Purification and properties of AMP-deaminase from human uterine smooth muscle. Regulation by adenylate energy charge and activated fatty acids.
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 S0.5 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.
Nowak
G
G
Department of Biochemistry, Academic Medical School, Gdańsk, Poland.
Nagel-Starczynowska
G
G
Kaletha
K
K
D000659:AMP Deaminase / Q000302:isolation & purification / Q000378:metabolism*; D000249:Adenosine Monophosphate / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism*; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009130:Muscle, Smooth / Q000201:enzymology*; D014599:Uterus / Q000201:enzymology*
D005227:Fatty Acids; D000249:Adenosine Monophosphate; D000659:AMP Deaminase