Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.4.1.1 (pyruvate carboxylase)
 1,516 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cell extracts of Pseudomonas aeruginosa strain PAO were found to contain pyruvate carboxylase activity. Specific activities were minimal when cells were grown on Casamino Acids, acetate, or succinate, but were three- to fourfold higher when cells were grown in glucose, gluconate, glycerol, lactate, or pyruvate minimal media. The reaction in crude cell extracts and in partially purified preparations was dependent on pyruvate, adenosine 5'-triphosphate, and Mg(2+), but was not affected by either the presence or absence of acetyl coenzyme A. Activity was nearly totally inhibited by avidin and this inhibition was substantially blocked by free biotin in incubation mixtures. Cell extracts were shown to fix (14)CO(2) in a reaction that had these same characteristics. Eight pleiotropic, carbohydrate-negative mutant strains of the organism were isolated after nitrosoguanidine mutagenesis. Each mutant strain grew normally in acetate, succinate, and citrate minimal media but failed to utilize glucose, gluconate, 2-ketogluconate, mannitol, glycerol, lactate, and pyruvate as sole sources of carbon and energy. These strains were found by quantitative transductional analysis with phage F116 to form a single linkage group. Cell extracts of each mutant strain were either lacking or severely deficient in pyruvate carboxylase activity. Spontaneous revertants of five of the eight strains were isolated and found to recover simultaneously both pyruvate carboxylase activity and the ability to utilize each of the C(6) and C(3) compounds. A second linkage group of similar mutant strains that grew on the C(3) compounds was found to contain normal levels of pyruvate carboxylase activity, but each strain was deficient in an enzyme of the Entner-Doudoroff pathway.
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PMID:Pyruvate carboxylase deficiency in pleiotropic carbohydrate-negative mutant strains of Pseudomonas aeruginosa. 420 15

The object of this work was to investigate the operation of enzymes of the citric acid cycle, the glyoxylate pathway, the glucose metabolism as well as of pyruvate and phosphoenolpyruvate carboxylases in Pseudomonas aeruginosa 640x capable of complete degradation of DDT under the conditions of cometabolism. The activity of isocitrate and glucose-6-phosphate dehydrogenases producing reduced NADP, which is required for reductive dechlorination of DDT, appears to be high. Pyruvate carboxylase and phosphoenolpyruvate carboxylase (EC 4.1.1.31.) function simultaneously in the culture. Differences in the pathways of anaplerotic carbon dioxide fixation were found in P. aeruginosa 640x and the collection strain of P. aeruginosa PAO incapable of DDT degradation.
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PMID:[Central metabolic characteristics of a Pseudomonas aeruginosa culture degrading DDT]. 680 12