Rivedal E, Sanner T
Biochim Biophys Acta. 1979 Mar 16;567(1):60-5. doi: 10.1016/0005-2744(79)90172-4.
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.
不同离子对猪乳酸脱氢酶(L-乳酸:NAD+氧化还原酶,EC 1.1.1.27)的H4和M4同工酶的影响方式相同,即在低丙酮酸浓度下抑制该酶,而在高丙酮酸浓度下,酶活性增强。这种抑制作用对丙酮酸和NADH具有竞争性。高丙酮酸浓度下酶活性的增强是由于丙酮酸的Km值增加,这意味着需要更高的底物浓度才能产生底物抑制。硫酸根的行为与其他离子不同。它对丙酮酸的抑制作用是非竞争性的,并且在高丙酮酸浓度下不会激活该酶。离子的作用随着阴离子大小的增加而增强。离子强度的影响较小。