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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)

Acetylpyridine NADP replaced NADP in promoting the Mn2+ ion-requiring mitochondrial "malic" enzyme of Hymenolepis diminuta. Disrupted mitochondria displayed low levels of an apparent oxaloacetate-forming malate dehydrogenase activity when NAD or acetylpyridine NAD served as the coenzyme. Significant malate-dependent reduction of acetylpyridine NAD by H. diminuta mitochondria required Mn2+ ion and NADP, thereby indicating the tandem operation of "malic" enzyme and NADPH:NAD transhydrogenase. Incubation of mitochondrial preparations with oxaloacetate resulted in a non-enzymatic decarboxylation reaction. Coupling of malate oxidation with electron transport via the "malic" enzyme and transhydrogenase was demonstrated by polarographic assessment of mitochondrial reduced pyridine nucleotide oxidase activity.
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PMID:Coupling of "malic" enzyme and NADPH:NAD transhydrogenase in the energetics of Hymenolepis diminuta (Cestoda). 673 50

Adipose tissue from fetuses decapitated at 45 d of gestation was removed and structurally and histochemically analyzed at 65, 85 and 110 d of gestation. Subcutaneous adipose tissue from decapitated and control fetuses at 65 d of gestation was histologically and histochemically similar. A reduced number of fat cell clusters in the outer layer of subcutaneous tissue and a poorly developed dermis was evident in decapitated fetuses at 85 d of gestation. Fat cell size was similar for control and decapitated fetuses at 65 d of gestation, whereas cells in 85 d-old decapitated fetuses were larger than cells in control fetuses. Adipocytes from control and 85 d-old decapitated fetuses were histochemically similar except for an elevated number of esterase positive cells in decapitated fetuses. At 110 d of gestation, adipocytes from decapitated fetuses had higher activities of the following enzymes than did control adipocytes: malate dehydrogenase (NADP dependent) glucose 6-phosphate dehydrogenase NADP dependent), isocitrate dehydrogenase (NADP dependent), alpha-glycerol phosphate dehydrogenase (NADP dependent), NADPH-tetrazoleum reductase and esterase. Levels of succinate dehydrogenase, glutamate dehydrogenase and NADH-tetrazoleum reductase were similar in cells from controls and decapitated fetuses. These data indicate that fetal decapitation probably exerts a positive influence on enzymes involved in lipid synthesis. However, fetal decapitation also exerts a negative influence on fat cell hyperplasia.
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PMID:Histochemical and cellular aspects of adipose tissue development in decapitated pig fetuses: an ontogeny study. 674 43

This study has investigated the feasibility of calculating the cytoplasmic free [NADP+]/[NADPH] ratio in rat brain. The time course of the change in the substrate ratios of the malate dehydrogenase (decarboxylating) [E.C. 1.1.1.40], NADP+-isocitrate dehydrogenase (decarboxylating) [E.C. 1.1.1.42] and 6-phosphogluconate dehydrogenase (decarboxylating) [E.C. 1.1.1.44] reactions was followed for up to 10 min after a single, unmodified electroconvulsive seizure. From the results it has been concluded that during periods of low flux, the direction and magnitude of the change in the cytoplasmic free [NADP+]/[NADPH] ratio can, in fact, be reasonably determined even though there is some uncertainty in the absolute value of the ratio itself. It is recommended that reliance not be placed on a single enzyme system but that one or both of the other systems also be observed under a given experimental condition to increase confidence in the determination. The results also demonstrate that seizure and anoxia have a far lesser effect on the cytoplasmic free [NADP+]/[NADPH] ratio than on the free [NAD+]/[NADH] ratio in the same compartment. These results suggest that the pathways using the nicotinamide-adenine dinucleotide phosphate system are relatively protected from the rapid fluctuations that seizure and anoxia can produce.
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PMID:The calculation of the cytoplasmic free [NADP+]/[NADPH] ratio in brain: effect of electroconvulsive seizure. 679 9

Adult H. microstoma mitochondria catalyzed a malate dehydrogenase, decarboxylating ("malic" enzyme) activity. This "malic" enzyme was found as a soluble component of the mitochondrion, was specific for NADP, and required a divalent cation with Mn++ ion yielding the greatest activity. The H. microstoma "malic" enzyme could fulfill the need for generating intramitochondrial reducing equivalents required for electron transport. The H. microstoma mitochondria also exhibited an NADPH:NAD transhydrogenation reaction. The electron transport system of this cestode was apparently specific for NADH both in terms of the rotenone-sensitive oxidase and fumarate reductase systems. Electron transport-associated NADPH oxidation was increased markedly with the addition of NAD to the system. Coupling of NADPH utilization to fumarate reduction, in the presence of NAD, was apparent under conditions of reduced oxygen tension. This was consistent with the presence of the NADPH:NAD transhydrogenase which catalyzed a transfer of reducing equivalents from NADPH to NAD, producing NADH for electron transport function. The data presented suggest that H. microstoma mitochondria can engage in an anaerobic, electron transport-associated production of succinate, and presumably concomitant phosphorylation. Malate may serve as the mitochondrial substrate supplying reducing equivalents for electron transport via the activity of the "malic" enzyme coupled to the NADPH:NAD transhydrogenase. In addition to the NADPH:NAD transhydrogenase activity, H. microstoma mitochondria catalyzed an NADH:NAD transhydrogenation.
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PMID:Mitochondrial malate dehydrogenase, decarboxylating ("malic" enzyme) and transhydrogenase activities of adult Hymenolepis microstoma (Cestoda). 707 55

'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

NADP-linked malic enzyme (malate dehydrogenase (oxaloacetate-decarboxylating) NADP+, EC 1.1.1.40) has been partially purified from adult Onchocerca volvulus and Dirofilaria immitis. Suramin was found to inhibit the activity of malic enzyme from both filarial worms. The inhibition constants for suramin were calculated to be 0.011 microM and 0.015 microM for the enzymes from O. volvulus and D. immitis, respectively. In the case of NADP-linked malic enzyme from Trypanosoma brucei and chicken liver the inhibition by suramin was less pronounced. The inhibition constants were found to be 0.8 microM and 2.5 microM for the protozoan and vertebrate enzymes, respectively. The type of inhibition was competitive with respect to malate. The Michaelis constants for malate and pyruvate were determined to be 0.9 and 4.5 mM for O. volvulus and 0.85 and 5.0 mM for D. immitis, respectively. The low Km values for malate compared to those for pyruvate and the about 15-fold greater turnover in the direction of decarboxylation compared to carboxylation indicated that malic enzyme from both filarial sources might be involved in an alternative pathway leading from phosphoenolpyruvate via oxaleacetate, malate and pyruvate to lactate. It is suggested, that the inhibition of malic enzyme activity from O. volvulus by suramin might interfere with the generation of NADPH for biosynthetic reactions.
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PMID:Inhibition of NADP-linked malic enzyme from Onchocerca volvulus and Dirofilaria immitis by suramin. 732 87

The paper deals with the intensity of NADPH formation in the isocytrate dehydrogenase reaction and NADPH oxidation in the lactate and malate dehydrogenase reactions. It is shown that bicarbonate, phosphate, acetate, chloride and triethanolamine buffer in concentrations of 1 . 10(-1) = 4 . 10(-1) M can inhibit these processes intensity. The inhibitory effect of the mentioned anions on the NADH-isocytrate dehydrogenase activity is considerably decreased when adding MnCl2 or MgCl2 to the incubation medium. Sucrose is established to inhibit the formation of NADPH in the isocitrate dehydrogenase reaction at 2 . 10(-1) M and higher.
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PMID:[Effect of bicarbonate and certain anions on NADP redox]. 738 74

Malic enzyme of the phototropic bacterium Chromatium vinosum strain D that lacks malate dehydrogenase was partially purified yielding a specific activity of 55 units/mg protein. The constitutive enzyme with a molecular weight of 110,000 and a pH optimum of 8.0 was absolutely dependent on the presence of a monovalent cation (NH4+, K+, Cs+, or Rb+) as well as a divalent cation (Mn2+, or Mg2+). The enzyme was inhibited by oxaloacetate, glyoxyate, and NADPH. The K0.5 value for L-malate and the inhibition constants for oxaloacetate and glyoxylate are dependent on the concentration of the monovalent cation, whereas the Km value for NADP (18 microM) and the KI value for NADPH (42 microM) are independent. Throughout all kinetic measurements hyperbolic saturation curves and linear double reciprocal plots were obtained.
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PMID:Malic enzyme of chromatium vinosum. 742 83

In this communication, the results of applying various histochemical techniques for the localization of oxidoreductases, transferases, hydrolases and isomerases in the human heart are presented. The Purkinje fibres of the atrioventricular conducting system of the human heart differ from the myocardium proper in containing a slightly higher activity of most of the glycolytic and gluconeogenetic enzymes investigated. The relatively higher activity of 6-phosphofructokinase, the key enzyme in anaerobic carbohydrate metabolism, is especially noteworthy. On the other hand, the activities of some of the enzymes that play a part in the aerobic energy metabolism is slightly less than those in the myocardium fibres. As for the activity of the NADPH regenerating enzymes, the activity of 6-phosphogluconate dehydrogenase and malate dehydrogenase (oxaloacetate-decarboxylating) is somewhat higher, and the activity of glucose-6-phosphate dehydrogenase similar, in the Purkinje fibres compared to that in the myocardial fibres. The activity of myosin ATPase is similar for both types of fibre. Likewise, the fibres of the conducting system and of the myocardium show a similar activity of acid phosphatase, beta-glucuronidase, non-specific naphthylesterase and peroxidase. The neurogenic function of the conducting system of the human heart was demonstrated by the high activity of acetylcholinesterase in the Purkinje fibres and in the atrioventricular node. All these histochemical findings in Purkinje fibres are similar at widely differing levels of the conducting system.
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PMID:Enzyme histochemical studies on the conducting system of the human heart. 744 Feb 54

To determine the potential site(s) of fatty acid synthesis and source(s) of reducing equivalents, the activities of the cytoplasmic NADPH producing enzymes--isocitrate dehydrogenase (IDH), malic enzyme (ME), glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH), and of aconitase, ATP-citrate lyase (CCE) and malate dehydrogenase (MDH) were measured in homogenates of liver, intestine, visceral fat, red muscle and white muscle of eels (Anguilla rostrata) fed beef liver or worms, or fasted for 2 to 6 months. There were no differences in enzyme activities between eels fed beef liver or fasted for 2 months. Eels fed worms had significantly greater G6PDH activity than fasted eels. Liver size and hepatosomatic index decreased in fasted eels, but lipid content per gram of liver or muscle increased. Based on the total activities of the NADPH producing enzymes, the liver appeared to be the primary organ for lipogenesis, although the intestine contained active lipogenic enzymes as well. In the liver, IDH had the lowest Km (NADP) and highest activity of the NADP-dehydrogenases. In the liver cytoplasm, the low activities of CCE and ME and the presence of an active aconitase, with a 20-fold greater affinity than CCE for citrate, suggest tha citrate cleavage is unimportant and that IDH is a major source of reducing equivalents. The source of carbon for fatty acid synthesis is discussed in relation to these conclusions.
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PMID:Influence of fasting and diet on lipogenic enzymes in the american eel, Anguilla rostrata LeSueur. 746 73


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