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Chemical model for oxaloacetate decarboxylase
Bioinorganic Chemistry, 1974Abstract Spectroscopic studies on the formation of metal complexes and rate studies on the metal catalyzed decarboxylation of oxaloacetate and its esters indicate that oxaloacetate, in the presence of metal ions, decarboxylates according to the mechanism of Steinberger and Westheimer [9].
C.S. Tsai +3 more
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Permeability of isolated mitochondria to oxaloacetate
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973Abstract 1. 1. The transport of oxaloacetate in mitochondria from several sources has been studied. 2. 2. Oxaloacetate is rapidly transported across the membrane of isolated ratliver mitochondria. The V is 80–270 nmoles/min per mg protein at 30 °C. The K m for oxaloacetate is 80–130 μM. 3. 3.
E.J. De Haan +2 more
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Micrometer-Sized Water Droplets Induce Spontaneous Reduction.
Journal of the American Chemical Society, 2019Bulk water serves as an inert solvent for many chemical and biological reactions. Here, we report a striking exception. We observe that in micrometer-sized water droplets (microdroplets), spontaneous reduction of several organic molecules occurs ...
Jae Kyoo Lee +3 more
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Tight binding of oxaloacetate to succinate dehydrogenase
Biochemical and Biophysical Research Communications, 1973Abstract [14C]Oxaloacetate forms a stable complex with succinate dehydrogenase which withstands repeated Sephadex filtration. Oxidized glutathione, 2-thenoyltrifluoroacetone, KCN and ageing at +4° at neutral pH do not prevent the enzyme to bind oxaloacetate.
Lech Wojtczak +2 more
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A new assay for glutamate-oxaloacetate transaminase
Analytical Biochemistry, 1970Abstract A new method for continuously measuring glutamate-oxaloacetate transaminase (GOT) activity is described. Oxaloacetate produced by GOT from aspartate is condensed with acetyl CoA to form citrate and CoA in a system coupled with citrate synthase. The CoASH formed is measured by its reaction with DTNB.
Paul A. Srere, Hajime Itoh
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Glutamic-Oxaloacetic Transaminases in Reticulocytes and Erythrocytes
Science, 1965In rabbits, mature erythrocytes contain only the anionic isozyme of glutamic-oxaloacetic transaminase. Reticulocytosis induced by massive bleeding or by treatment with acetylphenylhydrazine is characterized by a five- to sixfold increase in red-cell transaminase and the appearance of a cationic transaminase isozyme that apparently resides in the ...
J. S. Nisselbaum, Oscar Bodansky
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Oxaloacetate inhibition of aconitate hydratase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1969Abstract An oxaloacetate-Fe 2+ complex has been found to be a potent competitive inhibitor of aconitate hydratase. The requirement for both oxaloacetate and Fe 2+ in this inhibition appears to be absolute.
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Regulation of succinate dehydrogenase and tautomerization of oxaloacetate
Advances in Enzyme Regulation, 1989Highly purified succinate-ubiquinone reductase catalyzes the oxidation of L- or D-malate with a Km and initial Vmax equal to approximately 10(-3) M and approximately 100 nmol/min/mg of protein, respectively. The malate dehydrogenase activity of succinate dehydrogenase rapidly decreases regardless of the presence of glutamate plus glutamate-oxaloacetate
Alexander Kotlyar +3 more
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Oxaloacetate translocator in plant mitochondria
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1985In plant mitochondria, respiration of NADH linked substrates, such as 2-oxoglutarate or glycine, can be almost totally inhibited by the addition of oxaloacetate, the inhibition being due to reoxidation of the internal NADH by oxaloacetate, as catalyzed by mitochondrial malate dehydrogenase (Walker and Beevers 1956; Woo and Osmond 1976; Journet et al ...
H. Ebbighausen, Hans W. Heldt, Chen Jia
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The binding site for oxaloacetate on succinate dehydrogenase
Biochemical and Biophysical Research Communications, 1972Abstract Oxaloacetate, a competitive inhibitor of succinate dehydrogenase, bound with a sulfhydryl group of the enzyme to abolish the enzymic activity. Subsequently a thiosemiacetal was apparently formed to render the inhibition practically irreversible. The dehydrogenase, after taking up 25 silver equivalents per flavin, bound little oxaloacetate.
Daryl B. Winter +2 more
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