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:4.1.1.32 (phosphoenolpyruvate carboxykinase)
4,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Phosphopyruvate carboxylase activity rapidly appears in the liver of prematurely delivered rats and development of activity is prevented by injection of actinomycin D just before delivery. 2. The activity is considerably decreased by puromycin and amino acid analogues and thus appears to be due to enzyme synthesis. 3. Newborn or premature animals show a transient intense phase of hypoglycaemia after delivery. 4. When the hypoglycaemic phase is prevented by glucose injection little phosphopyruvate carboxylase activity appears in the liver, but galactose, mannose and fructose, which have no effect on the blood glucose concentration, also repress enzyme development. 5. Lactate, pyruvate and glycerol injections repress the premature development of phosphopyruvate carboxylase. 6. Injections of glucagon, adrenalin and noradrenalin into the rat foetus in utero result in development of phosphopyruvate carboxylase activity. 7. These findings are discussed in relation to the mechanism of initiation of enzyme synthesis in neonatal rat liver.
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PMID:Factors affecting the premature induction of phosphopyruvate carboxylase in neonatal rat liver. 566 96

Evidence is presented for the occurrence of glycosomes (organelles resembling peroxisomes) in four major species of Leishmania (viz. L. major, L.m. mexicana, L. b. braziliensis and L. donovani), based on latency as well as differential and isopycnic centrifugation studies. The enzymes involved in glycolysis; (hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase); glycerol metabolism (sn-glycerol-3-phosphate dehydrogenase and glycerol kinase); carbon dioxide fixation (phosphoenolpyruvate carboxykinase and possibly malate dehydrogenase); together with an enzyme involved in the beta-oxidation of fatty acids (3-beta-hydroxybutyryl coenzyme A dehydrogenase); a key enzyme in the synthesis of ether lipids (dihydroxyacetone phosphate acyltransferase) as well as the ADP utilising enzyme adenylate kinase, were all found associated, at least in part, with a subcellular organelle which had a buoyant density in sucrose gradients of 1.21 to 1.24 g cm-3. Little variance in enzyme composition was found between the different species of Leishmania or in comparison with other members of the Trypanosomatidae, supporting the unifying principle that glycosomes are a unique characteristic of this family. The occurrence of important catabolic, anabolic and anaplerotic pathways in the glycosomes of Leishmania renders them prime targets for chemotherapy.
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PMID:The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species. 644 18

Metabolic rates and adenine nucleotide content of liver and kidney from hibernating ground squirrels were measured and compared to rats to study the biochemical adaptation to hibernation. High rates of renal and hepatic gluconeogenesis were observed in squirrels, particularly from propionate and glycerol compared to rat. During hibernation and starvation soluble phosphoenolpyruvate carboxykinase activity was increased in both liver and kidney. Although metabolic rates are decreased during hibernation the results suggest that the enzymic complement is maintained at high activity even during torpor.
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PMID:Effect of hibernation on liver and kidney metabolism in 13-lined ground squirrels. 650 11

3- Aminopicolinate , a hyperglycemic agent that activates purified phosphoenolpyruvate carboxykinase in the presence of Fe2+, inhibits glucose synthesis from lactate, pyruvate, asparagine, monomethyl succinate, or glutamine but does not affect that from fructose, dihydroxyacetone, sorbitol, or glycerol in hepatocytes isolated from rats fasted for 24 h. Lactate production from monomethyl succinate by hepatocytes is also inhibited by 3- aminopicolinate . This compound elevates the concentrations of pyruvate, malate, and aspartate but decreases that of phosphoenolpyruvate in hepatocytes incubated with lactate plus pyruvate. In rats, the ability of 3- aminopicolinate to elevate blood glucose concentration is unimpaired by renalectomy . The drug does not significantly affect glycemia in functionally hepatectomized rats but accelerates blood lactate and pyruvate accumulation to higher maximum concentrations even when kidney function is also ablated. It is concluded that 3- aminopicolinate inhibits phosphoenolpyruvate carboxykinase in hepatocytes, that the reported stimulation of renal glutaminase and glutamine gluconeogenesis by this compound does not contribute significantly to its hyperglycemic property, and that the drug increases gluconeogenic substrate supply from peripheral tissues.
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PMID:3-Aminopicolinate inhibits phosphoenolpyruvate carboxykinase in hepatocytes and increases release of gluconeogenic precursors from peripheral tissues. 672 75

A mutant of Saccharomyces cerevisiae lacking phosphoenolpyruvate carboxykinase (E.C. 4.1.1.32) was isolated. The mutant did not grow on gluconeogenic sources except glycerol. The mutation was recessive and apparently affected the structural gene of the enzyme. Intracellular levels of metabolites related to the metabolic situation of the enzyme were not significantly affected after transfer of the mutant from a medium with glycerol to a medium with ethanol as carbon source. In these conditions only AMP decreased 3 to 5 times. A search for mutants affected in the other gluconeogenic enzyme, fructose 1,6 bisphosphatase, remained unsuccessful.
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PMID:Isolation and characterization of a mutant of Saccharomyces cerevisiae defective in phosphoenolpyruvate carboxykinase. 675 Dec 58

Intracellular concentrations of phosphoenolpyruvate (PEP) and five kinds of allosteric effectors (acetyl-CoA, fructose 1,6-bisphosphate, GTP, L-aspartate, and L-malate) of PEP carboxylase were measured in E. coli cells grown on various compounds as a carbon source. Based on the data obtained, reaction systems which contained a definite concentration of the enzyme and the ligands at the concentrations found in vivo were constructed and the enzyme activities were measured. The ratio of each activity thus obtained to the maximal activity attainable with the same concentration of enzyme and saturating concentrations of the activators was estimated. For the cells grown on glucose, glycerol, or lactate, the extent of exhibition of the enzyme activity was 2-15% of the maximal activity. For the cells grown on acetate or oleate, the extent was 1-3%. For the cells grown on succinate, L-aspartate, L-malate, or glucose plus L-aspartate, the extent was less than 0.4%. Consideration of the data obtained in the present studies, together with those obtained in our previous studies on the enzyme level (Teraoka, H. et al. (1970) J. Biochem. 67, 567-575), showed that the control of the enzyme reaction in vivo is considerably different from that expected from the in vitro experiments, and that deficiencies of "coarse control" are covered by a "fine control."
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PMID:Regulation of Escherichia coli phosphoenolpyruvate carboxylase by multiple effectors in vivo. Estimation of the activities in the cells grown on various compounds. 698 14

Treponema pallidum was observed to incorporate glucose carbons into lipids, ribonucleic acid, deoxyribonucleic acid, and protein. Only the glycerol portions of phosphatidylcholine and phosphatidylglycerol contained glucose-derived carbons. Incorporation of exogenous choline into phosphatidylcholine was detected. Glucose was incorporated into only the pentoses of nucleic acids. About 50% of the glucose incorporated into protein was present in only one amino acid, aspartate. Evidence suggests that aspartate synthesis could follow the conversion of phosphoenolpyruvate to oxalacetic acid by a guanosine 5'-diphosphate-dependent phosphoenolpyruvate carboxykinase.
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PMID:Distribution of glucose incorporated into macromolecular material by treponema pallidum. 701 54

The gluconeogenesis in the kidney in vivo in fed rats was studied by measuring the rate of synthesis of 14C-labeled blood glucose derived from 14C-labeled substrates injected into functionally hepatectomized rats. Among the substrates for the gluconeogenesis in the kidney examined, the most effective substrates were lactate, glycerol, pyruvate and glutamine, whose contributions to the renal gluconeogenesis were 54.0%, 26.5%, 4.1%, and 5.5% at 2:00 a.m., when the activity of phosphoenolpyruvate carboxykinase [EC 4.1.1.32] was highest, and 50.0%, 31.0%, 5.3%, and 3.2% at 2:00 pm., when it was lowest. These findings showed that there was no significant daily change in the total renal gluconeogenesis. Based on these data, we propose as a working hypothesis that a major function of the renal gluconeogenesis, utilizing lactate, glycerol, pyruvate, and glutamine as preferred substrates, is to meet the constant minimum requirement for blood glucose in the brain.
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PMID:Gluconeogenesis in the kidney in vivo in fed rats. Circadian change and substrate specificity. 707 47

The effects of 3-mercaptopicolinic acid, an inhibitor of phosphoenolpyruvate carboxykinase, were studied in bovine subcutaneous adipose tissue slices in vitro. Lactate and glucose stimulated the incorporation of [U-14C]acetate into total lipids and nonesterified fatty acids. 3-Mercaptopicolinic acid abolished the stimulatory effect of lactate on total synthesis but had no effect on that from glucose. The inhibitor decreased glyceride-glycerol and glyceride-fatty acid synthesis from L-[U-14C]lactate by 90 and 30%, respectively; glyceride-glycerol synthesis from D-[U-14C]glucose was refractory to inhibition by 3-mercaptopicolinic acid, whereas the inhibitor tended to increase glyceride-fatty acid synthesis from glucose. The presence of lactate plus glucose in the incubation media elicited a greater than additive stimulation of acetate incorporation into total lipids. Glucose doubled the incorporation of lactate into glyceride-fatty acids, but had no effect on the net incorporation of lactate into nonesterified fatty acids. Lactate, but not glucose, stimulated the incorporation of [1-14C]palmitate into glyceride-fatty acids; 3-mercaptopicolinic acid increased this rate for all substrate combinations studied, although this was opposite to expected results. As determined with 3H2O, lactate and glucose stimulated the synthesis of total lipids, and 3-mercaptopicolinic acid decreased the stimulatory effects of lactate and glucose on 3H2O incorporation. The results suggest that lactate, and possibly glucose, stimulate the incorporation of acetate into fatty acids by increasing the availability of alpha-glycerophosphate.
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PMID:The effect of 3-mercaptopicolinic acid and substrate interactions on the incorporation of lipogenic precursors into glyceride-glycerol, glyceride-fatty acids and nonesterified fatty acids in bovine adipose tissue. 712 10

To study the interrelationships of phosphoenolpyruvate carboxykinase and glyceroneogenesis in adipose tissue, investigations with two effectors of the hepatic carboxykinase, Fe2+ and Mn2+, and two inhibitors of the enzyme and of gluconeogenesis in liver, quinolinic acid and 3-mercaptopicolinic acid, were carried out. Incubating adipose tissue cytosol with 30 microM Fe2+ or 100 microM Mn2+ prior to assaying for phosphoenolpyruvate carboxykinase activity doubled the enzyme activity. Inhibition of the enzyme by quinolinate alone was minimal. Adding 30 microM Fe2+ to the cytosol decreased the K0.5 (concentration that gives 50% inhibition) for quinolinate to 0.4 mM and the K0.5 for mercaptopicolinate from 200 to 14 microM. Activating the enzyme with 100 microM Mn2+ did not lower the K0.5 values and adding 500 microM Mn2+ to the cytosol completely interfered with the enhancement of inhibition induced by Fe2+. Each inhibitor interfered with 14C incorporation into glyceride glycerol from labeled pyruvate, alanine and lactate in suspensions of adipocytes. Adding 1 mM Mn2+ to the adipocyte suspension almost completely prevented the inhibition of pyruvate and alanine incorporation into glyceride glycerol, but adding the Mn2+ or 250 microM Fe2+ to the adipocytes in the absence of inhibitors did not enhance glyceride glycerol formation. Adding 250 microM Fe2+ to the adipocytes did not enhance inhibition of lipid synthesis by mercaptopicolinate or quinolinate. Mercaptopicolinate did not inhibit glyceride glycerol, fatty acid, total lipid or CO2 production from glucose. The lack of activation of glyceride glycerol synthesis by added Fe2+ or Mn2+, the lack of enhancement of pyridine carboxylate inhibition by Fe2+ and the interference with inhibition by Mn2+ are compatible with the idea that a transition metal ion similar to Fe2+, if not Fe2+ itself, is available to, or loosely bound to, the adipose tissue carboxykinase in vivo. Taken together with the results of previous work which showed ferroactivator (a cytosol protein necessary for Fe2+ activation of the carboxykinase) to be present in adipose tissue, the present results indicate that the control of the adipose tissue carboxykinase may be similar to the enzyme in liver. Fatty acid synthesis was also diminished by the inhibitors, albeit to a lesser extent than was glyceride glycerol formation. It is hypothesized that this was secondary to decreased esterification caused by the lack of glycerol 3-phosphate from inhibition of the carboxykinase. Decreased esterification would lead to a build-up of fatty acyl CoA which inhibits fatty acid synthesis.
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PMID:Inhibition of phosphoenolpyruvate carboxykinase, glyceroneogenesis and fatty acid synthesis in rat adipose tissue by quinolinate and 3-mercaptopicolinate. 721 68


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