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ATP-utilizing enzymes comprise a diverse set of molecular machines that use the chemical energy in ATP to catalyze and regulate biological processes. Major subclasses include ATPases, which hydrolyze ATP to drive active transport, regulate ion gradients, or perform mechanical work; kinases, which transfer phosphate groups for signaling and regulatory functions; ATP synthase, which generates ATP using membrane potential; and ligases or synthetases, which use ATP to activate substrates for biosynthetic reactions. These enzymes are universal across all domains of life and are fundamental to cell viability. Their dysfunction is associated with diseases such as cancer, neurodegenerative and cardiovascular disorders, and they are targets for many modern drugs.
Drugs targeting ATP-utilizing enzymes can act via ATP-competitive inhibition (e.g., kinases), allosteric modulation (e.g., ribonucleotide reductase, kinases), covalent modification of catalytic residues (e.g., kinase active site, ABC transporter NBD), interference with ATP synthesis/hydrolysis (e.g., ATP synthase, ATPases), or substrate trapping or mimicking (small molecules preventing phosphorylation or ATP binding).
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