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)

Enzymes of parasite origin were identified by starch-gel electrophoresis. The species of parasite studied were Plasmodium berghei, Plasmodium yoelii nigeriensis, Babesia rodhaini and Anthemosoma garnhami. Lactate dehydrogenase, glucose phosphate isomerase and (NADP) glutamate dehydrogenase were detected in all species; phosphogluconate dehydrogenase was detected in both Plasmodium species but malate dehydrogenase only in P. y. nigeriensis. Glucose-6-phosphate dehydrogenase, alanine aminotransferase and aspartate aminotransferase were not detected in any parasite.
 ...
PMID:Biochemistry of intraerythrocytic parasites. I. Identification of enzymes of parasite origin by starch-gel electrophoresis. 38 67

Changes in oxidative metabolism were studied in hepatopancreas, muscle, and hemolymph of the edible crab Scylla serrata, exposed to a sublethal concentration (2.5 ppm) of cadmium chloride. A significant decrease in glycogen, total carbohydrates, and pyruvate and an increase in lactate levels in hepatopancreas and muscle were observed. Hemolymph sugar levels were increased in experimental crabs. An increase in phosphorylase suggested increased glycogenolysis during cadmium toxicity. The decrease in lactate dehydrogenase activity and the increase in lactate content indicated reduced mobilization of pyruvate into the citric acid cycle. Krebs cycle enzymes such as succinate dehydrogenase and malate dehydrogenase were found to be decreased, suggesting impairment of mitochondrial oxidative metabolism as a consequence of cadmium toxicity. Glucose-6-phosphate dehydrogenase activity was increased, suggesting enhanced oxidation of glucose by the HMP pathway. Cytochrome-c oxidase and Mg2+ ATPase activity levels decreased, indicating impaired energy synthesis during cadmium stress. Acid and alkaline phosphatase activities increased, suggesting enhanced breakdown of phosphates to release energy in view of impaired ATPase system during cadmium exposure. A significant decrease in protein and free amino acid and an increase in ammonia, urea, and glutamine levels were observed in the tissues during exposure. An increase in protease, alanine aminotransaminase, and aspartate aminotransaminase suggested increased proteolysis and transamination of amino acids. The increase in glutamate dehydrogenase, AMP deaminase, and adenosine deaminase indicated increased ammonia production. The increased arginase and glutamine synthetase suggested the detoxification or mobilization of ammonia toward the production of urea and glutamine. These results suggest that cadmium affects oxidative metabolism and induces hyperammonemia, and crabs switch over their metabolic profiles toward compensatory mechanisms for the survivability in cadmium-polluted habitats.
 ...
PMID:Changes in oxidative metabolism in selected tissues of the crab (Scylla serrata) in response to cadmium toxicity. 753 86

Activity of some enzymes of energy, protein and neurotransmitter metabolism in sensomotor cortex, caudate nucleus. S. nigra and N. accumbens of the right hemisphere was studied histochemically and biochemically, with parallel morphological investigation of these brain structures in rats bred for genetic predisposition to catalepsy (strain GC) and control Wistar rats. In GC rats, glutamate dehydrogenase activity was found to be increased in the cortex (by 12.8% in layer III and by 9.5% in layer V) and in the caudate nucleus (by 14.8%). Glucose-6-phosphate dehydrogenase activity was increased by 13.5% in layer III of the cortex, which, together with the increase of acetylcholine esterase activity in the light synaptosome fraction of the caudate nucleus (by 34.6%) reflects an advanced brain metabolism level as compared to Wistar rats. The diminution of the number of astroglia cells by 33.2% and oligodendroglia by 50.7% in N. accumbens, of neurons by 17.4% and astroglia by 24.6% with an increase of oligodendroglia cells by 21.6% in S. nigra seems to be associated with the change of functional activity of these brain structures. These structural changes in N. accumbens and S. nigra in rats with a genetic predisposition to cataleptic reaction reflect, probably, a pathological process in the central nervous system whose manifestation is susceptibility to catalepsy.
 ...
PMID:[The characteristics of the nigrostriatal brain system in genetic predisposition to catalepsy]. 816 May

Glucose-6-phosphate dehydrogenase (G6PD) and L-glutamate dehydrogenase (GDH) from Antarctic fish were isolated and characterized. G6PD was purified from the erythrocytes of red-blooded Dissostichus mawsoni and from the colorless blood of the icefish Chionodraco hamatus. Structural and functional characterization showed that the two enzymes do not differ significantly from each other. GDH was purified from the liver of the icefish Chaenocephalus aceratus. As in other fish ODHs, it showed a marked preference for NAD-. The amino acid sequence of the active-site peptide is virtually identical to that of other fish and vertebrate counterparts. Although the basic structural features of the Antarctic enzymes are similar to those of mesophilic organisms, some catalytic and thermodynamic properties make the Antarctic enzymes more suited to cold-adapted organisms.
 ...
PMID:Enzymes in antarctic fish: glucose-6-phosphate dehydrogenase and glutamate dehydrogenase. 950 17

Under conditions of controlled pH, nitrate and ammonium are equally effective in supporting the growth of young soybean (Glycine max var. Bansei) and sunflower (Helianthus annuus L. var., Mammoth Russian) plans. Soybean contains an active nitrate reductase in roots and leaves, but the low specific activity of this enzyme in sunflower leaves indicates a dependency upon the roots for nitrate reduction. Suppression of nitrate reductase activity in sunflower leaves may be due to high concentrations of ammonia received from the roots. Nitrate reductase activity in leaves of nitrate-supplied soybean and sunflower follows closely the distribution of nitrate reductase. For the roots of both species, glutamic acid dehydrogenase activity was greater with ammonium than with nitrate. The glutamic acid dehydrogenase of ammonium roots is wholly NADH-dependent, whereas that of nitrate roots is active with NADH and NADPH. In leaves, an NADPH-dependent glutamic acid dehydrogenase appears to be responsible for the assimilation of translocated ammonia and ammonia formed by nitrate reduction.In soybean roots ammonia is actively incorporated into amides, much of which remains in the roots. Sunflower roots are less active in amide formation but transfer much of it, together with ammonia, into the shoots. Glutamine synthetase activity in leaves is 20- to 40-fold lower than in roots.Glucose-6-phosphate dehydrogenase activity appears to be correlated with the activity of the nitrate reducing system in roots, but not in leaves.
 ...
PMID:Influence of ammonium and nitrate nutrition on enzymatic activity in soybean and sunflower. 1665 12