Abstract
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.
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Selected References
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