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Enzymes can also transiently form covalent bonds to phosphate groups during the course of catalytic turnover. In these cases, a phosphoryl—enzyme intermediate is formed by the transfer of an phosphate from substrate molecule or inorganic phosphate to specific amino acid side chains within the enzyme active site. Several examples of phosphoryl—enzyme intermediates are now known, which involve phosphoserine, phosphohistidine, and even phosphoaspartate formation. For example, the ATPases are enzymes that catalyze the hydrolysis of ATP (adenosine triphosphate) to form ADP (adenosine diphosphate) and P . In a subgroup of these enzymes, the Na, K, and the CaATPases, the -phosphate of ATP is transferred to the -carboxylate of an aspartic acid residue of the enzyme during the reaction. Since the phosphoaspartate is thermodynamically unstable, it very quickly dissociates to liberate inorganic phosphate.
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