Effects of Exercise, Training, and Diet on Muscle Citric Acid Cycle Enzyme Activity

1973 ◽  
Vol 51 (6) ◽  
pp. 849-854 ◽  
Author(s):  
G. Lynis Dohm ◽  
Richard L. Huston ◽  
E. Wayne Askew ◽  
H. Lee Fleshood
Keyword(s):  
Citric Acid ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Exhaustive Exercise ◽  
High Fat ◽  
Acid Cycle ◽  
Cycle Enzyme ◽  
High Fat Diets ◽  
Citric Acid Cycle Enzymes ◽  
Fat Diets

The effects of training, exhaustive exercise, and diet on the activity of skeletal muscle citric acid cycle enzymes were studied. Training increased the activities of all cycle enzymes. Exhaustion of trained rats resulted in lowered activities of NAD-specific isocitrate dehydrogenase, succinate dehydrogenase, and cytochrome oxidase but citrate synthase and malate dehydrogenase were unaffected. The enzyme activities in untrained muscle were not changed by exhaustive exercise. High carbohydrate and high fat diets did not alter citric acid cycle activities in trained rested or untrained rested rats and did not moderate or accentuate the effects of exhaustive exercise. The results indicate that muscle citric acid cycle activity is increased by training and decreased by exhaustion of trained animals.

scholarly journals The activities of the citric acid-cycle enzymes in rat bone-marrow cells

1968 ◽  
Vol 108 (3) ◽  
pp. 413-415
Author(s):  
Eugene Goldwasser
Keyword(s):  
Bone Marrow ◽  
Citric Acid ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Bone Marrow Cells ◽  
Mitochondrial Enzymes ◽  
Acid Cycle ◽  
Citric Acid Cycle Enzymes ◽  
Rat Bone ◽  
Marrow Cells

The activities of the eight citric acid-cycle enzymes of rat bone-marrow cells were determined along with several other mitochondrial and non-mitochondrial enzymes. Four of the citric acid-cycle enzymes (aconitase, succinyl-CoA thiokinase, α-oxoglutarate dehydrogenase and succinate dehydrogenase) have closely similar low activities; two [isocitrate dehydrogenase (NAD) and citrate synthase] have intermediate activities; the remaining two (malate dehydrogenase and fumarase) have high activities. The other enzymes surveyed also exhibited a spread of three orders of magnitude, the mitochondrial enzymes showing no less variation than the others.

Citric acid cycle enzymes of the archaebacteria: citrate synthase and succinate thiokinase

FEBS Letters ◽  
1985 ◽  
Vol 179 (1) ◽  
pp. 120-124 ◽  
Author(s):  
Michael J. Danson ◽  
Susan C. Black ◽  
David L. Woodland ◽  
Pauline A. Wood
Keyword(s):  
Citric Acid ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Acid Cycle ◽  
Citric Acid Cycle Enzymes

scholarly journals Activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenase in muscle from vertebrates and invertebrates

1976 ◽  
Vol 154 (3) ◽  
pp. 689-700 ◽  
Author(s):  
P R. Alp ◽  
E A. Newsholme ◽  
V A. Zammit
Keyword(s):  
Citric Acid ◽  
Isocitrate Dehydrogenase ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Insect Flight ◽  
Mechanical Activity ◽  
Activity Data ◽  
Acid Cycle ◽  
Equilibrium Reaction ◽  
Flight Muscles

1. The activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenase were measured in muscles from a large number of animals, in order to provide some indication of the importance of the citric acid cycle in these muscles. According to the differences in enzyme activities, the muscles can be divided into three classes. First, in a number of both vertebrate and invertebrate muscles, the activities of all three enzymes are very low. It is suggested that either the muscles use energy at a very low rate or they rely largely on anaerobic glycolysis for higher rates of energy formation. Second, most insect flight muscles contain high activities of citrate synthase and NAD+-linked isocitrate dehydrogenase, but the activities of the NADP+-linked enzyme are very low. The high activities indicate the dependence of insect flight on energy generated via the citric acid cycle. The flight muscles of the beetles investigated contain high activities of both isocitrate dehydrogenases. Third, other muscles of both vertebrates and invertebrates contain high activities of citrate synthase and NADP+-liniked isocitrate dehydrogenase. Many, if not all, of these muscles are capable of sustained periods of mechanical activity (e.g. heart muscle, pectoral muscles of some birds). Consequently, to support this activity fuel must be supplied continually to the muscle via the circulatory system which, in most animals, also transports oxygen so that energy can be generated by complete oxidation of the fuel. It is suggested that the low activities of NAD+-linked isocitrate dehydrogenase in these muscles may be involved in oxidation of isocitrate in the cycle when the muscles are at rest. 2. A comparison of the maximal activities of the enzymes with the maximal flux through the cycle suggests that, in insect flight muscle, NAD+-linked isocitrate dehydrogenase catalyses a non-equilibrium reaction and citrate synthease catalyses a near-equilibrium reaction. In other muscles, the enzyme-activity data suggest that both citrate synthase and the isocitrate dehydrogenase reactions are near-equilibrium.

scholarly journals Another Unusual Type of Citric Acid Cycle Enzyme inHelicobacter pylori: the Malate:Quinone Oxidoreductase

2000 ◽  
Vol 182 (11) ◽  
pp. 3204-3209 ◽  
Author(s):  
Birgit Kather ◽  
Kerstin Stingl ◽  
Michel E. van der Rest ◽  
Karlheinz Altendorf ◽  
Douwe Molenaar
Keyword(s):  
Electron Transfer ◽  
Citric Acid ◽  
Citric Acid Cycle ◽  
Acid Cycle ◽  
Electron Transfer Chain ◽  
Cycle Enzyme ◽  
Coa Transferase ◽  
Standard Textbook ◽  
H Pylori ◽  
Transfer Chain

ABSTRACT The only enzyme of the citric acid cycle for which no open reading frame (ORF) was found in the Helicobacter pylori genome is the NAD-dependent malate dehydrogenase. Here, it is shown that in this organism the oxidation of malate to oxaloacetate is catalyzed by a malate:quinone oxidoreductase (MQO). This flavin adenine dinucleotide-dependent membrane-associated enzyme donates electrons to quinones of the electron transfer chain. Similar to succinate dehydrogenase, it is part of both the electron transfer chain and the citric acid cycle. MQO activity was demonstrated in isolated membranes of H. pylori. The enzyme is encoded by the ORF HP0086, which is shown by the fact that expression of the HP0086 sequence from a plasmid induces high MQO activity in mqo deletion mutants of Escherichia coli or Corynebacterium glutamicum. Furthermore, this plasmid was able to complement the phenotype of the C. glutamicum mqo deletion mutant. Interestingly, the protein predicted to be encoded by this ORF is only distantly related to known or postulated MQO sequences from other bacteria. The presence of an MQO shown here and the previously demonstrated presence of a 2-ketoglutarate:ferredoxin oxidoreductase and a succinyl-coenzyme A (CoA):acetoacetyl-CoA transferase indicate that H. pylori possesses a complete citric acid cycle, but one which deviates from the standard textbook example in three steps.

scholarly journals Citric Acid Cycle in the Hyperthermophilic Archaeon Pyrobaculum islandicum Grown Autotrophically, Heterotrophically, and Mixotrophically with Acetate

2006 ◽  
Vol 188 (12) ◽  
pp. 4350-4355 ◽  
Author(s):  
Yajing Hu ◽  
James F. Holden
Keyword(s):  
Citric Acid ◽  
Yeast Extract ◽  
Growth Rates ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Autotrophic Growth ◽  
Acid Cycle ◽  
Hyperthermophilic Archaeon ◽  
Citrate Lyase ◽  
Pyrobaculum Islandicum

ABSTRACT The hyperthermophilic archaeon Pyrobaculum islandicum uses the citric acid cycle in the oxidative and reductive directions for heterotrophic and autotrophic growth, respectively, but the control of carbon flow is poorly understood. P. islandicum was grown at 95°C autotrophically, heterotrophically, and mixotrophically with acetate, H2, and small amounts of yeast extract and with thiosulfate as the terminal electron acceptor. The autotrophic growth rates and maximum concentrations of cells were significantly lower than those in other media. The growth rates on H2 and 0.001% yeast extract with and without 0.05% acetate were the same, but the maximum concentration of cells was fourfold higher with acetate. There was no growth with acetate if 0.001% yeast extract was not present, and addition of H2 to acetate-containing medium greatly increased the growth rates and maximum concentrations of cells. P. islandicum cultures assimilated 14C-labeled acetate in the presence of H2 and yeast extract with an efficiency of 55%. The activities of 11 of 19 enzymes involved in the central metabolism of P. islandicum were regulated under the three different growth conditions. Pyruvate synthase and acetate:coenzyme A (CoA) ligase (ADP-forming) activities were detected only in heterotrophically grown cultures. Citrate synthase activity decreased in autotrophic and acetate-containing cultures compared to the activity in heterotrophic cultures. Acetylated citrate lyase, acetate:CoA ligase (AMP forming), and phosphoenolpyruvate carboxylase activities increased in autotrophic and acetate-containing cultures. Citrate lyase activity was higher than ATP citrate synthase activity in autotrophic cultures. These data suggest that citrate lyase and AMP-forming acetate:CoA ligase, but not ATP citrate synthase, work opposite citrate synthase to control the direction of carbon flow in the citric acid cycle.

The extraordinary mitochondrion and unusual citric acid cycle in Trypanosoma brucei

2005 ◽  
Vol 33 (5) ◽  
pp. 967-971 ◽  
Author(s):  
J.J. van Hellemond ◽  
F.R. Opperdoes ◽  
A.G.M. Tielens
Keyword(s):  
Citric Acid ◽  
Energy Metabolism ◽  
Trypanosoma Brucei ◽  
Citric Acid Cycle ◽  
Clinical Importance ◽  
African Trypanosomes ◽  
Acid Cycle ◽  
Fermentative Metabolism ◽  
Influence Of Substrate ◽  
Citric Acid Cycle Enzymes

African trypanosomes are parasitic protozoa that cause sleeping sickness and nagana. Trypanosomes are not only of scientific interest because of their clinical importance, but also because these protozoa contain several very unusual biological features, such as their specially adapted mitochondrion and the compartmentalization of glycolytic enzymes in glycosomes. The energy metabolism of Trypanosoma brucei differs significantly from that of their hosts and changes drastically during the life cycle. Despite the presence of all citric acid cycle enzymes in procyclic insect-stage T. brucei, citric acid cycle activity is not used for energy generation. Recent investigations on the influence of substrate availability on the type of energy metabolism showed that absence of glycolytic substrates did not induce a shift from a fermentative metabolism to complete oxidation of substrates. Apparently, insect-stage T. brucei use parts of the citric acid cycle for other purposes than for complete degradation of mitochondrial substrates. Parts of the cycle are suggested to be used for (i) transport of acetyl-CoA units from the mitochondrion to the cytosol for the biosynthesis of fatty acids, (ii) degradation of proline and glutamate to succinate, (iii) generation of malate, which can then be used for gluconeogenesis. Therefore the citric acid cycle in trypanosomes does not function as a cycle.

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