title: Purification and properties of AMP-deaminase from human uterine smooth muscle. Regulation by adenylate energy charge and activated fatty acids.
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 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.
authors.affiliation: Department of Biochemistry, Academic Medical School, Gdańsk, Poland.
authors.forename: G
authors.initials: G
authors.lastname: Nowak
authors.forename: G
authors.initials: G
authors.lastname: Nagel-Starczynowska
authors.forename: K
authors.initials: K
authors.lastname: Kaletha
mesh_terms: 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*
chemical_list: D005227:Fatty Acids; D000249:Adenosine Monophosphate; D000659:AMP Deaminase