Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

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

Pyruvate carboxylase activity was measured in phytohemagglutinin-transformed lymphocytes (i.e. lymphoblasts). Mean value +/- S.D. for 10 controls was 259 +/- 38 pmoles/min per mg protein. It was about 7 times higher than that of peripheral leukocytes and a half of cultured skin fibroblasts with similar techniques. Deficient pyruvate carboxylase activity less than 6 pmoles/min per mg protein was demonstrated in the lymphoblasts from a patient with biotin-dependent multiple carboxylase deficiency. It is suggested that lymphoblasts may allow more reliable and ready diagnosis of patients with pyruvate carboxylase deficiency.
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PMID:Lymphoblasts and diagnosis of pyruvate carboxylase deficiency. 680 93

Adult male Long-Evans rats (250-300 g) were fed diets containing 15% of casein not supplemented with amino acids, supplemented with 0.505% cysteine or supplemented with 0.620% methionine for a period of 17 days. Rats fed the diets supplemented with cysteine had an increased incorporation of the 14C-radioactivity from [U-14C]alanine into liver glycogen and a decreased incorporation from [U-14C]acetate into fatty acids. Pyruvate carboxylase activity was slightly increased and citrate cleavage enzyme activity decreased in the livers of those rats fed the diets supplemented with cysteine. Rats fed diets supplemented with methionine had a decreased liver phosphoenolpyruvate carboxykinase activity. Based on these data it appears that rats fed diets supplemented with cysteine adapt metabolically to store energy as glycogen, while those fed diets supplemented with methionine tend to store energy as lipid.
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PMID:A metabolic comparison of cysteine and methionine supplements in the diet of a rat. 682 95

Pyruvate carboxylase activity was investigated in cultured fibroblasts from a patient shown to have hepatic pyruvate carboxylase deficiency. Under standard conditions, the activity in fibroblasts was 50% of controls (p less than 0.001). Kinetic investigations of the enzyme showed abnormal protein linearity with low activity at low protein concentration. Mixture of homogenates from the patient and a control revealed no endogenous inhibitor. Temperature stability of the mutant enzyme was similar to controls. Apparent kinetic constants for the substrates bicarbonate, ATP and pyruvate were in the patient 2.6 mmol/l, 0.08 mmol/l and 0.10 mmol/l compared to 2.1 mmol/l, 0.13 mmol/l and 0.22 mmol/l in controls, respectively. The 50% inhibitory concentration of oxaloacetate was 0.5 mmol/l in controls. However, no inhibitory effect of oxaloacetate was found for pyruvate carboxylase in fibroblasts from the patient. With acetyl-CoA, the apparent activation constant was 0.21 mmol/l in controls and 0.10 mmol/l in the patient, while the Hill coefficients were similar. These results may be explained by a mutation primarily affecting the transcarboxylation site of pyruvate carboxylase from the patient.
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PMID:A mutation of pyruvate carboxylase in fibroblasts from a patient with severe, chronic lactic acidaemia. 688 8

The specific activity of pyruvate carboxylase [pyruvate:carbon-dioxide ligase (ADP-forming); EC 6.4.1.1] in 3T3-L1 cells increases approximately 20-fold when these cells differentiate to an adipocyte-like form [Mackall, J. C. & Lane, M. D. (1977) Biochem. Biophys. Res. Commun. 79, 720-725]. A specific antibody to the purified rat liver enzyme quantitatively precipitated pyruvate carboxylase from 3T3-L1 crude homogenates. Use of this immunological technique permitted us to demonstrate that the increase in pyruvate carboxylase activity is due to an increase in the intracellular concentration of the enzyme. The content of pyruvate carboxylase in differentiated 3T3-L1 cells is sufficiently high (1-2% of total protein) that the increase in this large protein (subunit M(r) = 130,000) can be visualized when 3T3-L1 crude extracts are subjected to electrophoresis on sodium dodecyl sulfate/polyacrylamide gels. When 3T3-L1 cells differentiated in the presence of avidin, they contained less than 5% of the pyruvate carboxylase activity of cells that differentiated in the absence of avidin. However, the immunoprecipitable pyruvate carboxylase content of the avidin-treated cells was essentially the same as that of cells that differentiated without avidin. Full activity of the enzyme was rapidly restored in the avidin-treated cells upon the addition of excess biotin. The recovery of activity was closely correlated with the incorporation of [(14)C]biotin into immunoprecipitable pyruvate carboxylase. The rapidity with which the activity was restored and the insensitivity of the process to inhibitors of protein synthesis strongly suggest that the apoenzyme of pyruvate carboxylase accumulates during differentiation in the presence of avidin.
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PMID:Induction of pyruvate carboxylase apoenzyme and holoenzyme in 3T3-L1 cells during differentiation. 692 88

The effect of 90% jejunoileal bypass procedure on liver enzymes was evaluated in 11 obese Zucker fat rats after a 50% weight loss. Control tissues were also collected from 11 unoperated obese rats. In the jejunoileal bypass group, there was a significant decrease in phosphofructokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase activities. Pyruvate carboxylase, alanine aminotransferase, and lactate dehydrogenase activities were not altered. Fructose 1,6-biphosphatase, aldolase, aspartate aminotransferase, and phosphoenolpyruvate carboxykinase activities were increased in the jejunoileal bypass group. These studies suggest that after jejunoileal bypass glycolysis is reduced and gluconeogenesis is increased. Amino acids may provide an essential energy source for hepatic function.
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PMID:Changes in hepatic carbohydrate metabolism after jejunoileal bypass. 707 18

Pyruvate carboxylase of the facultative methylotroph Pseudomonas oleovorans was purified 40-fold by ammonium sulfate fractionation, gel filtration on Ultrogel AcA 34, ion-exchange chromatography on DEAE-Biogel A and concentration on DEAE-Sepharose CL-6B. The enzyme exerts its maximal activity in the presence of Mg2+ (pH 7.5, 40 degrees), is unstable and completely inactivated within 6 hrs at 25 degrees. In the presence of Mg2+ monovalent cations stimulate the enzyme activity. The molecular weight of pyruvate carboxylase as determined by gel filtration of Sepharose CL-6B is 300,000. The enzyme molecule contains biotin. The apparent Km values for pyruvate, ATP and HCO3- are 1.77, 0.19 and 0.23 mM, respectively. CoASAc, alpha-ketoglutarate and glutamate have no effect on the enzyme activity. The enzyme is inhibited by aspartate, malate, oxaloacetate and is activated by citrate, isocitrate and phosphosugars. The role of pyruvate carboxylase in methylotrophic metabolism of Ps. oleovorans is discussed.
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PMID:[Properties of pyruvate carboxylase of the facultative methylotrope Pseudomonas oleovorans]. 717 45

1. Three experiments were conducted to investigate the relationships between blood pyruvate carboxylase (pyruvate: carbon dioxide ligase (ADP-forming), EC 6.4.1.1; PC) activity, growth performance and dietary biotin level in broilers under different husbandry conditions. Blood PC activity was also used to gain information on the ingestion of biotin faecal origin by birds housed on wood shavings and the effect of steam-pelleting on the biotin content of diets. 2. Blood PC activity and relationship to dietary biotin level were similar in birds kept under different husbandry conditions. 3. Biotin requirement for growth was higher in birds kept under conditions that allowed them to reach their growth potential more fully. 4. The contribution of biotin of faecal origin to the biotin intake of birds housed on wood shavings was negligible at 3 weeks of age but by 7 weeks was equivalent to approximately 0.01 mg/kg diet. 5. Steam-pelleting did not affect the stability or availability of biotin of natural or synthetic origin in diets. 6. It is concluded that blood PC activity is a good criterion of biotin status and requirement in fast-growing broilers.
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PMID:Biotin status, blood pyruvate carboxylase (EC 6.4.1.1) activity and performance in broilers under different conditions of bird husbandry and diet processing. 741 95

The arylhydrocarbon receptor (AhR) plays a central role in mediating 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) toxicity in animals. The investigations described here provide evidence that support a role for the AhR in TCDD-mediated pyruvate carboxylase (PC) level/activity reductions in mice. Pyruvate carboxylase plays a pivotal role in gluconeogenesis and in supplying carbon units for the citric acid cycle. Delivered ip in a corn oil carrier, TCDD suppresses PC activity/amount at doses as low as 1 microgram/kg in responsive C57BL/6J(Ahb/b) mice. Corn oil alone injected ip into mice at 4 mL/kg appears to be an inducer that increases the amount and activity of PC. However, TCDD suppresses this induction. In the Ahb/b mouse, PC levels and activity are reduced to 10% of control values at a dose of 75 micrograms/kg. A time-course experiment shows that the PC reductions are apparent within 16 hours post-TCDD exposure. Here we report investigations on the PC/TCDD response using a congenic C57BL/6J(Ahd/d) mouse strain having an AhR with a low affinity for TCDD. If the PC/TCDD response is AhR mediated, the congenic mouse strain (Ahd/d) would require much higher doses of TCDD to suppress PC. In the Ahd/d mice, we observe that an approximately 60-fold increase in TCDD dose is necessary to produce a PC/TCDD effect. We also find that in Ahd/d mice, corn oil does not induce an increase in PC activity/amounts, as reported for Ahb/b mice.
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PMID:Ah receptor involvement in mediation of pyruvate carboxylase levels and activity in mice given 2,3,7,8-tetrachlorodibenzo-p-dioxin. 756 52

Pyruvate carboxylase (PC) was purified to homogeneity from an overexpressing strain of the purple photosynthetic bacterium Rhodobacter capsulatus using a rapid dye-ligand affinity chromatography procedure, in which dye-bound enzyme was specifically eluted with a low concentration of acetyl-CoA, an allosteric activator of the enzyme. The enzyme purified by this method was obtained in 75% yield with a specific activity of 40 U (mg protein)-1. In contrast, affinity chromatography on a monomeric avidin column, commonly used in the purification of biotin-containing carboxylases, resulted in a yield of < 40%, with a specific activity of 10 U (mg protein)-1. The enzyme purified by the dye-linked procedure had a subunit molecular mass of 140,000 Da and was absolutely dependent on acetyl-CoA for activity. Acetyl-CoA was also effective in protecting the enzyme from thermal denaturation. The enzyme was inhibited by 2-oxoglutarate and, to a lesser extent, L-aspartate, with sigmoidal kinetics with respect to acetyl-CoA concentration. The amino acid composition, pH optimum and kinetic constants for pyruvate, ATP and bicarbonate were determined. An N-terminal sequence of 26 residues was obtained, which was homologous to the N-terminal regions of several eukaryotic PCs, propionyl-CoA carboxylases and acetyl-CoA carboxylase.
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PMID:Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: rapid and efficient purification using dye-ligand affinity chromatography. 758 22


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