Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.37 (malate dehydrogenase)
 4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Little evidence has been available on the oxidative pathways of glutamine and glutamate, the major respiratory substrates of cancer cells. Glutamate formed from glutamine by phosphate-dependent glutaminase undergoes quantitative transamination by aerobic tumor mitochondria to yield aspartate. However, when malate is also added there is a pronounced decrease in aspartate production and a large formation of citrate and alanine, in both state 3 and 4 conditions. In contrast, addition of malate to normal rat heart, liver, or kidney mitochondria oxidizing glutamate causes a marked increase in aspartate production. Further analysis showed that extramitochondrial malate is oxidized almost quantitatively to pyruvate + CO2 by NAD(P)+-linked malic enzyme, present in the mitochondria of all tumors tested, but absent in heart, liver, and kidney mitochondria. On the other hand intramitochondrial malate generated from glutamate is oxidized quantitatively to oxalacetate by mitochondrial malate dehydrogenase of tumors. Acetyl-CoA derived from extramitochondrial malate via pyruvate and oxalacetate derived from glutamate via intramitochondrial malate are quantitatively converted into citrate, which is extruded. No evidence was found that malic enzyme of tumor mitochondria converts glutamate-derived malate into pyruvate as postulated in other reports. Possible mechanisms for the integration of mitochondrial malic enzyme and malate dehydrogenase activities in tumors are discussed.
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PMID:The pathways of glutamate and glutamine oxidation by tumor cell mitochondria. Role of mitochondrial NAD(P)+-dependent malic enzyme. 614 77

The activity and properties of malate dehydrogenase (MDH; EC 1.1.1.37) and of "malic" enzyme (EC 1.1.1.40) in cytosole of the trematode C. ijimai were determined. The activity of MDH directed to oxaloacetate formation was shown to be 14 times and maximum velocity 13 times lower than that of the reverse reaction. The apparent KM was one order higher in the direct reaction. This confirms the possibility of glycolytic pathway in C. ijimai via CO2 fixation into phosphoenolpyruvate to form oxaloacatate which is readily eliminated by active MDH. The presence of "malic" enzyme in C. ijimai testifies to the occurrence of different pathways of succinate formation in this species.
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PMID:[Cytosol malate dehydrogenase in Calicophoron ijimai trematodes and the effect of antiparasitic preparations on its activity]. 635 24

1. Both Isotricha intestinalis and I. prostoma possess microbody-like organelles, with a highly granular appearance. 2. These organelles, which are sedimentable at 10(5) g-min, bear no morphological similarity to mitochondria, but are enzymatically similar to organelles possessed by certain other anaerobic protozoa and termed hydrogenosomes. 3. The hydrogenosomes isolated from a preparation of mixed isotrichs bear a closer similarity to those isolated from the other rumen holotrich. Dasytricha ruminantium, than those recently identified in a mixed entodiniomorph preparation, or the trichomonads, in that the enzyme malate dehydrogenase (decarboxylating) is non-sedimentable and phosphoacetyl transferase together with acetate kinase are involved in the transformation of acetyl CoA to acetate. 4. The results enable a scheme of acetate, CO2 and H2 formation from carbohydrates to be proposed and extends the number of protozoa known to possess this organelle.
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PMID:Hydrogenosomes in a mixed isolate of Isotricha prostoma and Isotricha intestinalis from ovine rumen contents. 640 85

This work was done to discover how those nonphotosynthetic tissues of the Araceae that become thermogenic release, as CO2, carbon recently fixed by phosphoenolpyruvate carboxylase. Extracts of clubs of the spadix of Arum maculatum showed no activity for phosphoenolpyruvate carboxykinase and low activities of NADP malic enzyme. NAD malic enzyme activity in the above extracts and in those of thermogenic tissues of other Araceae was appreciable. Analysis of homogenates of clubs of Typhonium giraldii by differential centrifugation and sucrose gradients showed that NAD malic enzyme was confined to mitochondria. Centrifugation of mitochondria after freezing and thawing left all the NAD malic enzyme in the supernatant. NAD malic enzyme in isolated, intact mitochondria was completely latent, and was completely protected from exogenous trypsin. The responses of this latency and protection to different concentrations of Triton X-100 suggested that none of the NAD malic enzyme was accessible from either the outside or the intermembrane space of the mitochondria. Treatment of excised clubs of A. maculatum with 2-N-butylmalonate largely prevented the development of the rapid respiration responsible for thermogenesis, and severely inhibited dark fixation of 14CO2. The conclusion is that in mature clubs of the Araceae phosphoenolpyruvate is converted to malate in the cytosol by phosphoenolpyruvate carboxylase and NAD malate dehydrogenase, and that this malate then enters the mitochondrial matrix where it is converted to pyruvate by NAD malic enzyme.
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PMID:Role and location of NAD malic enzyme in thermogenic tissues of Araceae. 642 Dec 32

IR spectra of NAD-dependent malate dehydrogenase in the deuterium oxide solutions were studied in the absence of CO2 and at solution saturation with it. The presence of CO2 in the system results in weakening the absorption band intensity at 1650 cm-1 and in the appearance of the band at 1543 cm-1, which is explained by the formation of carbamates under conditions of the protein molecules free amino groups interaction with CO2.
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PMID:[Possible mechanism of CO2 interaction with NAD-dependent malate dehydrogenase]. 676 90

This paper reports for the first time the presence in the anaerobic rumen ciliate Dasytricha ruminantium (Schuberg) of microbody-like organelles, about 0.5 micrometer diameter, with a granular matrix and an equilibrium density of approx. 1.18 g/ml. These organelles can be isolated in a fraction sedimented at 10(5) g-min that contains 67% of the total pyruvate synthase (EC 1.2.7.1), 66% of the hydrogenase (EC 1.18.3.1) and 20% of the lactate dehydrogenase (EC 1.1.1.27). Thus in several respects this fraction is enzymically similar to those containing hydrogenosomes in some other parasitic anaerobic protozoa (the trichomonads). However, in contrast with the hydrogenosomes of trichomonads, the oxygen-tolerant enzyme malate dehydrogenase (decarboxylating) (EC 1.1.1.40) is not particulate, but occurs only in the cytosol. These results enable the proposal of a scheme for the pathway of product formation (acetate, lactate, CO2 and H2) from carbohydrates.
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PMID:Hydrogenosomes in the rumen protozoon Dasytricha ruminantium Schuberg. 680 78

The ratio of free ATP to free ADP in the mitochondrial matrix [( ATPf]/[ADPf]) has been measured in suspensions of isolated mitochondria under conditions of active phosphorylation of extramitochondrial ADP. These measurements utilized phosphoenolpyruvate carboxykinase which is present in the matrix of mitochondria from the livers of guinea pigs, chickens, and pigeons. Mitochondria isolated from these sources also contain nucleoside diphosphate kinase, malate dehydrogenase, and glutamate dehydrogenase or 3-OH-butyrate dehydrogenase. Together these enzymes catalyze the synthesis of phosphoenolpyruvate and CO2 from oxaloacetate with oxidative phosphorylation as an energy source. These reactions have been shown to be fully reversible in suspensions of mitochondria isolated from the above sources. With oxidative phosphorylation as the source of ATP, phosphoenolpyruvate was synthesized from malate and conversely addition of phosphoenolpyruvate, ADP, and CO2 led to synthesis of malate and ATP. The forward and reverse reactions were allowed to continue until the rate of change of metabolite concentrations was minimal and then the latter were measured. The intramitochondrial [Mg-ATPf]/[MgADPf] was calculated from the equilibrium constants for the reactions and the measured steady state concentrations of the metabolites in both the intra- and extramitochondrial spaces. The value of the intramitochondrial [MgATPf]/[MgADPf] was found to exceed the extramitochondrial value (adjusted to the same free Mg2+ concentration) by a factor (+/- S.E.) of 0.83 +/- 0.22 (n = 17) for the forward reaction and 1.81 +/- 0.54 (n = 11) for the reverse reaction. It is concluded that the adenine nucleotide translocase catalyzes electroneutral exchange of ATP for ADP and that this reaction does not contribute significantly to the energetics of mitochondrial oxidative phosphorylation.
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PMID:Evaluation of the relationship between the intra- and extramitochondrial [ATP]/[ADP] ratios using phosphoenolpyruvate carboxykinase. 688 88

'Malic enzyme' or malate dehydrogenase (NADP+), E.C.1.1.1.40, catalyses the reaction: L-malate + NADP in equilibrium pyruvate + CO2 + NADPH Baker & Manwell (1977), in a survey of a number of different enzymes reported that 'malic enzyme' was polymorphic in the erythrocytes and certain other tissues of sheep, and indicated that it would be a potentially useful new genetic marker for this species. This paper confirms the existence of the polymorphism in sheep erythrocytes and presents inheritance and breed data.
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PMID:'Malic enzyme' polymorphism in sheep erythrocytes. 731 44

The paper presents results of scientific activity of the Department of Metabolism Regulation. The main sections are: carbamates formation and their role in metabolism regulation; metabolic system of acid-base homeostasis in animals; polyamines metabolism in the extremal states; mechanisms of metabolic adaptation in mammals. Experimental data are presented which evidence for the fact that tissue proteins in vivo are subjected to nonenzymic carboxylation with formation of carbominic groups. In this case a charge variation in definite sites of protein molecule is observed, which specifies variation of the protein conformation and biological properties. Basic regularities of protein carbamate formation reactions are revealed with factors affecting their intensity. It is shown that the presence of carbonic acid in the medium increases the rate of reactions catalyzed with lactate dehydrogenase from the rabbit liver, glucose-6-phosphate dehydrogenase from yeast and trypsin. Under the same conditions the reaction velocity rate catalyzed with glucose-6-phosphate dehydrogenase from the rabbit liver and with ATP-citrate (pro-35)-liase is considerably decreased. Changes in the concentration of carbonic acid within the physiological limits are found to have no effect on lactate dehydrogenase from the cattle heart and chymotrypsin. The rate of the reaction catalyzed by NAD-dependent malate denydrogenase was studied as affected by carbon dioxide. It is shown that acceleration of the catalysis in these systems depends on the presence of both a bicarbonate anion and soluble carbon dioxide. IR spectra of NAD-dependent malate dehydrogenase in the deuterium oxide solutions were studied in the CO2-free solutions and solutions saturated with it.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Role of low molecular weight metabolites as natural regulators of metabolism]. 757 Oct 78

Chloroplastic NADP-dependent malate dehydrogenase (NADP-MDH) is a key enzyme in the photosynthetic CO2 fixation pathway of C4-plants. The presence of a histidine at its active site has been proposed, based on sequence alignment with nonchloroplastic NAD-dependent malate dehydrogenases. In order to investigate this hypothesis, the effect of diethylpyrocarbonate on the sorghum leaf enzyme has been tested. Diethylpyrocarbonate strongly inhibited NADP-MDH activity, its effect being dramatically decreased in the presence of substrates and reversed by hydroxylamine. When diethylpyrocarbonate-inactivated NADP-MDH was cleaved with trypsin, one peptide with increased absorbance at 240 nm was detected. Sequencing of this peptide and analysis by mass spectrometry demonstrated that histidine 229 was modified by diethylpyrocarbonate. This amino acid was changed to an alanine by site-directed mutagenesis, and the modified protein was produced in Escherichia coli. It was similar to the plant enzyme except that it was totally inactive. Taken together, these results indicate that His229 is an essential residue in the active site of sorghum NADP-MDH.
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PMID:Essential histidine at the active site of sorghum leaf NADP-dependent malate dehydrogenase. 796 39


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