Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.6.1.2 (alanine aminotransferase)
 26,722 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenases were measured in nervous tissue from different animals in an attempt to provide more information about the citric acid cycle in this tissue. In higher animals the activities of citrate synthase are greater than the sum of activities of the isocitrate dehydrogenases, whereas they are similar in nervous tissues from the lower animals. This suggests that in higher animals the isocitrate dehydrogenase reaction is far-removed from equilibrium. If it is assumed that isocitrate dehydrogenase activities provide an indication of the maximum flux through the citric acid cycle, the maximum glycolytic capacity in nervous tissue is considerably greater than that of the cycle. This suggest that glycolysis can provide energy in excess of the aerobic capacity of the tissue. 2. The activities of glutamate dehydrogenase are high in most nervous tissues and the activities of aspartate aminotransferase are high in all nervous tissue investigated. However, the activities of alanine aminotransferase are low in all tissues except the ganglia of the waterbug and cockroach. In these insect tissues, anaerobic glycolysis may result in the formation of alanine rather than lactate.
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PMID:Activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenases, glutamate dehydrogenase, aspartate aminotransferase and alanine aminotransferase in nervous tissues from vertebrates and invertebrates. 0 Oct 3

In the nerve tissue with proliferating macroglia cells were observed a lowered oxygen consumption, an increased aerobic glycolysis and alanine formation and a higher alanine aminotransferase and glutamate dehydrogenase activity than in the control tissue in the homogenates and in the cell sap fraction. The substrate saturation curves, apparent Km and pH optimum values in the tissue with proliferating macroglia and in the control did not differ from one another. The authors assume that a higher alanine aminotransferase activity in the tissue with macroglia proliferation can reflect either a higher synthesis of the enzyme in the altered tissue, or a predominance of glial elements in the altered tissue possessing a higher alanine aminotransferase activity than the nerve cells.
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PMID:Alanine formation and alanine aminotransferase activity in the nerve tissue with proliferating macroglia. 0 40

In previous studies it was found that: (a) aspartate aminotransferase increases the aspartate dehydrogenase activity of glutamate dehydrogenase; (b) the pyridoxamine-P form of this aminotransferase can form an enzyme-enzyme complex with glutamate dehydrogenase; and (c) the pyridoxamine-P form can be dehydrogenated to the pyridoxal-P form by glutamate dehydrogenase. It was therefore concluded (Fahien, L.A., and Smith, S.E. (1974) J. Biol. Chem 249, 2696-2703) that in the aspartate dehydrogenase reaction, aspartate converts the aminotransferase into the pyridoxamine-P form which is then dehydrogenated by glutamate dehydrogenase. The present results support this mechanism and essentially exclude the possibility that aspartate actually reacts with glutamate dehydrogenase and the aminotransferase is an allosteric activator. Indeed, it was found that aspartate is actually an activator of the reaction between glutamate dehydrogenase and the pyridoxamine-P form of the aminotransferase. Aspartate also markedly activated the alanine dehydrogenase reaction catalyzed by glutamate dehydrogenase plus alanine aminotransferase and the ornithine dehydrogenase reaction catalyzed by ornithine aminotransferase plus glutamate dehydrogenase. In these latter two reactions, there is no significant conversion of aspartate to oxalecetate and other compounds tested (including oxalacetate) would not substitute for aspartate. Thus aspartate is apparently bound to glutamate dehydrogenase and this increases the reactivity of this enzyme with the pyridoxamine-P form of aminotransferases. This could be of physiological importance because aspartate enables the aspartate and ornithine dehydrogenase reactions to be catalyzed almost as rapidly by complexes between glutamate dehydrogenase and the appropriate mitochondrial aminotransferase in the absence of alpha-ketoglutarate as they are in the presence of this substrate. Furthermore, in the presence of aspartate, alpha-ketoglutarate can have little or no affect on these reactions. Consequently, in the mitochondria of some organs these reactions could be catalyzed exclusively by enzyme-enzyme complexes even in the presence of alpha-ketoglutarate. Rat liver glutamate dehydrogenase is essentially as active as thebovine liver enzyme with aminotransferases. Since the rat liver enzyme does not polymerize, this unambiguously demonstrates that monomeric forms of glutamate dehydrogenase can react with aminotransferases.
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PMID:Effect of aspartate on complexes between glutamate dehydrogenase and various aminotransferases. 1 47

The activities of GOT, GPT, LDH, gamma-glutamyltranspeptidase (gamma-GTP), alkaline phosphatase (AP), glutamate dehydrogenase (GLDH) and the concentrations of bilirubin in blood plasma after a single intraruminal application of aflatoxins were studied in four dairy cows. The maximum changes in the activities of the enzymes and the maximum bilirubin concentration in plasma were obtained in the first two to three days following the application of aflatoxins. The statistically significant increase of GOT activity, compared with activity before the application of aflatoxins, persisted until the 23rd day; in the case of LDH and GLDH the increase persisted until the 38th day from the application of aflatoxins. The activities of gamma-GTP and AP were slightly higher even on the 50th day. The increased concentration of bilirubin in plasma lasted until the 23rd day from aflatoxin application. The increased activities of enzymes testify to an impaired function of the liver, which is also proved by the specific enzymes GLDH, gamma-GTP, by increased bilirubin levels, and by histological changes known from literature. The evaluation of enzymatic activities and bilirubin concentration in plasma can make a valuable contribution to correct diagnosis of aflatoxicoses in cattle.
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PMID:[Changes in enzyme activity induced by experimental aflatoxicosis in dairy cows]. 1 36

Biotin deficiency in Aspergillus nidulans resulted in a 70% increase of the protein content and increased levels of free and bound aspartate, glutamate, serine, leucine and methionine. Likewise, the activities of NADP+ glutamate dehydrogenase, NAD+ gluatmate dehydrogenase, aspartate aminotransferase and alanine aminotransferase were significantly increased. The total RNA content increased while the DNA content was unaffected. The rRNA/tRNA ratio remained higher in biotin-deficient cells. Supplementation of glutamate, aspartate, serine, leucine and methionine to the culture medium raised the rRNA/tRNA ratio, and the difference observed in the qualitative and the quantitative patterns of protein and dry cell mass between normal and biotin-deficient cultures was abolished.
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PMID:Factors affecting protein synthesis during biotin deficiency in Aspergillus nidulans. 4 77

Chronic ammonia toxicity in experimental mice was induced by exposing them for 2 and 5 days to 5 % (v/v) ammonia solution. The enzymes concerned with glutamate metabolism (aspartate-, alanine- and tyrosine aminotransferases, glutamate dehydrogenase and glutamine synthetase) and (Na+ + K+)-ATPase were estimated in the three regions of brain (cerebellum, cerebral cortex and brain stem) and in liver. Glutamate, aspartate, alanine, glutamine and GABA, RNA and protein were also estimated in the three regions of brain and liver. A significant rise in the activity of (Na+ + K+)-ATPase in all the three regions of brain along with a fall in the activity of alanine aminotransferase was noticed. Changes in the activities of other enzymes were also observed. A significant increase in alanine and a decrease in glutamic acid was observed while no change was observed in the content of other amino acids belonging to the glutamate family. As a result of this, changes in the ratios of glutamate/glutamine and glutamate + aspartate/GABA was observed. The results indicated that the brain was in a state of more depression and less of excitation. Under these conditions the liver tissue was showing a profound rise in the activity of the enzymes of glutamate metabolism. The results are further discussed.
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PMID:Chronic metabolic effects of ammonia in mouse brain. 9 19

Tetrahymena pyriformis Wh 14 was grown in Erlenmeyer flasks under continuous stirring at 30 degrees C for three days . After the culture had produced dry matter of about 100 mg HCB was added in acetone at a dose level of 0, 0.001, 0.1 and 1.0 ppm to the culture and incubated for another 7 days. At a dose level of 0.001 ppm the activity of delta-aminolevulinate dehydratase, hexokinase, and pyruvate kinase remained unaffected but was increased for glutamic-oxaloacetic transaminase, glutamic dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase while 0.1 ppm HCB increased the activity of all enzymes studied, the only exception being glutamic-pyruvic transaminase, the activity of which was depressed by HCB exposure. A concentration of 1.0 ppm HCB depressed the activity of most of the enzymes below control values with the exception of the two mitochondrial enzymes, MDH and ICDH, studied here.
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PMID:Effect of hexachlorobenzene (HCB) on the activity of some enzymes from Tetrahymena pyriformis. 10 53

Adaptation of Ehrlich ascites tumor cells to serial cultivation in media with progressively elevated (hypertonic) NaCl content ("high NaCl"-tolerant cells) has resulted in progressive increases of the cellular activities of NAD-dependent glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), NAD-dependent malate dehydrogenase (EC 1.1.1.37), glutamate--oxalacetate transaminase (EC 2.6.1.1), NAD (P)-dependent glutamate dehydrogenase (EC 1.4.1.3), NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42). The activities of glutamate-pyruvate transaminase (EC 2.6.1.2.) and of glycolytic enzymes as phospho-fructokinase (EC 2.7.1.11), glyceraldehydephosphate dehydrogenase (EC 1.2.1.12) and lactate dehydrogenase (EC 1.1.1.27) were only slightly and not in progressive manner (in response to the progressive increase of the environmental NaCl concentration) affected. These changes are discussed with respect to a metabolic pattern of these "high NaCl"-tolerant cells which is compatible with increased energy requirements, especially for active cation transport. It is suggested that these increased cellular enzyme activities reflect an increased transfer of reducing equivalents across mitochondrial membranes (via the "glycerophosphate cycle and the malate-aspartate shuttle") and possibly a stimulated lipid metabolism. These alterations in the level of enzyme activities must be regarded asan adaptive cellular response to the "high NaCl" environment, since readaptation to growth in regular isotonic media resulted in a reversion to the enzyme pattern characteristic of the parent cells.
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PMID:Changes in enzyme pattern of Ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content. 12 1

The activities of glutamic-oxaloacetic transaminase (GOT), glutamic-pyruvic transaminase (GPT) and glutamate dehydrogenase (GLD) were determined in liver biopsy specimens and sera of patients with various liver diseases. Mitochondrial and cytosol isozymes of GOT were also separated for their assay. The activity ratio of GOT/GPT in serum was found to reflect the ratio in liver cytosol. The increased ratio in advanced or severe liver diseases, such as liver cirrhosis, was due to the greater decrease in liver cytosol GPT activity, this being pronounced in primary hepatoma. The activity of GLD decreased similarly but less markedly. The relatively greater decrease in GPT compared with GOT in advanced liver diseases was not mainly due to leakage of the enzyme from the liver, but to a specific mechanism associated with hepatic injury or its progression. Other pathological conditions of the liver such as those in obstructive jaundice and alcoholic liver injury also appeared to result in reduced liver GPT activity, which was reflected in the serum as an increased GOT/GPT ratio.
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PMID:The mechanism of release of hepatic enzymes in various liver diseases. II. Altered activity ratios of GOT to GPT in serum and liver of patients with liver diseases. 16 Jan 82

1)The time course of changes in concentration of renal metabolites in response to a non-toxic load of NH4 as NH4 Cl or NH4HCO3 were measured in fasted rats. 2) Following a NH4Cl load, decrease of renal concentration of 2-oxoglutarate occurs but this change is delayed in relation to the peak of the blood ammonia concentration and persists after disappearance of the hyperammoniemia. 3) Following a NH4HCO3 load, the oxoglutarate concentration changes are less marked and more transient. 4) No close relationship between the mitochondrial free NAD/NADH ratio calculated from the glutamate dehydrogenase and the 3-hydroxybutyrate dehydrogenase systems were seen during alteration of the ammonia concentration. 5) Contrary to the observations in the liver under similar circumstances (BROSNAN, J.T. et al.: Biochem.J. 138, 453, 1974), no increase in kidney tissue or renal venous blood alanine or aspartate concentration are seen. 6) A constant infusion of NH4HCO3 resulted only in an increase in tissue and renal venous blood glutamine concentration. 7) The infusion of NH4 together with a carbon source (malate) resulted in a similar increase in tissue glutamine concentration and more striking increase in renal venous glutamine concentration. No accumulation of aspartate nor alanine were seen. 8) In vitro studies indicate that the net flux through both the aspartate aminotransferase and the glutamate dehydrogenase reactions is dependent on the concentration of the reactants as expected for a near-equilibrium system. 9) It is concluded that the kidney response to an ammonia load differs from that of the liver despite the existence of a similar network of near-equilibrium reactions of (1) a lack of local availability of oxaloacetate, (2) a lower activity of alanine aminotransferase, (3) a greater in vivo activity of glutamine synthetase.
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PMID:Effect of an ammonia load on the kidney near-equilibrium systems in the rat in vivo. 18 80


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