Effect of pH on the inhibition of the nicotinamide-adenine dinucleotide-specific isocitrate dehydrogenase from baker's yeast by anions.
نویسندگان
چکیده
1. The sensitivity of the NAD(+)-specific isocitrate dehydrogenase from baker's yeast towards inhibition by anions decreases with decrease in pH. The patterns of the pH-dependence of the enzymic activity can be explained by this effect. 2. In the presence of a high isocitrate concentration, citrate, unlike AMP, has no antagonizing effect on the inhibition of the enzyme by anions. In the presence of AMP, citrate inhibits the enzyme at high isocitrate concentration and activates at low isocitrate concentration. 3. The effects on the enzymic activity of the previous incubation of the enzyme were studied in relation to the substrate concentration, the chloride concentration and the presence of citrate and AMP.
منابع مشابه
The Effect of Adenylic Acid on Yeast Nicotinamide Adenine Dinucleotide Isocitrate Dehydrogenase, a Possible Metabolic Control Mechanism.
The nicotinamide adenine dmucleotide-specific isocitrate dehydrogenase of yeast was reported by Kornberg and Pricer (1) to have an absolute requirement for adenylic acid and not to catalyze the reverse reaction under conditions suitable for such catalysis by the nicotinamide adenine dinucleotide phosphatespecific enzyme. Similar results have been obtained for the nicotinamide adenine dinucleoti...
متن کاملDinucleotide-Specific Isocitrate Dehydrogenase from Pea Mitochondria By G. F. COX AD
1. The effect ofpH on the co-operative activation of the NAD-specific isocitrate dehydrogenase from pea mitochondria by isocitrate is shown. 2. The interlinked effects of pH on the affinity of the NAD-specific isocitrate dehydrogenase for isocitrate and the dependence of the pH optimum on the substrate concentration are presented. 3. A consideration of the conditions ofpH and substrate concentr...
متن کاملPurification and characterization of NAD-isocitrate dehydrogenase from chlamydomonas reinhardtii
NAD-isocitrate dehydrogenase (NAD-IDH) from the eukaryotic microalga Chlamydomonas reinhardtii was purified to electrophoretic homogeneity by successive chromatography steps on Phenyl-Sepharose, Blue-Sepharose, diethylaminoethyl-Sephacel, and Sephacryl S-300 (all Pharmacia Biotech). The 320-kD enzyme was found to be an octamer composed of 45-kD subunits. The presence of isocitrate plus Mn2+ pro...
متن کاملREASSOCIATION AND REACTIVATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM STREPTOMYCES AUREOFACIENS AFTER DENATURATION BY 6 M UREA
Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...
متن کاملRegulation of the nicotinamide adenine dinucleotide-specific isocitrate dehydrogenase from a higher plant. The effect of reduced nicotinamide adenine dinucleotide and mixtures of citrate and isocitrate.
The NAD+-specific isocitrate dehydrogenase from pea stems is shown to respond to the mole fraction of NADH when total NAD (NAD+ plus NADH) is kept constant. Fifty per cent inhibition occurs when the mole fraction of NADH is 0.1. In this region the enzyme is extremely sensitive to NADH concentration and it is suggested that this acts in a similar manner to energy charge in other systems. In an a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 109 3 شماره
صفحات -
تاریخ انتشار 1968