Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Das, S. K. (Calcutta University, Calcutta, India), and G. C. Chatterjee. Pyrithiamine adaptation of Staphylococcus aureus. II. Tricarboxylic acid cycle and related enzymes. J. Bacteriol. 86:1157-1164. 1963.-Evidence for the stimulated operation of the tricarboxylic acid cycle in Staphylococcus aureus after pyrithiamine adaptation is presented. In the cell-free extracts, isocitric, glutamic, malic, and succinic dehydrogenases and catalase were found to be stimulated after the adaptation of S. aureus to pyrithiamine. Besides such stimulation, the appearance of isocitratase and malate synthetase in the adapted strain supports the appearance of the glyoxalate bypass after such adaptation. There is little change in the activities of reduced nicotinamide adenine dinucleotide (NADH) and reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidases and diaphorase. Lactic dehydrogenase, NADH-cytochrome c reductase, and NADPH-cytochrome c reductase could not be demonstrated either in the normal or in the pyrithiamine-adapted S. aureus. These observations support the postulation that there is a stimulation in the tricarboxylic acid cycle and can account for the very marked stimulation in the utilization of acetate by the organism after adaptation.
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PMID:PYRITHIAMINE ADAPTATION OF STAPHYLOCOCCUS AUREUS. II. TRICARBOXYLIC ACID CYCLE AND RELATED ENZYMES. 1408 84

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

The endosperm of 3-day germinated seedlings of Ricinus communis was homogenized in the presence or absence of Mg(2+). When the Mg(2+) -containing homogenate was fractionated on linear, 20 to 40% sucrose gradients, the endoplasmic reticulum (ER) reached equilibrium at a density of 1.146 grams per cubic centimeter. Absence of Mg(2+) in the grinding medium resulted in displacement of the ER in the gradient from a density of 1.146 to 1.138 grams per cubic centimeter. At either density, the activities of both malate and citrate synthase were found to overlap the activity of NADH-cytochrome c reductase (an ER marker) in the gradient. Furthermore, this overlap of activities was observed whether the gradients were centrifuged for 3 or 19 hours. An analysis of sedimentation characteristics of the solubilized enzymes revealed that they exist, predominantly, as a 5.2S (s(20,w) x 10(-13)) form (malate synthase) and a 6.8S form (citrate synthase) in the glyoxysomes and cytosol. When the two enzymes were released from the ER, they appeared as aggregate forms of 70S and 55S, respectively. These results support the conclusion that the synthases are associated with the ER.
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PMID:Aggregated Forms of Malate and Citrate Synthase are Localized in Endoplasmic Reticulum of Endosperm of Germinating Castor Bean. 1666 90

In homogenates of resting rapeseeds no lipase activity (glycerolester hydrolase, EC 3.1.1.3) could be detected using a titrimetric assay procedure. Following a 30-h lag-phase after imbibition, lipase activity increased sharply, reaching its maximum at day 4 after sowing. Simultaneously triglyceride content of the cotyledons decreased sharply. At any time during the 11-day period of seedling growth examined, only an alkaline lipase activity with a pH optimum around 9 was present. White light had essentially no effect on the development of lipase activity. However, the disappearance of lipase activity from the cotyledons after fat utilization was found to depend on nitrogen nutrition of the seedlings. The activities of the glyoxysomal enzymes catalase and malate synthetase showed the usual rise and fall patterns with peak activities at day 4 after sowing, independently of the mineral nutrition of the seedlings.About 90% of the lipase activity was associated with a microsomal membrane fraction. Resolution of this fraction by sucrose density gradient centrifugation (62,000 g for 14 h) yielded three distinct membrane fractions. Maximum activities of membrane marker enzymes were recovered from the gradients at following densities: The major portion of microsomal protein and lipase activity at 1.085 kg/l; microsomal malate synthetase and phosphorylcholineglyceride transferase at 1.116 kg/l; NADH-cytochrome c reductase and phosphorylcholinecytidyl transferase at 1.133 kg/l. Evidently in rapeseed cotyledons lipase activity is associated only with a discrete microsomal membrane fraction which sediments differently from membrane fractions of the endoplasmic reticulum.
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PMID:Development and intracellular localization of lipase activity in rapessed (Brassica napus L.) cotyledons. 2441 67