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:2.3.3.1 (citrate synthase)
4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The growth response of Listeria monocytogenes strains A4413 and 9037-7 to carbohydrates was determined in a defined medium. Neither pyruvate, acetate, citrate, isocitrate, alpha-ketoglutarate, succinate, fumarate, nor malate supported growth. Furthermore, inclusion of any of these carbohydrates in the growth medium with glucose did not increase the growth of Listeria over that observed on glucose alone. Resting cell suspensions of strain A4413 oxidized pyruvate but not acetate, citrate, isocitrate, alpha-ketoglutarate, succinate, fumarate, or malate. Cell-free extracts of strain A4413 contained active citrate synthase, aconitate hydratase, isocitrate dehydrogenase, malate dehydrogenase, fumarate hydratase, fumarate reductase, pyruvate dehydrogenase system, and oxidases for reduced nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide phosphate. The alpha-ketoglutarate oxidation system, succinate dehydrogenase, isocitrate lyase, and malate synthase were not detected. Cytochromes were not detected. The data suggest that strain A4413, under these conditions, utilizes a split noncyclic citrate pathway which has an oxidative portion (citrate synthase, aconitate hydratase, and isocitrate dehydrogenase) and a reductive portion (malate dehydrogenase, fumarate hydratase, and fumarate reductase). This pathway is probably important in biosynthesis but not for a net gain in energy.
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PMID:Citrate cycle and related metabolism of Listeria monocytogenes. 499 14

The levels of Krebs cycle, glyoxylate cycle, and certain other enzymes were measured in a wild-type strain and in seven groups of acetate-nonutilizing (acu) mutants of Neurospora crassa, both after growth on a medium containing sucrose and after a subsequent 6-hr incubation in a similar medium, containing acetate as the sole source of carbon. In the wild strain, incubation in acetate medium caused a rise in the levels of isocitrate lyase, malate synthase, phosphoenolpyruvate carboxykinase, acetyl-coenzyme A synthetase, nicotinamide adenine dinucleotide phosphate-linked isocitrate dehydrogenase, citrate synthase, and fumarate hydratase. Isocitrate lyase activity was absent in acu-3 mutants; acu-5 mutants lacked acetyl-coenzyme A synthetase activity; and no oxoglutarate dehydrogenase activity (or only low levels) could be detected in acu-2 and acu-7 mutants. In acu-6 mutants, phosphoenolpyruvate carboxykinase activity was either very low or absent. No specific biochemical deficiencies could be attributed to the acu-1 and acu-4 mutations. The role of several of these enzymes during growth on acetate is discussed.
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PMID:Acetate-nonutilizing mutants of Neurospora rassa. II. Biochemical deficiencies and the roles of certain enzymes. 564 48

During exponential growth, ordinary colorless (OC) plants of Blastocladiella emersonii consumed little glucose and produced no lactic acid. Similarly, resistant sporangial (RS) plants did not utilize glucose or produce lactic acid during the first 24 hr of exponential growth. During the next 24 hr of RS development, glucose was consumed with the concomitant production of lactic acid which was then reutilized. Lactic acid gradually accumulated again at maturity. Enzyme studies on cell-free extracts indicated the presence of all tricarboxylic cycle enzymes except alpha-ketoglutarate dehydrogenase at all stages of development of both RS and OC plants. Included among the enzymes detected were an adenosine monophosphate-stimulated, nicotinamide adenine dinucleotide-isocitric dehydrogenase, and citrate-condensing enzyme. When measured on a per plant basis, tricarboxylic cycle enzyme levels increased during the exponential growth of both kinds of plants. Only after the bicarbonate ceased to have effect on RS plant morphogenesis was there a decrease in the levels of the tricarboxylic cycle enzymes when measured on a per plant basis. Specific activity measurements indicated some differences in the differential rates of synthesis among the enzymes studied previous to 36 hr. Preliminary studies utilizing short periods of (14)C-bicarbonate fixation in young RS plants indicated that during the first 4 min most of the label was located in aspartic acid. These results are discussed in terms of previous results and particularly Cantino's hypothesis concerning the relationship between bicarbonate induction and tricarboxylic-cycle enzymes in the morphogenesis of B. emersonii.
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PMID:Tricarboxylic acid cycle enzymes and morphogenesis in Blastocladiella emersonii. 580 5

Burton, Sheril D. (Institute of Marine Science, University of Alaska, College), Richard Y. Morita, and Wayne Miller. Utilization of acetate by Beggiatoa. J. Bacteriol. 91:1192-1200. 1966.-A proposed system which would permit acetate incorporation into four-carbon compounds without the presence of key enzymes of the citric acid cycle or glyoxylate cycle is described. In this system, acetyl-coenzyme A (CoA) is condensed with glyoxylate to form malate, which, in turn, is converted to oxaloacetate. Oxaloacetate then reacts with glutamate to produce alpha-ketoglutarate, which is subsequently converted to isocitrate. Cleavage of isocitrate produces glyoxylate and succinate. Thus, the proposed system is similar to the glyoxylate bypass in that malate is produced from glyoxylate and acetyl-CoA, but differs from both the citric acid cycle and the glyoxylate bypass, since citrate and fumarate are not involved. Fumarase, aconitase, catalase, citritase, pyruvate kinase, enolase, phosphoenolpyruvate carboxylase, lactic dehydrogenase, alpha-ketoglutarate dehydrogenase, and condensing enzyme were not detectable in crude extracts of Beggiatoa. Succinate was oxidized by a soluble enzyme not associated with an electron-transport particle. Isocitrate was identified as the sole compound labeled when C(14)O(2) was added to a reduced nicotinamide adenine dinucleotide, CO(2) generating system (crystalline glucose-6-phosphate dehydrogenase and glucose-6-phosphate) in the presence of alpha-ketoglutarate.
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PMID:Utilization of acetate by Beggiatoa. 592 51

Muscle biopsy specimens from the middle gluteal muscle were studied in 16 red blood cell hypervolaemic (Group HV) and 19 normovolaemic (Group NV) Standardbred racehorses. All horses were stallions, 4-8 years old and having similar mean racing performance values, as described by an individual selection index value. All horses raced regularly but those in Group HV did not perform as expected and were therefore referred to the clinics for exercise tolerance testing. Muscle biopsy specimens were analysed for fibre type distribution (Type I, IIA and IIB), fibre area and relative fibre area. In addition, oxidative capacity of the fibres was evaluated by staining for nicotinamide adenine dinucleotide (NADH) tetrazolium reductase, and the activities of citrate synthase, 3-OH-acyl CoA dehydrogenase and lactate dehydrogenase were analysed in whole-muscle samples. With the exception of a higher percentage of Type IIB fibres in Group HV having a high oxidative capacity as evaluated by the NADH stain, no significant difference were found in fibre composition, fibre area or enzyme activity between the Groups HV and NV.
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PMID:Skeletal muscle characteristics in red blood cell normovolaemic and hypervolaemic standardbred racehorses. 857

A mass spectrometer coupling electrospray ionization with time-of-flight mass spectrometry (ESI-TOFMS) has been used to investigate the oligomeric species of Escherichia coli citrate synthase, and to determine the effect of nicotinamide adenine dinucleotide (NADH), an allosteric inhibitor of this enzyme, on the equilibrium between the oligomeric forms. An equilibrium mixture of dimers (M = 95,770 Da) and hexamers (M = 287,310 Da) was found under the conditions used (KA = 6.9 x 10(10) M-2), and NADH was observed to bind selectively to the hexamer (KD = 1.1 microM), shifting the equilibrium to the latter form. The power of ESI-TOFMS to measure ions of very large mass-to-charge ratio (up to m/z approximately 10,000 in this case) is shown to be a valuable tool for obtaining accurate information about compositions of noncovalent complexes and equilibrium constants. The measured constants agree with those determined by conventional means.
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PMID:Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry. 955 14

We report automated methods for assaying the activities of the mitochondrial respiratory chain enzyme cytochrome c oxidase (COX), the matrix enzyme citrate synthase (CS), and the cytoplasmic enzyme lactate dehydrogenase (LDH) on a random access analyzer, the Roche Mira S. COX activity was assayed by measuring the initial rate of oxidation of reduced cytochrome c. The CS assay was based on the reaction of this enzyme with oxaloacetate and acetyl-CoA to produce CoASH, which further reacts with dithionitrobenzoic acid producing a free thionitrobenzoate ion. LDH activity was assayed by measuring the reduction of nicotinamide adenine dinucleotide during the oxidation of lactate to pyruvate. Precision of the COX assay was 2. 3%, CS assay 0.7%, and LDH 5.6%. These automated methods were faster by as much as 80%, cheaper by 50%, and used less than half the sample material needed for traditional manual methods. While these assays are often performed by specialized laboratories using dedicated staff, the automated methods presented here are easily performed by staff trained in the regular diagnostic laboratory.
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PMID:Automated analysis of mitochondrial enzymes in cultured skin fibroblasts. 961 94

Bacteroids formed by Mesorhizobium ciceri CC 1192 in symbiosis with chickpea plants (Cicer arietinum L.) contained a single form of citrate synthase [citrate oxaloacetate-lyase (CoA-acetylating) enzyme; EC 4.1.3.7], which had the same electrophoretic mobility as the enzyme from the free-living cells. The citrate synthase from CC 1192 bacteroids had a native molecular mass of 228 +/- 32 kDa and was activated by KCl, which also enhanced stability. Double reciprocal plots of initial velocity against acetyl-CoA concentration were linear, whereas the corresponding plots with oxaloacetate were nonlinear. The Km value for acetyl-CoA was 174 microM in the absence of added KCl, and 88 microM when the concentration of KCl in reaction mixtures was 100 mM. The concentrations of oxaloacetate for 50% of maximal activity were 27 microM without added KCl and 14 microM in the presence of 100 mM KCl. Activity of citrate synthase was inhibited 50% by 80 microM NADH and more than 90% by 200 microM NADH. Inhibition by NADH was linear competitive with respect to acetyl-CoA (Kis = 23.1 +/- 3 microM) and linear noncompetitive with respect to oxaloacetate (Kis = 56 +/- 3.8 microM and Kii = 115 +/- 15.4 microM). NADH inhibition was relieved by NAD+ and by micromolar concentrations of 5'-AMP. In the presence of 50 or 100 mM KCl, inhibition by NADH was apparent only when the proportion of NADH in the nicotinamide adenine dinucleotide pool was greater than 0.6. In the microaerobic environment of bacteroids, NADH may be at concentrations that are inhibitory for citrate synthase. However, this inhibition is likely to be relieved by NAD+ and 5'-AMP, allowing carbon to enter the tricarboxylic acid cycle.
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PMID:Biochemical controls of citrate synthase in chickpea bacteroids. 1064 3

In 1992-1994, a disorder known as the epidemic neuropathy afflicted more than 50,000 Cubans. Three different forms of the illness were identified: epidemic optic neuropathy, peripheral neuropathy and mixed optic and peripheral neuropathy. The causes are still unknown. Skeletal muscle biopsy samples were analyzed by standard histological techniques and by biochemical assays. Elevated activities of citrate synthase, a non-respiratory-chain mitochondrial matrix enzyme, suggested possible mitochondrial proliferation in 7 of the 8 patients. Nicotinamide adenine dinucleotide phosphate (NADP(+)) levels were higher in the patients than in the controls (p = 0.04). Levels of nicotinamide adenine dinucleotide (NAD) and the reduced compounds NADH and NADPH were comparable in patients and controls. Elevations of succinate dehydrogenase and citrate synthase activities and high NADP(+) levels suggest that alterations of mitochondrial functions may be associated with this disorder.
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PMID:Biochemical studies of patients with Cuban epidemic neuropathy. 1172 Nov 82

Smith, Paul F. (University of South Dakota, Vermillion), and C. V. Henrikson. Comparative biosynthesis of mevalonic acid by Mycoplasma. J. Bacteriol. 89:146-153. 1965.-Three representative Mycoplasma, M. laidlawii strain B, M. gallisepticum strain J, and M. hominis strain 07, were examined for the presence or absence of enzymes associated with the biosynthetic pathway to mevalonic acid. M. laidlawii served as a control, because it synthesizes carotenoids from acetate. M. laidlawii was shown to contain a specific acetokinase and phosphotransacetylase for the synthesis of acetyl coenzyme A, and a beta-ketothiolase and coenzyme A transferase for the synthesis of acetoacetyl coenzyme A. M. gallisepticum contained a specific acetokinase, phosphotransacetylase, and possibly an aceto coenzyme A kinase forming acetyl coenzyme A; it also contained a beta-ketothiolase, a coenzyme A transferase, and a coenzyme A transphorase forming acetoacetyl coenzyme A directly or indirectly. The beta-ketothiolase of M. gallisepticum was not affected by iodoacetamide, in contrast to the other two strains. M. laidlawii exhibited beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme, and M. hominis did not. This activity of M. gallisepticum was masked by thiolase activity. M. laidlawii and M. gallisepticum contained a nicotinamide adenine dinucleotide phosphate-linked beta-hydroxy-beta-methylglutaryl coenzyme A reductase, and M. hominis did not. C(14)-labeled acetate was incorporated into mevalonic acid only by M. laidlawii and M. gallisepticum. The lack of beta-hydroxy-beta-methylglutaryl coenzyme A condensing enzyme and reductase activities in M. hominis explains its growth requirement for sterol. The enzymatic block in M. gallisepticum must occur after mevalonic acid in the biosynthetic pathway to terpenoids.
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PMID:COMPARATIVE BIOSYNTHESIS OF MEVALONIC ACID BY MYCOPLASMA. 1425 55


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