Activation and inhibition of rabbit muscle pyruvate kinase by transition-metal ions.
The paper reports a comparative study of the effects of Mn2+, Ni2+ and Co2+ on the reaction of ADP with phosphoenolypyruvate when catalysed by K+-activated rabbit muscle pyruvate kinase. The activation and subsequent inhibition that occurs as the bivalent ion concentration is increased is taken as evidence that the substrates of the enzyme are phosphoenolypyruvate, uncomplexed ADP and free bivalent cation. Kinetic constants for the binding of the bivalent cation to the enzyme are reported.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D002413:Cations, Divalent; D003035:Cobalt / Q000494:pharmacology; D004789:Enzyme Activation; D008345:Manganese / Q000494:pharmacology; D008670:Metals / Q000494:pharmacology*; D009132:Muscles / Q000201:enzymology*; D009532:Nickel / Q000494:pharmacology; D010728:Phosphoenolpyruvate / Q000378:metabolism; D011188:Potassium / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism*; D011817:Rabbits
D002413:Cations, Divalent; D008670:Metals; D003035:Cobalt; D008345:Manganese; D000244:Adenosine Diphosphate; D010728:Phosphoenolpyruvate; D009532:Nickel; D011770:Pyruvate Kinase; D011188:Potassium