Role of ions in the regulation of porcine lactate dehydrogenase.
Different ions affect the H4 and M4 isoenzymes of porcine lactate dehydrogenase (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) in the same way, inhibiting the enzyme at low pyruvate concentrations, whereas at high pyruvate concentrations, the activities were enhanced. The inhibition was competitive with regard to pyruvate and NADH. The enhancement of the enzyme activity at high pyruvate concentration is due to the increase in the Km value for pyruvate, implying that higher substrate concentrations are needed to obtain substrate inhibition. Sulphate behaved differently from the other ions. It inhibited in a noncompetitive manner with regard to pyruvate and did not activate the enzyme at high pryvuate concentration. The effect of ions increased with the size of the anion. The ionic strength was of less importance.
D000818:Animals; D001965:Bromides / Q000494:pharmacology; D002712:Chlorides / Q000494:pharmacology; D007454:Iodides / Q000494:pharmacology; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D009566:Nitrates / Q000494:pharmacology; D013431:Sulfates / Q000494:pharmacology; D013552:Swine
D001965:Bromides; D002712:Chlorides; D007454:Iodides; D007527:Isoenzymes; D009566:Nitrates; D013431:Sulfates; D007770:L-Lactate Dehydrogenase