Abstract
The cleavage of ATP has been investigated with 18O in several phosphokinase reactions, namely yeast hexokinase, phosphoglycerate kinase, and adenylate kinase, and in the hydrolysis of ATP catalyzed by a Mg ++-activated ATPase in muscle extract. In all these reactions, the bond was cleaved between oxygen and the terminal P of ATP. The cleavage of 1,3-diphosphoglyceric acid was investigated in the glyceraldehyde-3-phosphate dehydrogenase reaction and the phosphoglycerate kinase reaction. In the first reaction, the CO bond was cleaved and in the second reaction the OP bond was cleaved. The mechanism of these reactions is discussed in relation to the behavior of 1,3 diphosphoglyceric acid as an acyl or phosphate donor. Comparison with other reactions reveals a general pattern in analogous reactions.
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