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PubMed1992

A novel mutation FruS, altering synthesis of components of the phosphoenolpyruvate: fructose phosphotransferase system in Escherichia coli K12.

A novel mutation, FruS localised in the fru operon was obtained. It uncouples expression of the genes determining synthesis of the fructose-specific transport proteins and fructose-1-phosphate kinase. In FruS bacteria the fruA and fruF genes (coding for Enzyme IIfru and FPr, respectively) are constitutive by expressed while fruK (encoding fructose-1-phosphate kinase) remains inducible. In contrast to other mutations, which render expression of the whole fru operon constitutive, the FruS mutation: (1) does not lead to D-xylitol sensitivity; (2) does not inhibit growth on D-lactate, pyruvate and L-alanine; (3) does not decrease phosphoenolpyruvate (PEP) synthase activity.

Alanine↗
PubMed1996

Enzymes of carbohydrate metabolism in young and adult rats fed diets differing in fat and carbohydrate.

Glycogen content as well as glycolytic, gluconeogenic and fatty acid synthesis enzyme activities were monitored in young and adult male rats fed diets differing in fat content: 11% (low), 22% (medium) and 42% (high) of total energy from fat. The results showed significant differences in the responses of young and adult rats to changes in dietary fat and carbohydrate. In young animals, increasing dietary fat decreased total liver glycogen phosphorylase (GP), pyruvate kinase (PK), glycerol 3-phosphate dehydrogenase, glucose 6-phosphate dehydrogenase, malic enzyme (ME), ATP-citrate lyase (ATP-CL) and fatty acid synthase (FAS). Increasing dietary fat also affected enzyme levels in other tissues: hexokinase (HK) and pyruvate dehydrogenase (PDH) activities decreased whereas skeletal muscle PK activity increased. The pattern of enzyme changes was similar in livers of fed adults with the exception that liver GP was not affected by dietary manipulations. Overnight food deprivation decreased liver glucokinase (GK), ME, ATP-CL, and FAS activities and increased liver phosphoenolpyruvate carboxykinase (PEPCK) and phosphofructokinase in both young and adult animals. In young animals, food deprivation also: (i) reduced liver GK and PK, (ii) increased kidney PEPCK, (iii) decreased muscle PEPCK and (iv) decreased kidney PDH. Food-deprived adults had increased skeletal muscle PEPCK and kidney glycogen synthetase as well as decreased kidney PEPCK muscle GP activity. These differences suggest that young animals are somewhat more responsive to changes in dietary manipulations. They also show that overnight food restriction causes a more profound metabolic re-organization in younger than in older animals.

Age Factors↗
PubMed2004

Relationships between maximal muscle oxidative capacity and blood lactate removal after supramaximal exercise and fatigue indexes in humans.

The present study investigated whether blood lactate removal after supramaximal exercise and fatigue indexes measured during continuous and intermittent supramaximal exercises are related to the maximal muscle oxidative capacity in humans with different training status. Lactate recovery curves were obtained after a 1-min all-out exercise. A biexponential time function was then used to determine the velocity constant of the slow phase (gamma(2)), which denoted the blood lactate removal ability. Fatigue indexes were calculated during all-out (FI(AO)) and repeated 10-s cycling sprints (FI(Sprint)). Biopsies were taken from the vastus lateralis muscle, and maximal ADP-stimulated mitochondrial respiration (V(max)) was evaluated in an oxygraph cell on saponin-permeabilized muscle fibers with pyruvate + malate and glutamate + malate as substrates. Significant relationships were found between gamma(2) and pyruvate + malate V(max) (r = 0.60, P < 0.05), gamma(2) and glutamate + malate V(max) (r = 0.66, P < 0.01), and gamma(2) and citrate synthase activity (r = 0.76, P < 0.01). In addition, gamma(2), glutamate + malate V(max), and pyruvate + malate V(max) were related to FI(AO) (gamma(2) - FI(AO): r = 0.85; P < 0.01; glutamate + malate V(max) - FI(AO): r = 0.70, P < 0.01; and pyruvate + malate V(max) - FI(AO): r = 0.63, P < 0.01) and FI(Sprint) (gamma(2) - FI(Sprint): r = 0.74, P < 0.01; glutamate + malate V(max) - FI(Sprint): r = 0.64, P < 0.01; and pyruvate + malate V(max) - FI(Sprint): r = 0.46, P < 0.01). In conclusion, these results suggested that the maximal muscle oxidative capacity was related to blood lactate removal ability after a 1-min all-out test. Moreover, maximal muscle oxidative capacity and blood lactate removal ability were associated with the delay in the fatigue observed during continuous and intermittent supramaximal exercises in well-trained subjects.

Adult↗
PubMed1968

The assimilation of carbon by Chloropseudomonas ethylicum.

1. The enzymes in ultrasonically prepared extracts of Chloropseudomonas ethylicum were studied to elucidate how this organism assimilates acetate and carbon dioxide and why it cannot grow with either of these two compounds alone. 2. Such extracts can (i) convert acetate and oxaloacetate into alpha-oxoglutarate, (ii) convert oxaloacetate into succinyl-CoA, (iii) convert phosphopyruvate into 3-phosphoglyceraldehyde and (iv) interconvert phosphopyruvate and pyruvate via oxaloacetate. 3. Pyruvate kinase, alpha-oxoglutarate dehydrogenase, ribulose diphosphate carboxylase, isocitrate lyase and malate synthase were not detected. 4. It is difficult to detect aconitate hydratase, fumarate hydratase and citrate synthase in extracts of the organism ultrasonically treated in tris buffer; to demonstrate these enzymes extracts should be prepared in phosphate buffer containing 2-mercaptoethanol. 5. Provided that this organism can synthesize pyruvate from acetate and carbon dioxide, the enzymes detected are sufficient to account for the nutritional requirements of this organism.

Acetates↗
PubMed1986

Regulation of rabbit fetal glycogen: effect of in utero fetal decapitation on the metabolism of glycogen in fetal heart, lung, and liver.

To understand the control mechanisms involved in the regulation of fetal glycogen, we have studied the effect of in utero fetal decapitations on glycogen metabolism in rabbit fetal heart, lung, and liver. In utero fetal decapitations were performed between days 18 and 21 of gestation. Two to four fetuses on one side of the horn were decapitated. Fetuses were delivered between days 23 and 26 or between days 28 and 30 of gestation. Fetal heart, lungs, and liver were analyzed for DNA, protein, glycogen, glycogen synthase (I and D forms), glycogen phosphorylase (a and b forms), phosphofructokinase, pyruvate kinase, and lactic dehydrogenase. In fetal heart and lung, no difference was observed in any of the above measurements in the intact and decapitated fetuses. In contrast, fetal liver does not appear to develop the glycogen system as indicated by the very low levels of glycogen (0.02 mg/mg DNA) in decapitated fetuses as compared with intact fetuses (0.4 mg/mg DNA). Similarly the levels of glycogen synthase and phosphorylase were two to three times lower in livers from decapitated fetuses as compared with the livers from intact fetuses. The three enzymes phosphofructokinase, pyruvate kinase, and lactic dehydrogenase were not affected by fetal decapitation in all three tissues. These results indicate that the fetal hypothalamic-pituitary-adrenal (thyroid) axis is not required at least after day 18 of gestation for the normal accumulation and subsequent utilization of glycogen in fetal heart and lungs, while it is an absolute requirement for the development of the fetal liver glycogen system.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2002

Effects of benfluorex on fatty acid and glucose metabolism in isolated rat hepatocytes: from metabolic fluxes to gene expression.

The effects of benfluorex and two of its metabolites (S 422-1 and S 1475-1) on fatty acid and glucose metabolic fluxes and specific gene expression were studied in hepatocytes isolated from 24-h fasted rats. Both benfluorex and S 422-1 (0.1 or 1 mmol/l) reduced beta-oxidation rates and ketogenesis, whereas S 1475-1 had no effect. At the same concentration, benfluorex and S 422-1 were more efficient in reducing gluconeogenesis from lactate/pyruvate than S 1475-1. Benfluorex inhibited gluconeogenesis at the level of pyruvate carboxylase (45% fall in acetyl-CoA concentration) and of glyceraldehyde-3-phosphate dehydrogenase (decrease in ATP/ADP and NAD(+)/NADH ratios). Accordingly, neither benfluorex nor S 422-1 inhibited gluconeogenesis from dihydroxyacetone, but both stimulated gluconeogenesis from glycerol. In hepatocytes cultured in the presence of benfluorex or S 422-1 (10 or 100 micromol/l), the expression of genes encoding enzymes of fatty acid oxidation (carnitine palmitoyltransferase [CPT] I), ketogenesis (hydroxymethylglutaryl-CoA synthase), and gluconeogenesis (glucose-6-phosphatase, PEPCK) was decreased, whereas mRNAs encoding glucokinase and pyruvate kinase were increased. By contrast, Glut-2, acyl-CoA synthetase, and CPT II gene expression was not affected by benfluorex or S 422-1. In conclusion, this work suggests that benfluorex mainly via S 422-1 reduces gluconeogenesis by affecting gene expression and metabolic status of hepatocytes.

Acetyl Coenzyme A↗
PubMed1981

Comparison between developmental and senescent changes in enzyme activities linked to energy metabolism in rat heart.

The developmental and senescent patterns of a number of heart enzyme activities linked to energy metabolism have been studied in rats aged between 4 days and 21 months. A morphometric study of mitochondrial volume fractions and numbers has been also carried out. Developmental changes result in a rise of most mitochondrial enzymes (NADP+-isocitrate dehydrogenase, malic enzyme, succinate dehydrogenase, citrate synthase) and mitochondrial volume fractions. Exceptions are NAD+-isocitrate dehydrogenase, which declines from 4 days onwards, and NAD+-malate dehydrogenase, which declines and then rises over the same period. Senescent changes follow two different trends. While pyruvate kinase and those mitochondrial enzymes lying between citrate formation and isocitrate oxidation (citrate synthase, NADP+-and NAD+-isocitrate dehydrogenases) decline to some degree, mitochondrial succinate dehydrogenase and NAD+-malate dehydrogenase activities increase over the same period. This could point towards a partial impairment of Krebs cycle function, and a reduced energy-producing capacity in the aged rat heart.

Aging↗
PubMed1990

Role of synaptosomal enzymatic alterations and drug treatment in brain aging.

The activity patterns of enzyme linked to energy transduction are measured as an estimate of the energy potential capacity of the brain during aging. Early investigations provided information on age-related modifications in the apparent activity of these enzymes in the brain as a whole without taking into account the anatomical, morphological, and functional heterogeneity of the discrete brain regions, the metabolic compartments, and their different time course of aging processes. These considerations prompted the investigators to focus their efforts on subcellular organelles, representative of metabolic compartments, isolated from selected brain regions. In the present study, to better elucidate the role of the synaptic compartment during aging, the maximum rate (Vmax) of enzymes involved in energy metabolic pathways is evaluated in synaptosomes isolated from the cerebral cortex of rats aged 4, 12, and 24 months. The potential catalytic activity of phosphofructokinase and citrate synthase is not affected by aging. In contrast, the Vmax of pyruvate dehydrogenase and particularly of cytochrome oxidase decreases in aged rats. A marked increase is found in the Vmax of glucose-6-phosphate dehydrogenase in 24-month-old rats and could support the availability of nicotinamide adenine dinucleotide phosphate (NADPH) for antiperoxidative processes. Pretreatments of the animals with certain drugs are performed in order to check the responsiveness of the tissue and the plasticity of enzyme proteins during aging. Papaverine (acting on macrocirculation) is ineffective, but raubasine (acting on microcirculation and metabolism) and almitrine (acting on oxygen availability) both interfere with the potential activity of some of the enzymes tested. Their influence differs with the age of the animal and are in agreement with their action on brain carbohydrate and phospholipid metabolism.

Aging↗
PubMed1993

Inhibition of tryptophan synthase by (1-fluorovinyl)glycine.

Tryptophan synthase (alpha 2 beta 2 complex) from Salmonella typhimurium catalyzes the formation of tryptophan from serine and indole. The enzyme is inactivated by (1-fluorovinyl)glycine. Concomitant with enzyme inactivation, the absorbance at 485 nm increases, indicating covalent modification of pyridoxal 5'-phosphate. It is proposed that inactivation involves elimination of HF to form an allene, which reacts with a nucleophile at the active site. The inactivation reaction involves an alpha,beta-elimination, as does the formation of tryptophan from indole and serine. The inactivation occurs with k(in) > 1.3 s-1, which is very close to k(cat) (6.4 s-1) for the formation of tryptophan from indole and serine. The inactive enzyme (alpha 2 beta 2) regains activity with k(off) = 0.005 min-1. Aminoacetone is formed during reaction, and pyridoxal 5'-phosphate is regenerated. Tryptophan synthase also catalyzes the dehydration of serine, or 3-fluoroalanine, to pyruvate in the absence of indole. This reaction involves an alpha,beta-elimination and the intermediate formation of an aminoacrylate adduct with pyridoxal 5'-phosphate, as does the formation of tryptophan. Pyruvate formation proceeds at less than 5% the rate of tryptophan formation. With [2-2H]serine an isotope effect (DVmax = 1.5) is observed. We propose that pyruvate formation is limited by the rate of hydration of the aminoacrylate intermediate and the rate of the abstraction of the serine alpha-hydrogen.

Acetone↗
PubMed1989

Effect of starvation and insulin in vivo on the activity of the pyruvate dehydrogenase complex in rat skeletal muscles.

The in vivo responses of pyruvate dehydrogenase (PDH) complex to starvation and insulin was assessed in heart, diaphragm and red quadriceps muscle. PDH complex activity was decreased by starvation (3.4-10.2-fold), the magnitude of change depending on muscle type. Insulin increased PDH activity in all muscle types. In fed rats, this effect was relatively small (1.25-1.29-fold). In starved rats there were effects in heart (4.3-fold) and red quadriceps (1.7-fold) but no effect in diaphragm. These results demonstrate that PDH complex in different groups of muscle has different insulin sensitivity (particularly in tissues from starved animals).

Adipose Tissue, Brown↗
PubMed1983

'Insulin-like' effects of lithium ion on isolated rat adipocytes. II. Specific activation of glycogen synthase.

Lithium ion, like insulin, activated adipocyte glycogen synthase with or without glucose in the medium. However, the effect of lithium ion was much greater than that of insulin under both conditions. The lithium-activated glycogen synthase was stable to both Sephadex chromatography and ethanol precipitation of the enzyme, indicating that the effect of lithium ion on glycogen synthase was through covalent modification of the enzyme. Glycogen synthase was significantly activated by lithium ion under conditions where concentrations of cellular ATP were unaffected. The effect of lithium ion on glycogen synthase was rapid and observed at concentrations as low as 1 to 3 mM, reaching a maximum at the concentration of 40 mM. It was thus the most sensitive of all the effects studied (see previous paper). Insulin further stimulated glycogen synthase at low concentrations but not at maximal concentration of lithium ion. Lithium-activated glycogen synthase was inhibited by both epinephrine and dibutyryl cyclic AMP, but was not affected by the removal of extracellular Ca++. Interestingly, lithium ion had no detectable effect on basal pyruvate dehydrogenase as well as on epinephrine-stimulated phosphorylase. The failure of lithium ion to thus mimic insulin actions on pyruvate dehydrogenase and on phosphorylase suggests that the action of lithium ion on glycogen synthase is quite specific and may be mediated by stimulating a phosphatase or by inhibiting a protein kinase acting specifically on glycogen synthase.

Adipose Tissue↗
PubMed1983

Effect of clofibrate feeding on palmitate and branched-chain 2-oxo acid oxidation in rat liver and muscle.

Oxidation rates of palmitate (total and antimycin-insensitive), pyruvate, leucine, 4-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate and activities of two mitochondrial marker enzymes (citrate synthase and cytochrome c oxidase) were assayed in liver and muscle homogenates of fed, clofibrate-treated and 18 hr-starved rats. Significant alterations in the clofibrate-treated and the starved rats were predominantly observed in the liver. Clofibrate feeding increased antimycin-insensitive (peroxisomal) and antimycin-sensitive (mitochondrial) palmitate oxidation and 4-methyl-2-oxopentanoate and pyruvate oxidation in liver. In muscle, only the activities of citrate synthase and cytochrome c oxidase were slightly decreased. Short starvation increased antimycin-sensitive palmitate and 4-methyl-2-oxopentanoate oxidation in liver. The rates of pyruvate and 3-methyl-2-oxobutanoate oxidation were decreased in muscle homogenates. Results suggest that myopathic phenomena observed after chronic clofibrate administration are not related to changes in the capacity of oxidative metabolism of muscle.

Animals↗
PubMed1971

Salmonella locus affecting phosphoenolpyruvate synthase activity identified by a deletion analysis.

Strain leu-4017, derived from Salmonella typhimurium LT2, cannot utilize acetate, pyruvate, or citric acid cycle intermediates as sole sources of carbon. The mutation in this strain extends from the A cistron of the leucine operon to some point between leu and azi, presumably deleting one or more loci involved in the utilization of these compounds. One of these loci is required for phosphoenolpyruvate synthase activity.

Acetates↗
PubMed1971

Regulation at the phosphoenolpyruvate branchpoint in Azotobacter vinelandii: pyruvate kinase.

Pyruvate kinase (EC 2.7.1.40) from Azotobacter vinelandii responds sharply to the adenylate energy charge, with a decrease in activity at high values of charge, as expected for an enzyme of an adenosine triphosphate-regenerating sequence. Glycolytic intermediates, especially glucose 6-phosphate, fructose 6-phosphate, and fructose-1,6-diphosphate, strongly stimulate the reaction and overcome the inhibition caused by high values of energy charge. Thus, the properties of this enzyme depend on interaction between energy charge and the concentrations of hexose phosphates. The properties of pyruvate kinase, together with those of phosphoenolpyruvate carboxylase, aspartokinase, and citrate synthase, seem adapted to provide appropriate partitioning of phosphoenolpyruvate between competing pathways in response to metabolic need.

Adenine Nucleotides↗
PubMed1990

Effect of microgravity on metabolic enzymes of individual muscle fibers.

Eleven enzymes were measured in individual fibers of soleus and tibialis anterior (TA) muscles from two flight and two control (synchronous) animals. There were five enzymes of glycogenolytic metabolism: phosphorylase, glucose-6-phosphate isomerase, glycerol-3-phosphate dehydrogenase, pyruvate kinase, and lactate dehydrogenase (group GLY); five of oxidative metabolism: citrate synthase, malate dehydrogenase, beta-hydroxyacyl-CoA dehydrogenase, 3-ketoacid CoA-transferase, and mitochondrial thiolase (group OX); and hexokinase, subserving both groups. Fiber size (dry weight per unit length) was reduced about 35% in both muscles. On a dry weight basis, hexokinase levels were increased 100% or more in flight fibers from both soleus and TA. Group OX enzymes increased 56-193% in TA without significant change in soleus. Group GLY enzymes increased an average of 28% in soleus fibers but underwent, if anything, a modest decrease (20%) in TA fibers. These changes in composition of TA fibers were those anticipated for a conversion of about half of the originally predominant fast glycolytic fibers into fast oxidative glycolytic fibers. Calculation on the basis of fiber length, rather than dry weight, gave an estimate of absolute enzyme changes: hexokinase was still calculated to have increased in both soleus and TA fibers, but only by 50 and 25%, respectively. Three of the OX enzymes were, on this basis, unchanged in TA fibers, but 3-ketoacid CoA-transferase and thiolase had still nearly doubled, whereas TA GLY enzymes had fallen about 40%. In soleus fibers, absolute levels of OX enzymes had decreased an average of 25% and GLY enzymes were marginally decreased.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1991

Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates.

The flux control distribution of the net rate of state 3 respiration was determined in heart and kidney mitochondria incubated with low concentrations of pyruvate (0.5 mM) or 2-oxoglutarate (1 mM), and in conditions that led to activation of NAD-linked dehydrogenases, i.e., high substrate or Ca2+ concentrations. Control of flux was exerted by the ATP/ADP carrier (flux control coefficient, ci = 0.37) and Site 1 of the respiratory chain (ci = 0.28) when dehydrogenase activity was low. Control of the process shifted to the ATP synthase (ci = 0.32) and the Pi carrier (Ci = 0.27) when dehydrogenases were activated by high pyruvate and high Ca2+. The changes in the control exerted by the ATP/ADP carrier and the ATP synthase were not due to changes in the transmembrane potential, nor to a modification of intramitochondrial ATP/ADP ratios. Applying the summation theorem of the control analysis, it was found that at low Ca2+ and pyruvate concentrations the dehydrogenases shared the control of state 3 respiration with other steps. The NAD-linked dehydrogenases did not exert any significant control at high Ca2+ or high pyruvate concentrations.

Animals↗
PubMed1974

Enzyme localization in the anaerobic mitochondria of Ascaris lumbricoides.

Mitochondria from the muscle of the parasitic nematode Ascaris lumbricoides var. suum function anaerobically in electron transport-associated phosphorylations under physiological conditions. These helminth organelles have been fractionated into inner and outer membrane, matrix, and intermembrane space fractions. The distributions of enzyme systems were determined and compared with corresponding distributions reported in mammalian mitochondria. Succinate and pyruvate dehydrogenases as well as NADH oxidase, Mg(++)-dependent ATPase, adenylate kinase, citrate synthase, and cytochrome c reductases were determined to be distributed as in mammalian mitochondria. In contrast with the mammalian systems, fumarase and NAD-linked "malic" enzyme were isolated primarily from the intermembrane space fraction of the worm mitochondria. These enzymes are required for the anaerobic energy-generating system in Ascaris and would be expected to give rise to NADH in the intermembrane space. The need for and possible mechanism of a proton translocation system to obtain energy generation is suggested.

Adenosine Triphosphatases↗
PubMed1994

Parkinson-like disease by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) toxicity in Macaca fascicularis: synaptosomal metabolism and action of dihydroergocriptine.

The maximal rates (Vmax) of some enzyme activities related to synaptosomal energy metabolism were studied in different types of synaptosomes from cerebellar cortex of Macaca Fascicularis (Cynomolgus monkey). Different synaptosomal populations, namely "large" and "small" synaptosomes, were isolated from the anterior lobule of the cerebellar cortex of monkeys treated p.o. with dihydroergocriptine at the dose of 12 mg/kg/day before and during the induction of a Parkinson's-like syndrome by MPTP administration (i.v., 0.3 mg/kg/day for 5 days). The enzymes were chosen according to their regulatory role and as markers of the following metabolic pathways: (a) glycolysis ((hexokinase, phosphofructokinase, lactate dehydrogenase), (b) Krebs' (TCA) cycle (citrate synthase, malate dehydrogenase), (c) amino acid, glutamate metabolism (glutamate dehydrogenase, glutamate-pyruvate- and glutamate-oxaloacetate-transaminases), (d) acetylcholine catabolism (acetylcholinesterase) and (e) ATPases, i.e. Na(+)-K(+)-ATPase, Mg(2+)-ATP synthetase, Mg(2+)-ATPase, Ca(2+)-Mg(2+)-ATPase and Ca(2+)-ATPase Low and High affinity for Ca2+. The MPTP administration modified the activities of citrate synthase, malate dehydrogenase, Na(+)-K(+)-ATPase, acetylcholinesterase and glutamate-oxaloacetate transaminase only on selected types of synaptosomes. Pharmacological treatment by dihydroergocriptine was able to recovery at the steady-state levels the activities of these enzymes, thus demonstrating a partial protective effect on these biochemical parameters.

Acetylcholine↗