Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.32 (phosphoenolpyruvate carboxykinase)
 4,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phosphoenolpyruvate carboxylase (orthophosphate:oxaloacetate carboxylase (phosphorylating), EC 4.1.1.31) from plant cells of soybean nodules was studied to assess its role in providing carbon skeletons for aspartate and asparagine synthesis. The enzyme was purified 119-fold by (NH4)2SO4 fractionation and DEAE-cellulose, BioGel A-1.5m, and hydroxyapatite chromatography. Five activity bands were resolved with discontinuous polyacrylamide gel electrophoresis. A small quantity of enzyme from the most active band was separated from the others by preparative electrophoresis. The apparent Michaelis constants of this enzyme for phosphoenolpyruvate and HCO3- were 9.4.10(-2) and 4.1.10(-1) mM, respectively. A series of metabolite tested at 1 mM had no significant effect on enzyme activity. These experiments indicate that the major factors directly controlling phosphoenolpyruvate carboxylase activity in vivo are phosphoenolpypyruvate and HCO3- concentrations.
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PMID:Phosphoenolpyruvate carboxylase from soybean nodule cytosol. Evidence for isoenzymes and kinetics of the most active component. 57 39

Changes in mitochondrial and sarcoplasmic proteins using proteinomics and Western blotting in hearts from copper-deficient rats were explored in this study. Also, key enzymes that are involved in cardiac energy metabolism via glycolysis and fatty acid oxidation and related transcription factors were determined. Rats were fed one of two diets: a copper-adequate diet containing 6 mg Cu/kg diet or a diet with less than 1 mg Cu/kg diet for 5 weeks. Copper deficiency was confirmed by low liver copper levels, decreased hematocrit levels and cardiac hypertrophy. Proteinomic data revealed that of the more than 50 proteins identified from the mitochondrial fraction of heart tissue, six were significantly down-regulated and nine were up-regulated. The proteins that were decreased were beta enolase 3, carbonic anhydrase 2, aldose reductase 1, glutathione peroxidase, muscle creatine kinase and mitochondrial aconitase 2. The proteins that were up-regulated were isocitrate dehydrogenase, dihydrolipoamide dehydrogenase, transferrin, subunit d of ATP synthase, transthyretin, preproapolipoprotein A-1, GRP 75, alpha-B crystalline and heat shock protein alpha. Follow-up Western blots on rate-limiting enzymes in glycolysis (phosphofructose kinase), fatty acid oxidation (medium chain acyl dehydrogenase, peroxisome proliferator-actvator receptor-alpha or PPARalpha) and gluconeogenesis (phosphoenolpyruvate carboxykinase) did not reveal changes in metabolic enzymes. However, a significant increase in peroxisome proliferator-activated receptor-gamma coactivator (PGC)-1alpha protein, as well as the transcript, which increased 2.5-fold, was observed. It would appear that increased mitochondrial biogenesis known to occur in copper deficiency hearts is caused by an increased expression in the master regulator of mitochondrial biogenesis, PGC-1alpha.
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PMID:Mitochondrial and sarcoplasmic protein changes in hearts from copper-deficient rats: up-regulation of PGC-1alpha transcript and protein as a cause for mitochondrial biogenesis in copper deficiency. 1899 53