Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.6.1.19 (GABA transaminase)
808 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of enzymes involved in the tricarboxylic acid cycle was studied in Nocardia erythropolis IBFM B-293. It was found to be low and hardly change, with some exceptions, in the course of growth in the presence of various carbon sources. Acetate induced enzymes of the glyoxylate cycle which was here an important mechanism of oxalacetate synthesis. The absence of alpha-ketoglutarate dehydrogenase in the case of all studied substrates and the absence of 4-aminobutyrate aminotransferase, the key enzyme of the compensating 4-aminobutyrate shunt, suggest that the tricarboxylic acid cycle is decoupled. Therefore, this cycle does not operate as a mechanism generating energy in N. erythropolis, but fulfills mainly biosynthetic functions.
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PMID:[Characteristics of the tricarboxylic acid cycle in Nocardia erythropolis]. 42 7

Adult male rats were exposed to Hashish smoke for 15 min. Certain biochemical parameters were determined. This treatment did not change the brain glutamic acid level, whereas it significantly decreased brain gamma aminobutyric acid level. There was a significant increase in the activity of the brain enzyme forming gamma aminobutyric acid, namely glutamate decarboxylase, as well as in that enzyme metabolizing gamma aminobutyric acid, namely aminobutyrate aminotransferase. However, the increase was much more marked in the case of aminobutyrate aminotransferase, a finding that might explain the decrease observed in brain gamma aminobutyric acid upon exposure to Hashish. Blood glucose and fibrinolytic activity were significantly increased. It was concluded that these changes might be due to an adrenaline releasing effect of Hashish smoke inhalation. Serum lactate dehydrogenase and serum glutamate oxalacetate transaminase activities were significantly increased, whereas serum glutamate pyruvate transaminase activity was unaffected. From these data it was suggested that the source of leakage of these enzyme activities into the blood is probably the skeletal muscles rather than the liver.
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PMID:Effect of hashish on brain gamma aminobutyric acid system, blood fibrinolytic activity and glucose and some serum enzymes in the rat. 121 94

We have isolated and characterized an aspartate transaminase (glutamate:oxalacetate transaminase, EC 2.6.1.1) from the thermophilic microorganism Bacillus stearothermophilus. The purified enzyme has a molecular mass of 40.5 kDa by sodium dodecyl sulfate gel analysis, a temperature optimum of 95 degrees C, and a pH optimum of 8.0. The corresponding gene, aspC, was cloned and overexpressed in Escherichia coli. The recombinant glutamate:oxalacetate transaminase protein was used in immobilized form together with 4-aminobutyrate:2-ketoglutarate transaminase (EC 2.6.1.19) from E. coli for the production of L-phosphinothricin [L-homoalanin-4-yl-(methyl)phosphinic acid], the active ingredient of the herbicide Basta (AgrEvo GmbH), from its nonchiral 2-keto acid precursor 2-oxo-4-[(hydroxy)(methyl)phosphinoyl]butyric acid (PPO). In this new coupled process conversion rates of ca. 85% were obtained with substrate solutions containing 10% PPO by using only slight excesses of the amino donors glutamate and aspartate. The contamination of the reaction broth with amino acid by-products was < 3%.
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PMID:Stereospecific production of the herbicide phosphinothricin (glufosinate): purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process. 883 36