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)

Microbodies from rat liver and a variety of plant tissues were osmotically shocked and subsequently centrifuged at 40,000 g for 30 min to yield supernatant and pellet fractions. From rat liver microbodies, all of the uricase activity but little glycolate oxidase or catalase activity were recovered in the pellet, which probably contained the crystalline cores as many other reports had shown. All the measured enzymes in spinach leaf microbodies were solubilized. With microbodies from potato tuber, further sucrose gradient centrifugation of the pellet yielded a fraction at density 1.28 g/cm(3) which, presumably representing the crystalline cores, contained 7% of the total catalase activity but no uricase or glycolate oxidase activity. Using microbodies from castor bean endosperm (glyoxysomes), 50-60% of the malate dehydrogenase, fatty acyl CoA dehydrogenase, and crotonase and 90% of the malate synthetase and citrate synthetase were recovered in the pellet, which also contained 96% of the radioactivity when lecithin in the glyoxysomal membrane had been labeled by previous treatment of the tissue with [(14)C]choline. When the labeled pellet was centrifuged to equilibrium on a sucrose gradient, all the radioactivity, protein, and enzyme activities were recovered together at peak density 1.21-1.22 g/cm(3), whereas the original glyoxysomes appeared at density 1.24 g/cm(3). Electron microscopy showed that the fraction at 1.21-1.22 g/cm(3) was comprised of intact glyoxysomal membranes. All of the membrane-bound enzymes were stripped off with 0.15 M KCl, leaving the "ghosts" still intact as revealed by electron microscopy and sucrose gradient centrifugation. It is concluded that the crystalline cores of plant microbodies contain no uricase and are not particularly enriched with catalase. Some of the enzymes in glyoxysomes are associated with the membranes and this probably has functional significance.
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PMID:Localization of enzymes within microbodies. 472 5

Seed-specific expression in Arabidopsis thaliana of oleate hydroxylase enzymes from castor bean and Lesquerella fendleri resulted in the accumulation of hydroxy fatty acids in the seed oil. By using various Arabidopsis mutant lines it was shown that the endoplasmic reticulum (ER) n-3 desaturase (FAD3) and the FAE1 condensing enzyme are involved in the synthesis of polyunsaturated and very-long-chain hydroxy fatty acids, respectively. In Arabidopsis plants with an active ER Delta12-oleate desaturase the presence of hydroxy fatty acids corresponded to an increase in the levels of 18:1 and a decrease in 18:2 levels. Expression in yeast indicates that the castor hydroxylase also has a low level of desaturase activity.
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PMID:Production of hydroxy fatty acids in the seeds of Arabidopsis thaliana. 1117 Dec 67

Lesquerella fendleri seed oil contains up to 60% hydroxy fatty acids, nearly all of which is the 20-carbon hydroxy fatty acid lesquerolic acid (D-14-hydroxyeicos-cis-11-enoic acid). Previous work suggested that lesquerolic acid in L. fendleri was formed by the elongation of the 18-carbon hydroxy fatty acid, ricinoleic acid. To identify a gene encoding the enzyme involved in hydroxy fatty acid elongation, an L. fendleri genomic DNA library was screened using the coding region of the Arabidopsis Fatty Acid Elongation1 gene as a probe. A gene, LfKCS3, with a high sequence similarity to known very long-chain fatty acid condensing enzymes, was isolated. LfKCS3 has a 2,062-bp open reading frame interrupted by two introns, which encodes a polypeptide of 496 amino acids. LfKCS3 transcripts accumulated only in the embryos of L. fendleri and first appeared in the early stages of development. Fusion of the LfKCS3 promoter to the uidA reporter gene and expression in transgenic Arabidopsis resulted in a high level of beta-glucuronidase activity exclusively in developing embryos. Seeds of Arabidopsis plants transformed with LfKCS3 showed no change in their very long-chain fatty acid content. However, when these Arabidopsis plants were crossed with the transgenic plants expressing the castor oleate 12-hydroxylase, significant amounts of 20-carbon hydroxy fatty acids accumulated in the seed, indicating that the LfKCS3 condensing enzyme specifically catalyzes elongation of 18-carbon hydroxy fatty acids.
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PMID:A condensing enzyme from the seeds of Lesquerella fendleri that specifically elongates hydroxy fatty acids. 1174 8

Expression of a cDNA encoding the castor bean ( Ricinus communis L.) oleate Delta12-hydroxylase in the developing seeds of Arabidopsis thaliana (L.) Heynh. results in the synthesis of four novel hydroxy fatty acids. These have been previously identified as ricinoleic acid (12-hydroxy-octadec- cis-9-enoic acid: 18:1-OH), densipolic acid (12-hydroxy-octadec- cis-9,15-enoic acid: 18:2-OH), lesquerolic acid (14-hydroxy-eicos- cis-11-enoic acid: 20:1-OH) and auricolic acid (14-hydroxy-eicos- cis-11,17-enoic acid: 20:2-OH). Using mutant lines of Arabidopsis that lack the activity of the FAE1 condensing enzyme or FAD3 ER Delta-15-desaturase, we have shown that these enzymes are required for the synthesis of C20 hydroxy fatty acids and polyunsaturated hydroxy fatty acids, respectively. Analysis of the seed fatty acid composition of transformed plants demonstrated a dramatic increase in oleic acid (18:1) levels and a decrease in linoleic acid (18:2) content correlating to the levels of hydroxy fatty acid present in the seed. Plants in which FAD2 (ER Delta12-desaturase) activity was absent showed a decrease in 18:1 content and a slight increase in 18:2 levels corresponding to hydroxy fatty acid content. Expression of the castor hydroxylase protein in yeast indicates that this enzyme has a low level of fatty acid Delta12-desaturase activity. Lipase catalysed 1,3-specific lipolysis of triacylglycerol from transformed plants demonstrated that ricinoleic acid is not excluded from the sn-2 position of triacylglycerol, but is the only hydroxy fatty acid present at this position.
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PMID:Heterologous expression of a fatty acid hydroxylase gene in developing seeds of Arabidopsis thaliana. 1452 May 76

Electron micrographs are presented which establish the identity of the components of the 3 major bands observed after sucrose density centrifugation of the crude particulate fraction from the endosperm of germinating castor bean seedlings. These are: mitochondria (density 1.19 g/cc), proplastids (density 1.23 g/cc) and glyoxysomes (density 1.25 g/cc). Further evidence is provided on the enzymatic composition of the glyoxysomes. Essentially all of the particulate malate synthetase, isocitrate lyase, catalase, and glycolic oxidase is present in these organelles. The distribution of glyoxysomal enzymes on sucrose density gradients is contrasted with that of the strictly mitochondrial enzymes fumarase, NADH oxidase, and succinoxidase. Malate dehydrogenase and citrate synthetase are present in both organelles. The functional role of glyoxysomes and their relationship to cytosomes from other tissues is discussed.
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PMID:Characterization of glyoxysomes from castor bean endosperm. 1665 30

In cotyledons of sunflower seedlings glyoxysomal and peroxisomal enzymes exhibit different rates of development during germination. The total activity of isocitrate lyase, a glyoxysomal marker enzyme, rapidly increased during the first 3 days, and then decreased 89% by day 9. Exposure to light accelerated this decrease only slightly. The specific activity of glyoxysomal enzymes (malate synthetase, isocitrate lyase, citrate synthetase, and aconitase) in the microbody fraction from sucrose density gradients increased between days 2 and 4 about 2- to 3-fold, and thereafter it remained about constant in light or darkness.Total activity of the peroxisomal enzymes increased slowly in the dark during the first 4 days of germination and thereafter remained at a constant level of activity in the dark or increased 2-fold in 24 hours of light. The specific activties of glycolate oxidase, hydroxypyruvate reductase, and serine-glyoxylate aminotransferase in the isolated microbody fraction increased about 10-fold between days 2 and 4 in the dark and then remained constant or increased again 10-fold after an additional 48 hours in the light.The total activity of the common microbody marker, catalase, developed similarly to isocitrate lyase, but decreased only 72% by day 9. The specific activities of enzymes (catalase, malate dehydrogenase, and aspartate aminotransferase) common to both microbody systems were 10- to 1000-fold greater than those of other enzymes. It is proposed that malate and aspartate may be involved in hydrogen transport between microbodies and other cellular sites.Glutamate-glyoxylate aminotransferase was very active in microbodies from castor bean endosperm and sunflower cotyledons. The specific activity of this aminotransferase developed similarly to glyoxysomal enzymes in the dark but further increased in the light, as did peroxisomal enzymes.The microbody fraction of castor bean endosperm germinated in the dark for 5 days contained both glyoxysomal and peroxisomal enzymes of similar specific activity.Adjacent to the microbody fraction on sucrose gradients from sunflower cotyledons were etioplasts at slightly lower densities and protein bodies at similar and higher densities. Their presence in the microbody fractions resulted in artificially low specific activities.
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PMID:Development of Microbodies in Sunflower Cotyledons and Castor Bean Endosperm during Germination. 1665 39

Rabbit gamma-globulin obtained after the injection of solubilized proteins of castor bean (Ricinus communis L var. Hale) glyoxysomes contains antibodies against some of the glyoxysomal enzymes. The gamma-globulin was shown to inhibit by 50% and 80%, respectively, the in vitro activities of the castor bean glyoxysomal citrate synthetase and malate dehydrogenase. The conditions required for the inactivation are described.The glyoxysomal and mitochondrial citrate synthetase from castor bean endosperm show no significant difference in the above immunological test, in their apparent Michaelis constant values for acetyl coenzyme A and oxaloacetate, or in their sensitivity toward ATP inhibition. In the immunological test, glyoxysomal malate dehydrogenase from castor bean endosperm appeared to be related more closely to the leaf peroxisomal malate dehydrogenase from spinach (Spinacia oleracea L.) and to the glyoxysomal malate dehydrogenase from a variety of other fatty seedlings than to the castor bean mitochondrial or soluble malate dehydrogenase. Unlike the mitochondrial or soluble malate dehydrogenase, the castor bean glyoxysomal malate dehydrogenase is easily inactivated by gentle heat treatment, as was reported previously by other workers for the leaf peroxisomal malate dehydrogenase. Thus, the malate dehydrogenases from various plant microbodies share some common characteristics which distinguish them from other isozymes of malate dehydrogenase.
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PMID:Immunological and biochemical studies on isozymes of malate dehydrogenase and citrate synthetase in castor bean glyoxysomes. 1665 89

Homogenates of the endosperm of castor bean (Ricinus communis var. Hale) were prepared at intervals during germination and fractionated on sucrose gradients. Early in germination when glyoxysomes were being produced, a substantial proportion (50%) of the activities of malate synthetase and citrate synthetase was recovered in the membranes of the endoplasmic reticulum (mean density 1.12 grams per cubic centimeter). This proportion declined to less than 10% at 4 days when the glyoxysomes were fully developed.Gradient fractions challenged by antiglyoxysome-protein antiserum in double immunodiffusion assay revealed strong antigenic response in the endoplasmic reticulum membranes. The results support the view advanced earlier that glyoxysomes are derived directly from the endoplasmic reticulum.
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PMID:Role of the endoplasmic reticulum in glyoxysome formation in castor bean endosperm. 1665 92

Seedlings of castor bean (Ricinus communis cv. Hale) were exposed to a range of concentrations of gibberellin A(3) (GA(3)). Treatments for 20 hours with GA(3) concentrations of 0.5 muM or higher resulted in increased levels of NADH-cytochrome c reductase, phosphorylcholine glyceride transferase, and malate synthase in endoplasmic reticulum (ER) isolated from endosperm on linear sucrose gradients. GA(3) treatment also resulted in increased RNA associated with ER. Malate synthase and catalase in crude homogenates were enhanced by 1 to 100 muM GA(3) concentrations. Isocitrate lyase, citrate synthase, malate synthase, catalase, and glycolate oxidase in isolated glyoxysomes were enhanced by 60, 20, 18, 40, and 28%, respectively, over controls. Treatment with abscisic acid led to decreased levels of glyoxysomal enzymes and reduced glyoxysomal protein. The effect of GA(3) and abscisic acid on the specific activities of glyoxysomes of different densities suggests that GA(3) influences enzyme levels and glyoxysome assembly.
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PMID:Effect of gibberellin a(3) on the endoplasmic reticulum and on the formation of glyoxysomes in the endosperm of germinating castor bean. 1666 May 35

Seedlings of castor bean (Ricinus communis cv. Hale) were exposed to gibberellin A(3) (GA(3)) (100 micromolar) for periods up to 20 hours. Endosperm homogenates were fractionated on linear sucrose gradients and enzymes in mitochondria, glyoxysome, and cytosol fractions were assayed. Gibberellin treatment resulted in increases in the activities of enzymes in all three compartments. There were also enzymes in all three compartments which were not affected by exogenous applications of GA(3). The isozymes of l-asparate-alpha-ketoglutarate aminotransferase in both mitochondria and glyoxysomes were induced coordinately, whereas the isozymes of citrate synthase and malate dehydrogenase were not. All gluconeogenic enzymes in glyoxysomes are induced by GA(3). With the exception of the mitochondrial malate dehydrogenase isozyme, all enzymes of the tricarboxylic acid cycle believed to participate in glyconeogenesis were increased. The cytosolic enzymes malate dehydrogenase, phosphoenolpyruvate carboxykinase, and fructose bisphosphatase were induced, but the levels of pyruvate kinase and enolase were not affected by GA(3) treatment.
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PMID:Induction of glyconeogenic enzymes by gibberellin a(3) in endosperm of castor bean seedlings. 1666 12


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