Vidal P, Machado A
Mol Cell Biochem. 1977 Oct 7;17(3):151-6. doi: 10.1007/BF01730835.
We have studied the isocitrate dehydrogenase of Tetrahymena pyriformis. This enzyme is able to utilize both NAD and NADP, but kinetic studies suggest that the enzymatic activity with NAD is not of physiological signifance. Some of the factors that might regualte the NADP-dependent isocitrate dehydrogenase were also studied. This enzyme has an absolute requirement for divalent cations; Mg,+ and Mn2+ will serve as cofactors but the latter is more effective than the former. It is known that this enzyme is subject to a concerted inhibition by oxaloacetate and glyoxylate. Either glyoxylate or oxaloacetate alone also are capable of inhibiting the enzyme although higher concentrations are required. We have found concerted inhibition also for the NAD-dependent isocitrate dehydrogenase from rat liver and yeast. The activity of the Tetrahymena pyriformis enzyme is inhibited by NADPH. This inhibition is competitive with NADP. The Ki and Km values are, respectively, 20 micrometers and 18 micrometers.
我们研究了梨形四膜虫的异柠檬酸脱氢酶。这种酶能够利用NAD和NADP,但动力学研究表明,NAD的酶活性没有生理意义。我们还研究了一些可能调节依赖NADP的异柠檬酸脱氢酶的因素。这种酶对二价阳离子有绝对需求;Mg²⁺和Mn²⁺可作为辅因子,但后者比前者更有效。已知这种酶受到草酰乙酸和乙醛酸的协同抑制。单独的乙醛酸或草酰乙酸也能够抑制该酶,尽管需要更高的浓度。我们还发现大鼠肝脏和酵母中依赖NAD的异柠檬酸脱氢酶也存在协同抑制。梨形四膜虫的这种酶的活性受到NADPH的抑制。这种抑制与NADP竞争。Ki和Km值分别为20微摩尔和18微摩尔。