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

1. The main forage for camels in northern Djibouti (mangrove with Avicennia marina) is very poor in nitrogen and energy. In a trial, 32 young camels (less than 2 years old) were used in four groups of eight each. 2. All the camels received mangrove as basal diet ad lib. 3. After 1 month, the camels received mineral supplementation in copper and zinc (groups 1 and 3) or/and a concentrate rich in protein and energy (groups 2 and 3) or continued with the basal diet (controls). 4. Any supplementation was stopped after 2 months for 1 month. 5. Growth performance was 550 g/day (concentrate-supplemented camels) and 570 g/day (concentrate+mineral-supplemented camels). 6. The growth was negative for the two others groups (-260 g/day). 7. Food intake of mangrove was slightly more important with mineral supplementation only and with mineral+concentrate supplementation. 8. The changes in metabolic profiles have shown an important catabolism in non-supplemented animals, an increase of urea and free fatty acid concentrations in plasma and a decrease of glucose concentrations. 9. Three camels died in the control group with symptoms of starvation and signs of liver damage (increase of liver enzymes glutamate dehydrogenase and gamma-glutamyl transferase).
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PMID:The influence of high dietary protein, energy and mineral intake on deficient young camel (Camelus dromedarius)--I. Changes in metabolic profiles and growth performance. 135 89

In a flock of sheep to which food with excess copper (= Cu) had been fed for some months 39 animals died of chronic copper toxicosis. In 5 sheep of this flock the plasma concentrations of the enzymes glutamate dehydrogenase (GLDH), sorbitol dehydrogenase (SDH), aspartate-amino-transferase (ASAT) and copper were measured several times over a period of 100 days. At day 23, 58 and 97 needle biopsies of the liver were taken. The biopsies were used for histological examination and Cu-analysis. After 100 days the sheep were slaughtered and chronic copper poisoning was diagnosed by raised Cu concentration and typical histological alterations in the liver. The activities of GLDH and SDH in the plasma of the 5 sheep were consistently above normal, ASAT activity and the plasma Cu level were raised only occasionally. The results of Cu determination in biopsy samples were of little predictive value compared with post mortem Cu analysis of the liver.
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PMID:[The diagnostic significance of different blood parameters and liver biopsy in chronic copper poisoning of sheep]. 206 9

Treatments with copper sulphate (CuSO4), paraquat (PQ) and methidathion (MD) caused tissue damage and stress effects in carp, indicated by the increased lactate dehydrogenase (LDH), glutamic oxaloacetic transaminase (GOT), and glutamate dehydrogenase (GIDH) enzyme activities and elevated blood-sugar levels. Copper sulphate, administered together with PQ and MD, were synergistic in terms of tissue damage and stress effects. The isoenzyme patterns showed organ-specific tissue damage. The administered chemical and isoenzymes indicating liver damage were detectable in the blood. The combination of CuSO4 and MD caused focal cell necrosis, which was observable in the liver tissue by light microscopy. Electron microscopic studies revealed the presence of damaged parenchymal cells with electron transparent cytoplasms, myelin figures, and altered mitochondria ER and Golgi.
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PMID:The effects of pesticides on some biochemical parameters of carp (Cyprinus carpio L.). 232 21

The concentration of total plasma bile acids was measured in normal sheep and in sheep in which liver damage was induced by chronic copper poisoning, ligated bile ducts or induced ketosis. All three treatments produced a rise in total bile acid concentration in plasma which was proportional to the degree of hepatic damage seen histologically and which tended to parallel changes in activity of iditol, and glutamate dehydrogenase and aspartate amino-transferase in plasma. Plasma bile acid concentration was a more sensitive method of detecting these types of liver damage than was the measurement of total plasma bilirubin concentration, and could be used to assess alterations in liver function in sheep.
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PMID:Changes in the concentrations of bile acids in the plasma of sheep with liver damage. 368 38

The effects of bivalent copper ions on the activity of bovine liver glutamate dehydrogenase (L-glutamate NAD (P) oxidoreductase, EC 1.4.1.3) were studied. Cu2+ effectively interacts with the enzyme; this interaction is accompanied by a loss of the enzyme activity in the reaction of reductive amination of alpha-ketoglutarate. The data obtained are indicative of a similar type of the enzyme inhibition by GTP and copper ions.
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PMID:[Effect of bivalent copper ions on the catalytic properties of bovine liver glutamate dehydrogenase]. 711 1

Pyrococcus furiosus is a strictly anaerobic archaeon that grows optimally at 100 degrees C by a fermentative-type metabolism in which complex peptide mixtures such as yeast extract and Tryptone, and also certain sugars, are oxidized to organic acids, H2 and CO2. Enzymes involved in the utilization of peptides such as proteases, aromatic amino transferases, and glutamate dehydrogenase have been previously purified from this organism. It is shown here that P. furiosus also contains significant cytoplasmic concentrations of a new enzyme termed indolepyruvate ferredoxin oxidoreductase (IOR). This catalyzes the oxidative decarboxylation of aryl pyruvates, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA. IOR is a tetramer (alpha 2 beta 2) of two identical subunits (66,000 and 23,000 Da) with a molecular weight of 180,000. The enzyme contains one molecule of thiamine pyrophosphate and four [4Fe-4S]2+,1+ and one [3Fe-4S]0,1+ cluster, as determined by iron analyses and EPR spectroscopy. Significant amounts of other metals such as copper and zinc were not detected. IOR was virtually inactive at 25 degrees C and exhibited optimal activity above 90 degrees C (at pH 8.0) and at pH 8.5-10.5 (at 80 degrees C). The enzyme was sensitive to inactivation by O2, losing 50% of its activity after exposure to air for 20 min at 23 degrees C, and was quite thermostable, with a half-life of activity at 80 degrees C (under anaerobic conditions) of about 80 min. The Km values (in microM) for indolepyruvate, p-hydroxyphenylpyruvate, phenylpyruvate, CoASH, and P. furiosus ferredoxin, the physiological electron carrier, were 250, 110, 90, 17, and 48, respectively. IOR was inhibited by KCN (apparent Ki = 7.5 mM), but not by CO (1 atm). An enzyme analogous to IOR has not been reported previously. Curiously, it has few properties in common with the pyruvate ferredoxin oxidoreductase of P. furiosus, even though the two enzymes catalyze virtually identical reactions. In fact, of known ketoacid oxidoreductases, the catalytic mechanism of IOR appears to be most similar to that of the pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium Thermotoga maritima.
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PMID:Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A new enzyme involved in peptide fermentation. 820 94

Inactivation of D-amino acid oxidase occurred by different mechanisms. The enzyme showed a rapid loss of activity in the presence of micromolar amounts of Cu2+ and Hg2+. It was also sensitive to oxidative inactivation by Fe2+ and H2O2 when both reagents were added in millimolar amounts. When oxidatively inactivated D-amino acid oxidase and a corresponding non-treated control were modified with the sulfhydryl-modifying, fluorescent reagent monobromobimane and subsequently digested with endoproteinase Glu-C, Cys-298 was identified to be a target for oxidative modification according to differences in the known peptide profile of fluorescence intensity. Another reason for the observed loss of enzyme activity in crude extracts was the specific proteolytic digestion of D-amino acid oxidase, which was dependent on the growth phase of the cells used. This cleavage was catalyzed by a serine-type proteinase and was the introductory step for the further complete degradation of the enzyme. In addition, a coenriched 50-kDa protein, identified as NADPH-specific glutamate dehydrogenase, significantly decreased the stability of the D-amino acid oxidase activity. Treatment of apo-D-amino acid oxidase from T. variabilis with monobromobimane resulted in a significantly increased fluorescence of two peptides, neither of which contained any cysteine residue. Thus, an involvement of cysteine residues in binding the FAD coenzyme should be excluded.
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PMID:Studies on the inactivation of the flavoprotein D-amino acid oxidase from Trigonopsis variabilis. 873 70

The NAD-dependent glutamate dehydrogenase (GDH) (EC 1.4.1.2) from Laccaria bicolor was purified 410-fold to apparent electrophoretic homogeneity with a 40% recovery through a three-step procedure involving ammonium sulfate precipitation, anion-exchange chromatography on DEAE-Trisacryl, and gel filtration. The molecular weight of the native enzyme determined by gel filtration was 470 kDa, whereas sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave rise to a single band of 116 kDa, suggesting that the enzyme is composed of four identical subunits. The enzyme was specific for NAD(H). The pH optima were 7.4 and 8.8 for the amination and deamination reactions, respectively. The enzyme was found to be highly unstable, with virtually no activity after 20 days at -75 degrees C, 4 days at 4 degrees C, and 1 h at 50 degrees C. The addition of ammonium sulfate improved greatly the stability of the enzyme and full activity was still observed after several months at -75 degrees C. NAD-GDH activity was stimulated by Ca2+ and Mg2+ but strongly inhibited by Cu2+ and slightly by the nucleotides AMP, ADP, and ATP. The Michaelis constants for NAD, NADH, 2-oxoglutarate, and ammonium were 282 &mgr;M, 89 &mgr;M, 1.35 mM, and 37 mM, respectively. The enzyme had a negative cooperativity for glutamate (Hill number of 0.3), and its Km value increased from 0.24 to 3.6 mM when the glutamate concentration exceeded 1 mM. These affinity constants of the substrates, compared with those of the NADP-GDH of the fungus, suggest that the NAD-GDH is mainly involved in the catabolism of glutamate, while the NADP-GDH is involved in the catalysis of this amino acid. Copyright 1997 Academic Press. Copyright 1997 Academic Press
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PMID:Purification and characterization of the NAD-dependent glutamate dehydrogenase in the ectomycorrhizal fungus laccaria bicolor (Maire) orton 945 44

15 castrated rams were exposed to an oral copper-dosage of 3.64 mg/d/kg body weight for 84 days. The control group consisted of 11 rams with a copper intake of 0.14 mg/d/kg bodyweight. Liver biopsies were taken percutaneously (100 samples), under laparoscopic control (53 samples) or post mortem (14 samples) before, during and up to 200 days after the controlled copper intake. Analysis of copper concentration in the liver tissue was done by a modified photometrical Bathocuproin-method after cold extraction with hydrochloric and trichloracetic acid. By using a parallel specimen blank with added EDTA, disturbing factors of the sample matrix were eliminated. The method was evaluated by the atom-absorption-spectroscopy after wet incineration as well as by standard addition of copper titrisol. The correlation with the reference method was very good (r > 0.99); the recovery rate after standard addition was 95 +/- 5.4%. The maximum copper concentrations in the liver were reached after the completion of the copper dosage. Blackheaded sheep showed significantly higher values (480 +/- 173 mg/kg wet tissue weight) than Merino sheep (338 +/- 103). The values of the control animals were 36 +/- 18 mg/kg. In the copper dosed rams the course of copper storage in the liver tissue could be described by an multiple regression with an accuracy of r2 > 0.75. The half-life of the copper concentration in the liver after exceeding maximum levels was 175 +/- 91 days. The pathogenetic role of the copper retention in the dosed animals was proven by regularly increased values of the hepatocellular enzyme glutamate dehydrogenase in the plasma.
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PMID:[Photometric determination of copper content in the liver during experimental chronic copper poisoning in sheep]. 947 15

Severe iron deficiency results in complex systemic disorders e.g., including metabolism of energy and minerals. To investigate whether also moderate iron depletion may alter the activities of citric cycle enzymes and the cytochrome oxidase, the trace element status, and serum enzymes indicative of cell damage, this experiment was carried out with rats supplied with sub-optimal iron (9, 13 and 18 mg iron per kg diet) over a total of 5 weeks. The study included 3 pair-fed groups and an ad libitum group, fed with 50 mg iron/kg diet. All iron-restricted rats were classified as iron-deficient on the basis of reduced iron concentrations in body and iron-depending blood parameters. Body weight gain and catalase activity in kidney were lowered in rats receiving the lowest dietary iron level, exclusively. Rats fed 9 and 13 mg iron per kg diet had nearly 6- and 3-fold, respectively higher platelet counts in blood than their corresponding pair-fed controls. The activities of transaminases ASAT and ALAT, alkaline phosphatase, glutamate dehydrogenase and lactate dehydrogenase in serum which are indicative of cell damage were also markedly influenced by moderate dietary iron restriction, in which the enzyme levels in serum increased with intensifying iron depletion. Although, moderate iron restriction to young male rats was associated with marked alterations in iron status and serum enzymes, the activities of tricarboxylic acid cycle enzymes including malic dehydrogenase, fumarase, and isocitric dehydrogenase as well as cytochrome oxidase in liver remained largely unaffected. Only hepatic aconitase showed a somewhat reduction with iron depletion. Moreover, iron restriction was also accompanied with an accumulation of copper in liver which was significant for rats fed 9 and 13 mg iron per kg diet, whereas zinc status remained completely unaffected by moderate iron deficiency. It can be concluded, that a short-term moderate iron deficiency with ranging hemoglobin concentrations from 66 and 121 g/L, was accompanied with altered platelet counts, serum enzyme activities indicative of cell damage, and hepatic copper concentrations, but the activities of the tricarboxylic acid cycle enzymes and cytochrome oxidase in liver remained largely unaffected.
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PMID:Effect of different degrees of moderate iron deficiency on the activities of tricarboxylic acid cycle enzymes, and the cytochrome oxidase, and the iron, copper, and zinc concentrations in rat tissues. 980 Mar 17


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