Abstract
At pH 7.0 and physiological concentrations of the main regulatory ligands (ATP, ADP, orthophosphate), human uterine muscle AMP-deaminase follows a hyperbolic type of saturation kinetics with S 0.5 parameter value about 2 mM. The enzyme is regulated by adenylate energy charge (AEC) variations, being the most active at the AEC value 0.5–0.6 or 0.5–0.7, depending on the size of the total adenine nucleotide pool. Long-chain acyl-CoA strongly inhibit activity of the enzyme, influencing mainly the maximum velocity of the reaction.
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