ATP-binding enzyme

ATP-binding enzymes represent a vast and diverse superfamily of proteins that utilize the energy derived from adenosine triphosphate (ATP) hydrolysis to catalyze essential biological reactions. This group includes protein kinases, which regulate signal transduction by phosphorylating substrates; ATPases, which power mechanical work and ion transport; and ABC transporters, which facilitate the movement of molecules across cellular membranes (UniProt, 2023). Because ATP is the primary energy currency of the cell, these enzymes are central to nearly every physiological process, including metabolism, DNA repair, and muscle contraction (PubMed, 2021). Dysregulation of ATP-binding enzymes is a hallmark of many diseases, most notably cancer, where hyperactive kinases drive uncontrolled cell proliferation and survival (NIH, 2022). Consequently, they are among the most significant classes of therapeutic targets in modern medicine, with hundreds of inhibitors developed for oncology and other indications (StatPearls, 2023). However, the high degree of structural conservation in the ATP-binding pocket across different enzyme families presents a major challenge for drug selectivity, often leading to off-target effects and therapeutic toxicity (Wikipedia, 2023).

Other names

ATP-utilizing enzymesATPasesKinasesABC transportersNucleotide-binding proteins

Drugs targeting these enzymes typically function as competitive inhibitors that occupy the ATP-binding pocket (orthosteric site), thereby preventing the hydrolysis of ATP or the transfer of its gamma-phosphate group to a substrate (PubMed, 2021).