The equilibrium constant of the isocitrate dehydrogenase reaction
نویسندگان
چکیده
منابع مشابه
The equilibrium constant of the isocitrate dehydrogenase reaction.
1. The equilibrium constant for oxidative decarboxylation of isocitrate by NADP(+), catalysed by isocitrate dehydrogenase, was measured in solutions of various ionic strengths and at several temperatures. 2. Thermodynamic values for the reaction were obtained by extrapolation to zero ionic strength, and the heat of reaction was estimated. 3. The effect of Mg(2+) ion concentration on the equilib...
متن کاملThe equilibrium constant of the phosphoglyceromutase reaction.
The equilibrium constant of the phosphoglyceromutase reaction was determined over a range of pH (5.4-7.9), in solutions of different ionic strength (0.06-0.3) and in the presence of Mg(2+), at 30 degrees C and at 20 degrees C. The values obtained (8.65-11.65) differ substantially from previously published values. The third acid dissociation constants were redetermined for 2- and 3-phosphoglycer...
متن کاملThe nature of the carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reaction.
1. It was shown that dissolved CO(2) and not HCO(3) (-) or H(2)CO(3) is the primary substrate for reductive carboxylation with 6-phosphogluconate dehydrogenase from sheep liver. 2. The equilibrium constant of the reaction was measured in solutions of various ionic strengths and at several temperatures, and the free energy and heat of reaction were determined.
متن کاملAn investigation of imine formation in the isocitrate dehydrogenase reaction.
The occurrence of imine formation at the active site of acetoacetate decarboxylase and several aldolases prompted an attempt to demonstrate this mechanism in the formally similar isocitrate dehydrogenase reaction. Although treatment of isocitrate dehydrogenase with NaBH4 in the presence of cr-ketoglutarate resulted in inactivation of the enzyme, reduction in the presence of labeled a-ketoglutar...
متن کاملRole of phosphoenolpyruvate in the NADP-isocitrate dehydrogenase and isocitrate lyase reaction in Escherichia coli.
Phosphoenolpyruvate inhibited Escherichia coli NADP-isocitrate dehydrogenase allosterically (Ki of 0.31 mM) and isocitrate lyase uncompetitively (Ki' of 0.893 mM). Phosphoenolpyruvate enhances the uncompetitive inhibition of isocitrate lyase by increasing isocitrate, which protects isocitrate dehydrogenase from the inhibition, and contributes to the control through the tricarboxylic acid cycle ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1968
ISSN: 0306-3283
DOI: 10.1042/bj1100217