Effect of adenosine 5'-monophosphate on adenosine 5'-triphosphate activation of methyl coenzyme M methylreductase in cell extracts of Methanosarcina barkeri.
In cell extracts of Methanosarcina barkeri, adenosine 5'-triphosphate (ATP)-activated methyl coenzyme M methylreductase was inhibited by adenosine 5'-monophosphate (AMP) but not by cyclic AMP. AMP (2 and 4 mM) shifted the saturation curve for ATP activation from hyperbolic (Hill coefficient [n] = 1.0) to sigmoidal (n = 1.5), decreased Vmax, and increased the apparent KmATP.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D019605:Euryarchaeota / Q000201:enzymology*; D007700:Kinetics; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D000227:Adenine Nucleotides; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D010088:Oxidoreductases; C023895:methyl coenzyme M methylreductase