Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Transferred nuclear Overhauser enhancement was used to examine the conformation of NAD+ and NADP+ bound to glucose-6-phosphate dehydrogenase and glutamate dehydrogenase and of NAD+ bound to lactate dehydrogenase. The results demonstrate that the conformation of the nicotinamide-ribose bond is anti for dehydrogenases with A stereospecificity and syn for dehydrogenases with B stereospecificity. In those dehydrogenases that bind both NAD+ and NADP+, significant differences occur in the conformations of the bound nicotinamide coenzymes.
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PMID:Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects. 687 Nov 63

Protease B [EC 3.4.22.9] was purified from baker's yeast by plasmolysis of yeast, acid activation, acid precipitation, and column chromatographies on QAE-Sephadex, SP-Sephadex, D-tryptophan methyl ester-Sepharose 4B and Sephadex G-100. The purified enzyme was inhibited by phenylmethylsulfonyl fluoride and sulfhydryl-blocking reagents. Chymostatin and antipain at extremely low concentrations (1 micro M) inhibited the protease B. The effects of the enzyme on various yeast enzymes were examined by measuring their inactivation. The enzyme inactivated 6-phosphogluconate dehydrogenase [EC 1.1.1.44] and uricase [EC 1.7.3.3], but not malate dehydrogenase [EC 1.1.1.37], alcohol dehydrogenase [EC 1.1.1.1], glutamate dehydrogenase [EC 1.4.1.3], glucose-6-phosphate dehydrogenase [EC 1.1.1.49] or hexokinase [EC 2.7.1.1].
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PMID:Purification and characterization of yeast protease B. 699 57

The malate dehydrogenase (MDH) electrophoretic mobilities of 128 strains of bacteroides belonging to 17 species, including three subspecies of Bacteroides melaninogenicus and two subspecies of Bacteroides ruminicola, were examined. Amongst the pigmented bacteroides, the migration of this enzyme correlated well with recognized taxa, and only one strain, VPI 9085 was clearly different. Other species such as B. oralis, B. buccalis, B. denticola, B. pentosaceus, B. bivius, B. disiens and B. ruminicola were delineated by the combined use of MDH and glutamate dehydrogenase. Forty-three strains belonging to the 'B. fragilis group' differed from the above species in possessing glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, and reference strains as well as fresh isolates were assigned to the correct species by the mobility pattern of these two enzymes. Other properties of MDH such as the pH optima for the oxidation of malate or the reduction of oxaloacetate were of limited taxonomic value. However, the alkaline stability of this enzyme at pH 9, 10 and 11 clearly differentiates the saccharolytic from the non-saccharolytic species of pigmented bacteroides with the latter showing highly stable enzymes with a half life greater than 50 min.
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PMID:Dehydrogenase patterns in the taxonomy of Bacteroides. 718 48

The activities of nine enzymes in liver specimens obtained from four children who had died from Reye's syndrome were compared to the corresponding activities of a control group of four children who had died from unrelated causes. At the 95% significance level, the alterations could be classified into three groups. Five activities [lactate dehydrogenase, alanine aminotransferase, glucose 6-phosphatase, cytochrome oxidase, and malate dehydrogenase (mitochondrial plus cytosolic)] showed no change. Three enzymes [glutamate dehydrogenase, isocitrate dehydrogenase (NADP), and monoamine oxidase] were decreased. One activity (glucose 6-phosphate dehydrogenase) was increased. The malate dehydrogenase isozymes were resolved by electrophoresis, and the two bands were stained and measured. The ratio of cytosolic:mitochondrial enzyme was significantly greater in Reye's syndrome than in the control group. These results lend further support to the view that in Reye's syndrome the impairment of hepatic function is largely confined to the mitochondria. The lowered activity of monoamine oxidase means that the abnormalities extend to the outer mitochondrial membrane. Imbalances of the cytosolic:mitochondrial enzyme activities were evaluated in needle biopsy specimens from four other children under conditions where neurologic abnormalities were less severe. Two patients had elevated ratios of both glutamate:lactate dehydrogenase and cytosolic:mitochondrial malate dehydrogenase activities, and a third had only an abnormal malate dehydrogenase ratio. In contrast to these Reye's syndrome patients, a fourth case admitted with a provisional diagnosis of Reye's syndrome showed no abnormality in either ratio in stage IV coma.
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PMID:Comparison of cytosolic and mitochondrial hepatic enzyme alterations in Reye's syndrome. 745 35

Reactions between ebselen and subcellular particles of rat liver were investigated by monitoring the activity of mitochondrial glutamate dehydrogenase and microsomal glucose 6-phosphate dehydrogenase. Rat small intestine lactate dehydrogenase was purified and was also used in the reaction between cytosolic protein and ebselen. Glutamate dehydrogenase in intact rat liver mitochondria was completely resistant to ebselen, but the enzyme was significantly inactivated in broken mitochondria mediated by Triton X-100, reflecting the fact that ebselen was not transported through the mitochondrial membrane into the matrix. Glucose 6-phosphate dehydrogenase in rat liver microsomes was inactivated by ebselen, accompanied by a slight decrease in the thiol groups of microsomal membrane protein. Purified cytosolic lactate dehydrogenase was inactivated concentration- and time-dependent by ebselen. The activity of rat small intestine lactate dehydrogenase abolished by ebselen was significantly restored by incubation with purified rat small intestine thioltransferase in the presence of reduced glutathione (GSH). The level of thiol groups in rat liver microsome membrane protein decreased by ebselen was partially restored by an incubation with purified rat liver thioltransferase in the presence of GSH. The results suggested that thioltransferase can cleave the Se-S conjugates between ebselen and cytosolic proteins or microsomal membrane proteins in the presence of GSH.
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PMID:Modulation of subcellular particles of the rat small intestine and liver by ebselen. 765 15

Saccharomyces cerevisiae mutants defective in the structural gene PGI1 lack phosphoglucose isomerase and hence cannot grow on glucose. Spontaneous mutants were isolated by selecting for the regained ability to grow on YEPD (yeast extract/peptone/glucose). Three complementation groups called spg29-31 (suppressor of pgi1 delta) were identified. The metabolism of [2-13C]glucose was studied by 13C NMR spectroscopy. This led to the conclusion that in a spg29 mutant suppression of the glycolytic defect was achieved by increased carbon flux through the hexose monophosphate pathway. The specific activities of enzymes of the hexose monophosphate pathway (except glucose-6-phosphate dehydrogenase) and NAD- and NADP-dependent glutamate dehydrogenase were increased in the bypass mutant.
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PMID:In Saccharomyces cerevisiae deletion of phosphoglucose isomerase can be suppressed by increased activities of enzymes of the hexose monophosphate pathway. 770 69

Galactosamine-induced hepatitis caused a marked increase in plasma lactate and pyruvate, but completely abolished the increase in ketone bodies in the rat exposed to an 8000 m simulated altitude. Plasma free fatty acid as the precursor of ketone bodies was higher in the galactosamine-treated rats during and after an exposure to 8000 m altitude. Treatment of the rat with galactosamine markedly reduced activities of citrate synthase, fumarase, glutamate dehydrogenase and fructose 1,6-bisphosphatase, but increased hexokinase and glucose 6-phosphate dehydrogenase in the liver. The effect of galactosamine-induced hepatitis on the energy metabolism can be explained by a reduction of mitochondrial oxidative enzymes and gluconeogenesis, and involves a shift of the aerobic metabolism to anaerobic glycolysis at high altitude.
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PMID:Effect of galactosamine-induced hepatitis on the aerobic and anaerobic metabolism of the rat exposed to high-altitude hypoxia. 774 7

In the course of a long-term L-DOPA administration (14 days) and 2 weeks after its cessation the activities of some protein enzymes (aminopeptidase, acid phosphatase), neuromediator (MAO, ACE) and oxidative (glutamate dehydrogenase, glucose-6-phosphate dehydrogenase) metabolism were studied by quantitative cytochemical methods in brain motor structures (sensorimotor cortex, caudate nucleus) and in structures not directly related to motor functions (hippocampus) of rats with high and low motor activity. After L-DOPA (madapar) cessation significant changes were revealed in the formation of motor system of the brain, primarily in the group of rats with low motor activity. It is suggested that a decrease in MAO activity after madapar cessation may be responsible for dyskinesia arising after cessation of L-DOPA preparations treatment.
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PMID:[Pathochemical changes in the motor structures of the brain under the influence of the administration of L-DOPA preparations and their withdrawal (experimental research)]. 790 Apr 46

Phosphoglucose isomerase pgi1-deletion mutants of Saccharomyces cerevisiae cannot grow on glucose as the sole carbon source and are even inhibited by glucose. These growth defects could be suppressed by an over-expression on a multi-copy plasmid of the structural gene GDH2 coding for the NAD-dependent glutamate dehydrogenase. GDH2 codes for a protein with 1092 amino acids which is located on chromosome XII and shows high sequence similarity to the Neurospora crassa NAD-glutamate dehydrogenase. Suppression of the pgi1 deletion by over-expression of GDH2 was abolished in strains with a deletion of the glucose-6-phosphate dehydrogenase gene ZWF1 or gene GDH1 coding for the NADPH-dependent glutamate dehydrogenase. Moreover, this suppression required functional mitochondria. It is proposed that the growth defect of pgi1 deletion mutants on glucose is due to a rapid depletion of NADP which is needed as a cofactor in the oxidative reactions of the pentose phosphate pathway. Over-expression of the NAD-dependent glutamate dehydrogenase leads to a very efficient conversion of glutamate with NADH generation to 2-oxoglutarate which can be converted back to glutamate by the NADPH-dependent glutamate dehydrogenase with the consumption of NADPH. Consequently, over-expression of the NAD-dependent glutamate dehydrogenase causes a substrate cycling between 2-oxoglutarate and glutamate which restores NADP from NADPH through the coupled conversion of NAD to NADH which can be oxidized in the mitochondria. Furthermore, the requirement for an increase in NADPH consumption for the suppression of the phosphoglucose isomerase defect could be met by addition of oxidizing agents which are known to reduce the level of NADPH.
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PMID:The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant. 790 Oct 8

To study the interactions between the citrate cycle and amino acid metabolism in zebrafish spinal motoneurons, we composed enzyme histochemical profiles from the activities of NAD-linked isocitrate dehydrogenase (NAD-ICDH), glutamate dehydrogenase (GDH), succinate dehydrogenase (SDH) and glucose 6-phosphate dehydrogenase (G6PDH). The enzyme assays were performed on serially-sectioned motoneuron somata. The motoneurons were identified by retrograde tracing from the trunk muscle and classified, on the basis of their location in the motor column, as those innervating the white, fast glycolytic fibers (WMNs) or those innervating the red and intermediate slow oxidative fibers (RIMNs). We found the following relationships between enzyme activities in WMNs: GDH correlates with G6PDH activity (r = 0.31; p = 0.02) and NAD-ICDH correlates with GDH activity (r = 0.37; p < 0.01); correlations between NAD-ICDH and SDH and between SDH and GDH are not significant. In RIMNs we found correlations between NAD-ICDH and SDH (r = 0.34; p = 0.03), between NAD-ICDH and GDH (r = 0.41; p < 0.01) and between GDH and SDH (r = 0.50; p < 0.01); the correlation between GDH and G6PDH is not significant. The differences in metabolic profiles between WMNs and RIMNs can be explained in the following way: in WMNs, alpha-ketoglutarate is drawn off from the citrate cycle and is used in amino acid metabolism whereas in RIMNs the removal of alpha-ketoglutarate from the cycle is balanced by formation of alpha-ketoglutarate. The data suggest that the functional role of the citrate cycle differs in the two motoneuron populations: in RIMNs energy generation predominates but in WMNs a role in biosyntheses seems most important.
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PMID:Metabolic profiles of white and red-intermediate spinal motoneurons in the zebrafish. 813 85


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