Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of five mitochondrial enzymes tested in liver from patients with Reye's syndrome were measured. Citrate synthase, glutamic dehydrogenase, succinic dehydrogenase, pyruvate carboxylase, and pyruvate dehydrogenase were all outside of the range shown by control samples and well below them in activity. The activity of two extramitochondrial enzymes, glucose-6-phosphatase, which is a microsomal enzyme, and fructose-1,6-diphosphatase, which is a soluble enzyme, were in the normal range in samples from Reye's syndrome patients. In both muscle and brain the activities of the mitochondrial enzyme, citrate synthase, glutamic dehydrogenase, and succinic dehydrogenase were all within the control range. Pyruvate dehydrogenase was found to be normal in muscle from these patients.
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PMID:Reye's syndrome: preservation of mitochondrial enzymes in brain and muscle compared with liver. 21 43

Activities of the 4 hepatic gluconeogenic enzymes: glucose-6-phosphatase, fructose-1,6-diphosphatase, pyruvate carboxylase, particulate and cytosolic phosphoenolpyruvate carboxykinase (PEPCK) have been measured in fetal rabbits (22, 25, 28, 30 and 31 days of gestation) and in fasted or suckling newborns (1 and 2 days after birth). Between days 25 and 31 of gestation, fructose 1,6-diphosphatase and particulate PEPCK activities represent 50% of adult (pregnant female) activities, while pyruvate carboxylase is present at adult values during the same period. Glucose-6-phosphatase is low and cytosolic PEPCK absent in fetal liver until 30 days of gestation and increase significantly during the day preceding birth. Al the enzymes show a further increase after birth independently of the nutritional status of the animals (starved or suckling).
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PMID:Perinatal development of glucoeneogenic enzymes in rabbit liver. 22 57

The effect of fasting and fasting and refeeding on hepatic and renal gluconeogenic enzyme activities were studied in six-week-old chickens (Gallus domesticus: New Hampshire male x Columbian female). Hepatic pyruvate carboxylase appeared not to be affected by fasting, but the renal enzyme activity increased in four-day fasted chickens. The hepatic mitochondrial and cytosolic phosphoenolpyruvate carboxykinases were essentially not affected by fasting. The renal mitochondrial phosphoenolpyruvate carboxykinase showed a slight increase in activity only after a four-day fast, but the cytosolic enzyme activity increased markedly already after a two-day fast. Also the activities of the hepatic and renal fructose-1,6-diphosphatase and glucose-6-phosphatase increased markedly on fasting. Refeeding for four days after a four-day fast returned these enzyme activities to near control values.
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PMID:Effect of fasting and fasting and refeeding on hepatic and renal gluconeogenic enzymes in the chicken. 22 47

The activities of the key gluconeogenic, glycolytic, and pentose-shunt enzymes in chicken kidney were determined starting from 8 days before to 58 days after hatching. The activities of pyruvate carboxylase (PC), mitochondrial and cytosolic phosphoenolypruvate carboxykinase (PEPCK), fructose-1,6-diphosphatase (FDPase) and glucose-6-phosphatase (G6Pase) were low in the embryonic tissue but increased towards the time of hatching. After hatching, the activities of PC, mitochondrial PEPCK, and G6Pase continued to increase, but those of FDPase and cytosolic PEPCK decreased. Relatively little change in these activities was observed in chickens over 24 days old. The activities of hexokinase (HK), phosphofructokinase (PFK), pyruvate kinase (PK), and lactate dehydrogenase (LDH) increased during embryonic growth. After hatching, HK activity continued to increase and then decrease, whereas PFK appeared to decrease and then increase to prehatch levels in 28-day-old birds. LDH activity continued to increase until 8 days after hatching and remained constant thereafter. No definite pattern was discernible in the case of PK. As for the pentose-shunt enzymes, there was no significant change in glucose-6-phosphate dehydrogenase activity (G6PDH), but the activity of 6-phosphogluconate dehydrogenase (6PGDH) increased until the chickens were 14 days old and then remained relatively constant.
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PMID:Development of gluconeogenic, glycolytic, and pentose-shunt enzymes in the chicken kidney. 22 78

The intracellular distribution of hepatic and renal gluconeogenic enzymes in 20-day-old chicken embryos and 4-week-old chickens (Gallus domesticus: New Hampshire male X Columbian female) has been studied. Pyruvate carboxylase, fructose-1,6-diphosphatase, and glucose-6-phosphatase were found primarily in the mitochondrial, cytosolic, and microsomal fractions, respectively. Phosphenolpyruvate carboxykinase was present not only in the mitochondria but also in the cytosol of the chicken liver and the kidney. The intracellular distribution of the liver enzyme differed from that of the kidney enzyme in chicken embryos as well as in growing chickens.
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PMID:Intracellular distribution of hepatic and renal gluconeogenic enzymes in embryonic and growing chickens. 23 Apr 68

Intrauterine growth retardation was induced in rats by ligation of the artery of one of both uterine horns. Activities of pyruvate carboxylase, phosphoenolpyruvate carboxykinase, fructose-1,6-diphosphatase and glucose-6-phosphatase in liver were measured at 0, 1, 3 and 6 h after delivery in newborn rats from normal and sham-operated litters, and from ligated and contralateral uterine horns. Lower activities of fructose-1,6-diphosphatase were found in small-for-gestational-age animals in comparison with animals from contralateral horns. When small-for-gestational-age animals were compared with animals from sham litters (which could be regarded as more satisfactory controls), the activities of two other gluconeogenic enzymes (pyruvate carboxylase and glucose-6-phosphatase) appeared to be lower as well. It is concluded that a delay in the development of these gluconeogenic enzymes could play a role in neonatal hypoglycemia in small-for-gestational-age rats.
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PMID:Gluconeogenic key enzymes in normal and intrauterine growth-retarded newborn rats. 23 14

1. The metabolic response of livers to perfusion with ethanol with and without avenaciolide, has been followed by measuring the perfusate levels of glucose, lactate, pyruvate, beta-hydroxybutyrate, ethanol, amino acids, urea and lipid. 2. Analysis of the perfused livers showed changes in the activities of some of the key enzymes of glycolysis, gluconeogenesis and lipogenesis. Ethanol perfusion decreased the levels of phosphofructokinase, glucokinase and cytosolic isocitrate dehydrogenase, while avenaciolide lowered pyruvate carboxylase and phosphoenolpyruvate carboxykinase as well as glucokinase. Isocitrate dehydrogenase and phosphofructokinase were unchanged, but the ionophore increased the level of fructose-1,6-diphosphatase. Ethanol plus avenaciolide showed the same pattern as ethanol alone, together with the decrease in phosphoenolpyruvate carboxykinase found with avenaciolide. 3. Neither ethanol nor avenaciolide had any effect on kexokinase, pyruvate kinase or acetyl-CoA carboxylase. There were small changes in glucose-6-phosphatase and malic enzyme, and a tendency for citrate lyase levels to decline in avenaciolide perfusions.
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PMID:The actions of avenaciolide and ethanol on glucose metabolism and on related enzyme activities in the isolated perfused rat liver. 94 10

Human blood platelets contain no detectable activity of the enzymes fructose diphosphatase (EC 3.1.3.11), phospho-enolpyruvate carboxykinase (EC 4.1.1.32) and pyruvate carboxylase (EC 6.4.1.1.). Glucose-6-phosphatase (EC 3.1.3.9) activity is very low. Phosphofructokinase present in human blood platelets, catalyzes a reaction which can be stimulated by AMP in a platelet homogenate, due to the presence of endogenous ADP and myokinase. These enzymes are responsible for the formation of fructose-6-phosphate from fructose-1, 6-diphosphate. Pyruvate kinase (EC 2.7.1.40) in human blood platelets belongs to the M-type, which is not inhibited by ATP, at least not under the conditions applied. The results obtained indicate that gluconeogenesis in human blood platelets is not present in the way which has been established for liver and kidney.
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PMID:Insignificance of gluconeogenesis in human blood platelets. 112 26

The activities of glucose-6-phosphatase (G6Pase), fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK) and pyruvate carboxylase (PC) were determined in homogenates of adult Schistosoma mansoni worms and compared with the activities in homogenates of rat liver and rat skeletal muscle, tissues with a high and a low gluconeogenic capacity, respectively. All four gluconeogenic enzymes were present in S. mansoni. The enzymes were less active than in rat liver, but the activities of G6Pase, PEPCK and PC were at least an order of magnitude higher than in rat skeletal muscle whereas FBPase was approximately equally active in S. mansoni and in rat muscle. Experiments with 14C-labelled substrates or [14C]NaHCO3 failed to demonstrate the actual occurrence of gluconeogenesis in S. mansoni. Some possible other functions of the gluconeogenic enzymes were investigated. Experiments with inhibitors of PEPCK gave no indications that this enzyme was involved in the degradation of glucose. This was confirmed by 13C-NMR experiments which indicated that lactate was formed from phosphoenolpyruvate via the actions of pyruvate kinase and lactate dehydrogenase, and that PEPCK did not participate in the formation of lactate. Substrate cycling between fructose-6-dehydrogenase, and fructose-1,6-bisphosphate was demonstrated to occur in adult S. mansoni. This shows that FBPase participates in the glucose metabolism of this parasite.
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PMID:The enigmatic presence of all gluconeogenic enzymes in Schistosoma mansoni adults. 164 28

Male Sprague-Dawley rats (240-245 g) were dosed ip with 5, 15, 25, or 125 micrograms/kg -,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in corn oil. Ad libitum-fed and pair-fed controls received vehicle (4 ml/kg) alone. Two or 8 days after dosing five rats of each group were sacrificed, their livers removed and assayed for the activities of three gluconeogenic enzymes [phosphoenol-pyruvate carboxykinase (PEPCK; EC 4.1.1.32), pyruvate carboxylase (PC; EC 6.4.1.1), and glucose-6-phosphatase (G-6-Pase, EC 3.13.9)], and one glycolytic enzyme [pyruvate kinase (PK; EC 2.7.1.40)] by established procedures. The activity of PK was not affected by TCDD at either time point. The activity of G-6-Pase tended to be decreased in TCDD-treated animals, as compared to pair-fed controls, but the decrease was variable without an apparent dose-response. The activity of PEPCK was significantly decreased 2 days after dosing, but a clear dose-response was apparent only at the 8-day time point. Maximum loss of activity at the highest dose was 56% below pair-fed control levels. PC activity was slightly decreased 2 days after TCDD treatment and displayed statistically significant, dose-dependent reduction by 8 days after dosing with a 49% loss of enzyme activity after the highest dose. It is concluded that inhibition of gluconeogenesis by TCDD previously demonstrated in vivo is probably due to decreased activities of PEPCK and PC. The data also support the prevailing view that PEPCK and PC are rate-determining enzymes in gluconeogenesis.
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PMID:Key enzymes of gluconeogenesis are dose-dependently reduced in 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)-treated rats. 205 51


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