Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17174 (aspartate aminotransferase)
 14,872 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

384 hospitalized patients of both sexes were classified into drinkers and non-drinkers according to clinical criteria. On admission, we measured four blood parameters : glutamate dehydrogenase, gamma glutamyl transferase, aspartate aminotransferase and the mean corpuscular volume. the discriminating power of these laboratory parameters was evaluated by descriptive statistical tests and by the determination of their positive and negative predictive value. Glutamate dehydrogenase appears to present a sensitivity almost equivalent to that of gamma glutamyl transferase and a better specificity : this results in a more positive predictive value. The two other laboratory parameters are less discriminating.
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PMID:[Role of glutamate dehydrogenase in the biological detection of excessive drinkers]. 613 49

Glutamate dehydrogenase activity was determined in mitochondrial preparations from rat ventral prostate and rat kidney. Kinetic parameters of the ventral prostate enzyme were comparable to those for the kidney enzyme. Glutamate dehydrogenase activity in the direction of glutamate oxidative deamination was inhibited by alpha-ketoglutarate. However, the characteristics of alpha-ketoglutarate inhibition indicated that glutamate oxidation via glutamate dehydrogenase can occur at in vivo prostatic alpha-ketoglutarate levels. These results suggest that glutamate dehydrogenase activity in prostate may provide a continuous source of alpha-ketoglutarate for aspartate transamination to oxalacetate and ultimate citrate synthesis. In addition prostate mitochondria are able to couple the glutamic dehydrogenase reaction to aspartate aminotransferase. Under these conditions aspartate in the presence of glutamate and acetyl coenzyme A will result in a net synthesis of citrate. Consequently we propose an aspartate-glutamate pathway for citrate synthesis in prostate.
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PMID:Glutamate dehydrogenase and a proposed glutamate-aspartate pathway for citrate synthesis in rat ventral prostate. 615 Jan 22

Eleven soluble enzymes in the supernatant of bloodstream Trypanosoma brucei were compared for electrophoretic mobility and activity with those of T. brucei cultures grown in 3 different media. All bands of each enzyme found in the bloodstream form were also present in the cultured material, but extra bands of malate dehydrogenase (MDH) (EC 1.1.1.37), aspartate aminotransferase (ASAT) (EC 2.6.1.1), and in 2 to 6 cultures of isocitrate dehydrogenase (ICD) (EC 1.1.1.42) were present in culture forms but not in bloodstream forms. An interfering enzyme, peculiar to cultured T. brucei, which reacted with 2-oxoglutarate and possibly a trace amount of ammonium ions, ran with the fast-moving ASAT bands. Threonine dehydrogenase activity, high in cultured trypanosomes irrespective of the medium used but low in bloodstream trypanosomes, was markedly lower in Trypanosoma evansi and a much passaged T. brucei 8/18. Glucosephosphate isomerase activity on the other hand was high in bloodstream and low in cultured trypanosomes. Glutamate dehydrogenase activity was too low to record reliably in bloodstream trypanosomes, but could be clearly detected in cultured forms. As the differences point to some changes in gene expression between the two forms, culture material is likely to replace trypanosomes from living animals for electrophoretic characterization only when considerable comparative work has been done.
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PMID:The electrophoretic mobilities and activities of eleven enzymes of bloodstream and culture forms of Trypanosoma brucei compared. 645 Aug 96

Glutamate dehydrogenase (GDH) and the transaminases namely aspartate aminotransferase (AAT) and alanine aminotransferase (AIAT) were estimated in the muscle, liver, kidney, and brain of control and ammonium acetate administered frogs. The results indicated tissue specific responses during induced ammonotoxemia. The inherent endogenous ammonia production decreased in all the tissues. 2-Keto glutarate production appears to be the other main adaptive feature as a result of slightly stepped up transdeamination patterns.
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PMID:Transamination and glutamate deamination in Rana hexadactyla during induced ammonia toxicity. 651 Oct 61

Glutamate dehydrogenase activity in the liver of the rainbow trout increases when the animals are starved for four weeks. Glutamate dehydrogenase, alanine aminotransferase and aspartate aminotransferase activity in the kidney of rainbow trout kept in sea water (20% S) is significantly higher than in the kidney of rainbow trout kept in fresh water. Gill Na/K-ATPase activity in the rainbow trout is reduced significantly (44%) by starvation for four weeks. Most of the free amino acids investigated in the white muscle of the rainbow trout were present in significantly higher concentrations in animals fed in sea water than in animals fed in fresh water. The concentrations of these amino acids are even higher in the muscle of starved animals held in sea water than in fed animals held in sea water.
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PMID:Influence of nutrition on biochemical sea water adaptation of the rainbow trout (Salmo gairdneri richardson). 661 64

Experiments performed in polyethylene glycol and with a divalent crosslinker indicate that both mitochondrial malate dehydrogenase and aspartate aminotransferase can form hetero enzyme--enzyme complexes with either glutamate dehydrogenase or citrate synthase. In general, these as previous results indicate that complexes with the aminotransferase are favored over those with malate dehydrogenase and complexes with glutamate dehydrogenase are favored over those with citrate synthase. When the levels of enzymes are low, the only detectable complex is between the aminotransferase and glutamate dehydrogenase. Under these conditions, palmitoyl-CoA is required for complexes between the other three enzyme pairs, however, palmitoyl-CoA also enhances interactions between glutamate dehydrogenase and the aminotransferase. DPNH disrupts complexes with malate dehydrogenase and has little effect on those with the aminotransferase, while oxalacetate disrupts complexes with citrate synthase but has little effect on those with glutamate dehydrogenase. The citrate synthase-aminotransferase complex was favored in the presence of DPNH plus malate, which disrupt the other three enzyme-enzyme complexes. Glutamate dehydrogenase has a higher affinity and capacity than citrate synthase for palmitoyl-CoA. Consequently, lower levels of palmitoyl-CoA are required to enhance interactions with glutamate dehydrogenase. Furthermore, glutamate dehydrogenase can compete with citrate synthase for palmitoyl-CoA and thus can prevent palmitoyl-CoA from enhancing interactions between citrate synthase and either malate dehydrogenase or the aminotransferase.
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PMID:Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase. 682 31

1. The two molecular forms of mitochondrial malate dehydrogenase are partly bound to the mitochondrial membranes. 2. The A form is located on the outer surface of the inner mitochondrial membrane and also in the intermembrane space. 3. The B form of the enzyme appears in the matrix and bound in part, probably, to the inner surface of the inner mitochondrial membrane. 4. Glutamate dehydrogenase, glutamate oxaloacetate transaminase, fumarase and lactate dehydrogenase are bound, to a greater or lesser extent, to the mitochondrial membranes, the fumarase having the highest degree of binding.
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PMID:Intramitochondrial location of the molecular forms of chicken liver mitochondrial malate dehydrogenase. 706

Reaction of the pyridoxal form of cytosolic aspartate aminotransferase from pig heart with 1,2-cyclohexanedione or other alpha-dicarbonyls led to a progressive decrease in the enzymic activity toward natural dicarboxylic substrates. The inactivation was prevented by the presence of dicarboxylic substrate analogs. The dependence of the inactivation rate on the cyclohexanedione concentration indicated that the modifying reagent forms a dissociable complex with the enzyme prior to the inactivation. These saturation kinetics were observed also with other alpha-dicarbonyls tested. The inactivation was fully accounted for by the modification of a single arginine residue per monomeric unit of the enzyme. Activities for alpha, beta-elimination reaction with 3-chloro-L-alanine and transamination with L-alanine did not decrease but appeared to increase considerably with the progress of the arginine modification. In these aberrant reactions, affinity for the monocarboxylic substrates was higher with the modified enzyme than with the native unmodified enzyme. Glutamate or aspartate was still capable of reacting with the pyridoxal form of the extensively modified enzyme to produce the pyridoxamine form at a rate comparable to that of the reaction with 3-chloro-L-alanine or L-alanine. Succinate, glutarate, maleate, 2-methylaspartate or erythro-3-hydroxy-aspartate which bind strongly to the native enzyme and thus acts as potent inhibitors in the reactions with monocarboxylic substrates did not exhibit any appreciable inhibitory effect on these reactions catalyzed by the arginine-modified enzyme. Proton NMR spectroscopy demonstrated that succinate strongly interacts with the native enzyme to generate substantial changes in the enzyme spectra whereas there was no such evidence for the specific interaction with this dicarboxylate with the arginine-modified enzyme.
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PMID:A critical arginine residue in cytosolic aspartate aminotransferase from pig heart. 707 57

Holstein bull calves were used to determine the influence of degradable nitrogen and ration physical form on rumen epithelial transport and enzymic activity. Rations contained 30, 45 and 60% ruminal degradable nitrogen (RDN), each with three forms (ground hay, GR; chopped hay, CH; and all concentrate, CONC). Rumen tissue samples were obtained by biopsy (8 weeks) and at slaughter (20 weeks). Acetate transport across rumen epithelium increased between 8 and 20 weeks in calves fed GR and CH, but not in calves fed CONC. Propionate transport was highest in calves fed GR and lowest in calves fed CONC at both 8 and 20 weeks. Transport of acetate and propionate was incresed with increasing RDN at 20 weeks. There were no differences in ruminal tissue lactate production. Rumen papillae of calves fed CONC were abnormal in morphology and at 20 weeks dry mucosal weights (mg/cm2) were highest. Lactate dehydrogenase and NADP-malic dehydrogenase activities were not different. Propionyl CoA synthetase activity was higher in 20-week calves fed CONC, compared to GR to CH. Glutamate dehydrogenase and aspartate aminotransferase activities were highest in 20-week calves fed 60% RDN rations, regardless of physical form.
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PMID:Influence of ration physical form, ruminal degradable nitrogen and age on rumen epithelial propionate and acetate transport and some enzymatic activities. 744 67

The C57BL/10 SPS/sps mouse mutant are audiogenic seizure-susceptible. The enzymatic activities of glutamate decarboxylase (GAD), GABA aminotransferase (GABA-T), alanine aminotransferase (ALA-T), aspartate aminotransferase (ASP-T), and glutamate dehydrogenase (GDH) of whole brain supernatant are significantly reduced in these epileptic mice. GABA uptake is decreased in cortex, midbrain, and pons medulla. Previous studies showed the presence of two sodium-dependent GLU uptake systems in normal (SPS/SP) mice. Glutamate Umax by System 1 is significantly decreased in these mice, whereas the Umax value for System 2 is significantly increased in the epileptic mice.
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PMID:Altered GABAergic and glutamatergic transmission in audiogenic seizure-susceptible mice. 788 3


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