Abstract
Abstract Acetate kinase (ATP:acetate phosphotransferase, EC 2.7.2.1) catalyzes an ADP-ATP and an acetate-acetyl phosphate exchange. The rate of the nucleotide exchange is unaffected by the presence of acetate. The specific rate of the ADP-ATP exchange is 200 times greater than that of the acetate-acetylphosphate exchange. The exchanges and the over-all reaction have pH rate profiles which are separate and distinct from one another. Mercuric ion inhibits to the same degree the over-all reaction and the acetate-acetyl phosphate exchange but is without effect on the ADP-ATP exchange. Catalysis of the two exchanges accords with the mediation of a phosphoenzyme in the action of acetate kinase.
Highlights
2.7.2.1) catalyzes an ADP-ATP and an acetate-acetyl phosphate exchange
The usual laboratory distilled water was redistilled in glass from potassium permanganate and from oxalic acid
Acetate kinase (1) and acetyl phosphate (2) were discovered by Lipmann in the early Forties, and the reaction in which they participate has ever since been an object of interest to students of enzyme mechanism
Summary
2.7.2.1) catalyzes an ADP-ATP and an acetate-acetyl phosphate exchange. The rate of the nucleotide exchange is unaffected by the presence of acetate. The specific rate of the ADP-ATP exchange is 200 times greater changes catalyzed by acetate kinase. They uphold the reality of Reactions 2 and 3. They accord, with the existence of a phosphorylated acetate kinase, which mediates Reaction 1. The phosphoenzyme has since been isolated and briefly reported on (4)
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