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Protein Kinases (PTKs) are a class of enzymes that regulate the biological activity of proteins by phosphorylating a specific amino acid using ATP as the source of phosphate, thereby introducing a dynamic conformational change from an inactive to an active form of the protein. The PTK family has emerged as one of the most significant drug targets in the twenty-first century due to the dysregulation of protein kinase function in several diseases, including cancer. PTKs play a significant role in intracellular transduction on account of their ability to phosphorylate many proteins. Eukaryotic protein kinases are enzymes that catalyse the transfer of phosphoryl from MgATP to proteins' Ser/Thr and Tyr side chains. Their prevalence in eukaryotic genomes, representing 2-3% of the genes, including in the human genome, where 518 protein kinases have been annotated, serves as some indication of their significance. PKTs are intracellular enzymes regulating cell growth and proliferation as well as the induction and regulation of immune responses. They are important therapeutic targets in cancer due to their role in signalling mechanisms that drive malignant cell characteristics. Phosphorylation by various kinases is important in many biological processes, including enzyme activation, regulation, metabolism, cell signaling, cell division, and more.
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