Results 171 to 180 of about 294 (201)
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Coexistence of isocitrate lyase and NADP-isocitrate dehydrogenase in Turbatrix aceti mitochondria
Biochemical and Biophysical Research Communications, 1978Abstract Glyoxylate and Krebs cycle marker enzymes cobanded on sucrose gradients after isopycnic centrifugation of mitochondrial pellets. Mitochondrial heterogeneity was investigated by treating particles with a Nitro Blue Tetrazolium reaction mixture designed to specifically increase the buoyant density of mitochondria containing the Krebs cycle ...
M P, McKinley, R N, Trelease
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Isocitrate dehydrogenase of Tetrahymena pyriformis
Molecular and Cellular Biochemistry, 1977We 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.
P, Vidal, A, Machado
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On the Mechanism of Action of Isocitrate Lyase
European Journal of Biochemistry, 1975The enzymes citrate lyase and isocitrate lyase catalyse similar reactions in the cleavage of citrate to acetate plus oxaloacetate and of isocitrate to succinate plus glyoxylate, respectively. Nevertheless, the mechanism of action of each enzyme appears to be different from each other. Citrate lyase is an acyl carrier protein‐containing enzyme complex
P, Dimroth, K, Mayer, H, Eggerer
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Isocitrate dehydrogenase kinase/phosphatase
Biochimie, 1989In Escherichia coli, isocitrate dehydrogenase (IDH) is regulated by phosphorylation. This phosphorylation cycle is catalyzed by an unusual, bifunctional protein:IDH kinase/phosphatase. IDH kinase/phosphatase is expressed from a single gene, aceK, and both activities are catalyzed by the same polypeptide.
D C, Laporte, C S, Stueland, T P, Ikeda
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The isocitrate dehydrogenase from cyanobacteria
Archives of Microbiology, 1983The present communication describes the properties of isocitrate dehydrogenase in crude extracts from the unicellular Anacystis nidulans and from heterocysts and vegetative cells of Nostoc muscorum and Anabaena cylindrica. The activity levels of this enzyme are much higher in heterocysts than in vegetative cells of N. muscorum and A.
H, Papen, G, Neuer, M, Refaian, H, Bothe
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Phosphorylation of acinetobacter isocitrate lyase
Biochemical and Biophysical Research Communications, 1992During growth on succinate, Acinetobacter calcoaceticus contains two forms of the enzyme isocitrate dehydrogenase. Addition of acetate to a lag-phase culture grown on succinate causes a dramatic increase in activity of form II of isocitrate dehydrogenase and in isocitrate lyase.
J C, Hoyt, H C, Reeves
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Role of isocitrate dehydrogenase in glioma
Expert Review of Neurotherapeutics, 2011Recently, the isocitrate dehydrogenase (IDH) enzymes have become a focal point for research aimed at understanding the biology of glioma and identifying novel targets for therapy. Following the publication of a landmark genetic sequencing study in 2008, which identified IDH1 as a frequently mutated gene in glioblastoma, much work has been carried out ...
Brian M, Alexander, Minesh P, Mehta
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Biochemistry, 1975
D-Garcinia acid (D-threo-1,2-dihydroxy-1,2,3-propanetricarboxylate), like D-isocitrate, has an alpha-DS-hydroxyl group and a beta-LS configuration of the second carboxyl group. The maximal velocity of pyridine nucleotide reduction with D-garcinia acid is 8 and 21% of D-threo-isocitrate with the DPN-linked and TPN-linked isocitrate dehydrogenase from ...
G W, Plaut, R L, Beach, T, Aogaichi
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D-Garcinia acid (D-threo-1,2-dihydroxy-1,2,3-propanetricarboxylate), like D-isocitrate, has an alpha-DS-hydroxyl group and a beta-LS configuration of the second carboxyl group. The maximal velocity of pyridine nucleotide reduction with D-garcinia acid is 8 and 21% of D-threo-isocitrate with the DPN-linked and TPN-linked isocitrate dehydrogenase from ...
G W, Plaut, R L, Beach, T, Aogaichi
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Physiologia Plantarum, 1993
In the green alga Chlamydomonas reinhardtii, nitrogen staravation induced a reversible increase (2‐fold) in NAD‐isocitrate dehydrogenase (NAD‐IDH; EC 1.1.1.41) and NADP‐isocitrate dehydrogenase (NADP‐IDH; EC 1.1.1.42) activities. Both enzymes were not affected by the concentration of CO2, the dark or the nature of the nitrogen source (nitrate, nitrite,
José M, Martínez-Rivas, José M, Vega
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In the green alga Chlamydomonas reinhardtii, nitrogen staravation induced a reversible increase (2‐fold) in NAD‐isocitrate dehydrogenase (NAD‐IDH; EC 1.1.1.41) and NADP‐isocitrate dehydrogenase (NADP‐IDH; EC 1.1.1.42) activities. Both enzymes were not affected by the concentration of CO2, the dark or the nature of the nitrogen source (nitrate, nitrite,
José M, Martínez-Rivas, José M, Vega
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Isocitrate lyase of conifers (Pinus pinea
International Journal of Biochemistry, 19821. Isocitrate lyase has been purified about 60 times from the conifer Pinus pinea. A first characterization was made. 2. The high instability is an important feature of this enzyme from higher plants, this causes serious problems in the purification and characterization. 3.
PINZAUTI, GIANCARLO +2 more
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