Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

An investigation into isoenzymic analysis using four different buffer/gel systems was carried out. Fourteen different isoenzyme systems were surveyed on each buffer/gel system. It is shown that comparable results are not obtained between different systems. Previous workers in Cepaea nemoralis have used different buffer/gel systems from one another. Alkaline phosphatase and acid phosphatase and certain lactate and malate dehydrogenases are shown to behave similarly in three different systems. It is tentatively suggested that these isoenzymes may be genetically identical. "Nothing dehydrogenase" activity is demonstrated in gels stained for other dehydrogenases. It is suggested that nothing dehydrogenase activity may be attributable to glutamate or malate dehydrogenase.
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PMID:Survey of isoenzymes in the snail Cepaea nemoralis using different buffer/gel systems in polyacrylamide disc gel electrophoresis: validity of comparisons and effect of "nothing dehydrogenase" activity. 73 83

Blood sampling by catheterisation of the abdominal aorta to test plasma haemoglobin and various plasma enzyme activities was compared with two other blood sampling techniques and their application to farm-kept minks under general anaesthesia, cardiac puncture and tail-tip amputation. The plasma haemoglobin values in plasma obtained from the abdominal aorta were significantly lower than those recorded from the two other blood sampling techniques, which applied to plasma enzyme activities, as well. Those findings were equal for males and females. The plasma enzyme activities tested were glutamate oxalo-acetate transaminase, glutamate-pyruvate transaminase, lactate dehydrogenase, alpha-hydroxybutyrate dehydrogenase, and malic dehydrogenase. Some plasma enzyme actvities were tested from a random sample of 164 animals for sex-dependence (88 males and 76 non-pregnant unserved females), with no consideration being given to blood sampling techniques. The standards or physiological indices derived from those tests are reported.
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PMID:[Morphology and biochemistry of various Mustelidae. 2. Effect of different blood collection technics on various plasma enzyme activities in Mink (Mustela vision Schreber, 1777)]. 74 38

The pathway of acetate assimilation in Methanosarcina barkeri was determined from analysis of the position of label in alanine, aspartate, and glutamate formed in cells grown in the presence of [14C]acetate and by measurement of enzyme activities in cell extracts. The specific radioactivity of glutamate from cells grown on [1-14C]- or [2-14C]acetate was approximately twice that of aspartate. The methyl and carboxyl carbons of acetate were incorporated into aspartate and glutamate to similar extents. Degradation studies revealed that acetate was not significantly incorporated into the C1 of alanine, C1 or C4 of aspartate, or C1 of glutamate. The C5 of glutamate, however, was partially derived from the carboxyl carbon of acetate. Cell extracts were found to contain the following enzyme activities, in nanomoles per minute per milligram of protein at 37 degrees C: F420-linked pyruvate synthase, 170; citrate synthase, 0.7; aconitase, 55; oxidized nicotinamide adenine dinucleotide phosphate-linked isocitrate dehydrogenase, 75; and oxidized nicotinamide adenine dinucleotide-linked malate dehydrogenase, 76. The results indicate that M. barkeri assimilates acetate into alanine and aspartate via pyruvate and oxaloacetate and into glutamate via citrate, isocitrate, and alpha-ketoglutarate. The data reveal differences in the metabolism of M. barkeri and Methanobacterium thermoautotrophicum and similarities in the assimilation of acetate between M. barkeri and other anaerobic bacteria, such as Clostridium kluyveri.
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PMID:Acetate assimilation pathway of Methanosarcina barkeri. 76 16

The regulation of alpha-ketogluterate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase, and malic enzyme has been studied in Bacillus subitilis. The levels of these enzymes increase rapidly during late exponential phase in a complex medium and are maximal 1 to 2 h after the onset of sporulation. Regulation of enzyme synthesis has been studied in the wild type and different citric acid cycle mutants by adding various metabolites to the growth medium. Alpha-ketoglutarate dehydrogenase is induced by glutamate or alpha-ketoglutarate; succinate dehydrogenase is repressed by malate; and fumarase and malic enzyme are induced by fumarate and malate, respectively. The addition of glucose leads to repression of the citric acid cycle enzymes whereas the level of malic enzyme is unaffected. Studies on the control of enzyme activities in vitro have shown that alpha-ketoglutarate dehydrogenase and succinate dehydrogenase are inhibited by oxalacetate. Enzyme activities are also influenced by the energy level, expressed as the energy charge of the adenylate pool. Isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, and malic enzyme are inhibited at high energy charge values, whereas malate dehydrogenase is inhibited at low energy charge. A survey of the regulation of the citric acid cycle in B.subtilis, based on the present work and previously reported results, is presented and discussed.
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PMID:Regulation of the dicarboxylic acid part of the citric acid cycle in Bacillus subtilis. 80 68

Rickettsia typhi cultivated in the yolk sac of chicken embryos or in L cells irradiated 7 days previously was separated from host cell components by two cycles of Renografin density gradient centrifugation. Preliminary steps involved differential centrifugation and centrifugation over a layer of 10% bovine plasma albumin of infected yolk sac suspensions, or trypsinization and passage through filters of wide porosity of infected L cell suspensions. Rickettsial preparations obtained by these methods appeared to be free from host cell components while retaining high levels of hemolytic activity, egg infectivity, and capacity to catabolize glutamate. Average yields were 3.3 mg of rickettsial protein per yolk sac or 0.44 mg per 16-oz (ca. 475-ml) L cell culture. Extracts from these two preparations displayed malate dehydrogenase activity of electrophoretic mobility identical to each other but quite different in migration patterns from the corresponding host cell enzymes. This method of separation of rickettsiae from host cell constituents appears to be particularly well suited for the study of rickettsial enzymatic activity.
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PMID:Separation of viable Rickettsia typhi from yolk sac and L cell host components by renografin density gradient centrifugation. 81 89

L-Malate repressed sporulation in the wild-type strain of Bacillus subtilis. When 75 mM L-malate was added to the growth medium at the time of inoculation, the appearance of heat-resistant spores was delayed 6 to 8 h. The synthesis of extracellular serine protease, alkaline phosphatase, glucose dehydrogenase, and dipicolinic acid was similarly delayed. Sporulation was not repressed when malate was added to the culture at t4 or later. A mutant was selected for ability to sporulate in the presence of malate. This strain could also sporulate in the presence of glucose. The malate-resistant mutant grew poorly with malate as sole carbon source, although it possessed an intact citric acid cycle, and it showed increased levels of malic enzyme. This indicates a defect in the metabolism of malate in the mutant. A mutant lacking malate dehydrogenase activity was also able to sporulate in the presence of malate. A model for the regulation of sporulation by malate is presented and discussed. Citric acid cycle intermediates other than malate did not affect sporulation. In contrast to previous results, sporulation of certain citric acid cycle mutants could be greatly increased or completely restored by the addition of intermediates after the enzymatic block. The results indicate that the failure of citric acid cycle mutants to sporulate can be adequately explained by lack of energy and lack of glutamate.
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PMID:Repression of sporulation in Bacillus subtilis by L-malate. 81 66

The catabolism of glutamate and fumarate was studied by radiorespirometry in selected Neisseria species. The tricarboxylic acid cycle is functioning in all species tested, in spite of the known absence of in vitro malate dehydrogenase activity in N. meningitidis, N. gonorrhoeae and N. cinerea. The results imply a pyridine nucleotide independent oxidation of malate. The oxidation of glutamate is less complete in the presence of phosphate. In N. meningitidis, N. perflava, N. flava, N. subflava and N. lactamica the catabolism of fumarate was slow and incomplete in the absence of glutamate.
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PMID:Radiorespirometric studies in genus Neisseria. 2. The catabolism of glutamate and fumarate. 81 81

Cell-free extracts of Rickettsia typhi were tested for activities of enzymes of the tricarboxylic acid cycle, of glutamate catabolism, and of glycolysis. The organisms were grown in the yolk sacs of chicken embryos, harvested shortly before the time of embryo death, purified by Renografin density gradient centrifugation, and ruptured in a French pressure cell. The following enzymatic activities were demonstrated: high levels of malate dehydrogenase (MDH), moderate levels of glutamate-oxaloacetate transaminase, glutamate, succinate, and isocitrate dehydrogenases, and citrate synthase, and low levels of glutamate-pyruvate transaminase. The specific activities of some of these enzymes were higher when the rickettsiae were harvested at a time of active proliferation, 3 to 4 days prior to embryo death. Rickettsial MDH was differentiated from host MDH by its migration pattern on polyacrylamide gel electrophoresis. The activities of MDH and two other dehydrogenases, demonstrable after the cells had been disrupted, were absent from purified, intact rickettsial preparations. No activity was detected for glucose-6-phosphate, 6-phosphogluconate, glyceraldehyde-3-phosphate, lactate dehydrogenases, phosphoglucose isomerase, fructoaldolase, or pyruvate kinase. Our results suggest that extracts of R. typhi that contain demonstrable enzymes involved in the catabolism of glutamate and tricarboxylic acid cycle intermediates, unlike Coxiella burnetti, lack detectable glycolytic activity.
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PMID:Enzymatic activities of cell-free extracts of Rickettsia typhi. 82 Jun 44

Tricarboyxlic acid cycle activity was examined in Neisseria gonorrhoeae CS-7. The catabolism of glucose in N. gonorrheae by a combination of the Entner-Doudoroff and pentose phosphate pathways resulted in the accumulation of acetate, which was not further catabolized until the glucose was depleted or growth became limiting. Radiorespirometric studies revealed that the label in the 1 position of acetate was converted to CO2 at twice the rate of the label in the 2 position, indicating the presence of a tricarboxylic acid cycle. Growth on glucose markedly reduced the levels of all tricarboxylic acid cycle enzymes except citrate synthase (EC 4.1.3.7). Extracts of glucose-grown cells contained detectable levels of all tricarboxylic acid cycle enzymes except aconitase (EC 4.2.1.3), isocitrate dehydrogenase (EC 1.1.1.42), and a pyridine nucleotide-dependent malate dehydrogenase (EC 1.1.1.37). Extracts of cells capable of oxidizing acetate lacked only the pyridine nucleotide-dependent malate dehydrogenase. In lieu of this enzyem, a particulate pyridine nucleotide-independent malate oxidase (EC 1.1.3.3) was present. This enzyme required flavin adenine dinucleotide for activity and appeared to be associated with the electron transport chain. Radiorespirometric studies utilizing labeled glutamate demonstrated that a portion of the tricarboxylic acid cycle functioned during glucose catabolism. In spite of the presence of all tricarboxylic acid cycle enzymes, N. gonorrhoeae CS-7 was unable to grow in medium supplemented with cycle intermediates.
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PMID:Physiology and metabolism of pathogenic neisseria: tricarboxylic acid cycle activity in Neisseria gonorrhoeae. 82 68

The incorporation of various 14C-labeled amino acids into CO2 and lipids by rat lung slices was examined. Alanine, valine, leucine, isoleucine, aspartate, and glutamate were oxidized by lung tissue, whereas glycine and phenylalanine were not oxidized. Carbon originating from alanine, leucine, and glutamate was incorporated into pulmonary fatty acids by a mechanism indicative of de novo synthesis. Experiments with specifically labeled [14C]aspartate and [14C]glutamate revealed that the complete citrate-malate cycle described by Patel et al. (25) is of minor importance in pulmonary lipogenesis due to the extremely low activity of NADP-malate dehydrogenase. Glucose and pyruvate were also actively incorporated into fatty acids, and it is suggested that citrate in pulmonary tissue, as in other tissues, plays an important role in the transport of acetyl units from the mitochondria to the cell cytosol during lipogenesis from various carbohydrate and amino acid substrates.
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PMID:Pulmonary fatty acid synthesis. II. Amino acids as fatty acid precursors in rat lung. 85 Nov 80


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