinase function is implicated in a wide range of diseases, especially cancers, inflammatory and autoimmune disorders, neurodegenerative conditions, and cardiovascular disease[1][3][7]. Because of their central roles in cellular signaling and disease, kinases represent a core group of therapeutic targets, with numerous small molecule kinase inhibitors approved for use across oncology, immunology, and other fields[3][1]. However, the use of kinase inhibitors is often challenged by issues such as drug resistance, off-target toxicity, and adverse effects, necessitating ongoing research into more selective and effective kinase-targeting therapies[1][3].

Other names

kinaseprotein kinaseserine/threonine kinasetyrosine kinasedual-specificity kinasehistidine kinaselipid kinasecarbohydrate kinase

Competitive inhibition at the ATP-binding site; Allosteric inhibition; Irreversible covalent inhibition; Modulation of kinase activation or inactivation