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:2.3.3.1 (citrate synthase)
4,488 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetate oxidation by sulphate was studied with desulfobacter postgatei. Cell extracts of the organism were found to contain high activities of the following enzymes: citrate synthase, aconitase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase and pyruvate synthase. It is concluded that acetate oxidation with sulphate in D. postgatei proceeds via the citric acid cycle with the synthesis of pyruvate from acetyl CoA and CO2 as an anaplerotic reaction. The apparent Ks for acetate oxidation by D. postgatei as determined in vivo was near 0.2 mM. The apparent Ks for acetate fermentation to methane and CO2 by methanosarcina barkeri was 3 mM. The significantly lower ks for acetate of the sulphate reducer explains why methane formation from acetate in natural habitats is apparently inhibited by sulphate.
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PMID:Dissimilatory sulphate reduction with acetate as electron donor. 612 36

Histochemical analysis of five muscles from the water monitor, Varanus salvator, identified three major classes of fibers based on histochemical activities of the enzymes myosin ATPase (mATPase), succinic dehydrogenase (SDH), and alpha-glycerophosphate dehydrogenase (alpha GPDH). Fast-twitch, glycolytic (FG) fibers were the most abundant fiber type and exhibited the following reaction product intensities: mATPase, dark; SDH, light; alpha GPDH, moderate to dark. Fast-twitch, oxidative, glycolytic (FOG) fibers were characteristically mATPase, dark; SDH, light; alpha GPDH, moderate to dark. The third class of fibers had the following histochemical characteristics: mATPase, light; SDH, moderate to dark; alpha GPDH, light. These fibers were considered to be either slow twitch, or tonic, and oxidative (S/O). Pyruvate kinase (PK), alpha GPDH, and citrate synthase (CS) activities were measured in homogenates of the same muscles studied histochemically. There was a positive relationship between both PK and alpha GPDH activities and the percentage of glycolytic fiber types within a muscle. Likewise, CS activities were greater in muscles high in FOG and S/O content. Based on CS activities, Varanus S/O fibers were eight-fold more oxidative than FG fibers within the same muscle. PK/CS ratios suggested that FG fibers possess high anaerobic capacity, similar to the iguanid lizard Dipsosaurus. The fiber type composition of the gastrocnemius muscle, relative to that of other lizard species, suggests that varanid lizards may possess a greater proportion of FOG and S/O fibers than other lizards.
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PMID:A histochemical and enzymatic study of the muscle fiber types in the water monitor, Varanus salvator. 622 35

The behavior of several enzymes was studied during rat heart development (4 days before birth to adult stage). Hexokinase has its highest activity during the fetal period; it decreases at birth and remains with low activity in the adult. The alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate oxidase profiles are similar up to the 15th day of development. From there onwards, both profiles diverge, the cytoplasmic activity increasing 3-fold, while the mitochondrial activity remains unchanged. The developmental profiles of the malate dehydrogenases are almost parallel. The development of citrate synthase and succinate dehydrogenase results in a 2- to 4-fold increase in their activities. However, ATPase increases dramatically (20-fold) over the same period. With respect to the enzymes of the adenine nucleotide metabolism, adenylate kinase is fully expressed throughout all ages examined, showing no variation during development. AMP deaminase and creatine kinase increase during development, the cytoplasmic creatine kinase reaching a high level at birth whereas the increases of the mitochondrial enzymes take place gradually during development.
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PMID:Development of enzymes of energy metabolism in rat heart. 623 Jan 12

We studied the effects of running-training, heavy exercise and termination of training on the heart weight, the ratio heart to body weight and the cardiac muscle activities of actomyosin ATPase, citrate synthase, succinate dehydrogenase, cytochrome c oxidase, malate dehydrogenase, adenylate kinase and beta-glucuronidase with adult male NMRI-mice. Stable hypertrophy (6-7%), estimated by the ratio heart or ventricle weight to body weight, was achieved by 28 exercises and it was dependent on the running speed (20 vs. 25 m X min-1). The withdrawal of training for 5-61 days did not permanently decrease the heart weight or the heart to body weight ratio to the level of sedentary controls. The activity of enzymes of energy metabolism or actomyosin ATPase were not affected by training, heavy exercise or terminated training. beta-glucuronidase activity slightly (20-25%) increased in the trained animals and remained at a higher level during the period of terminated training. The results suggest that the capacity for aerobic metabolism of normal mice heart is sufficient to meet the enhanced demand for ATP imposed by running-training and that the heart enlargement occurs in equal proportions with the enzymatic potential of the cardiac tissue.
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PMID:Selected enzyme activities in mouse cardiac muscle during training and terminated training. 623 64

The Clarke-Carbon colony bank containing ColE1-Escherichia coli hybrid plasmids was screened by conjugation for complementation of the citrate synthase lesion of a gltA mutant. Three ColE1-gltA+ plasmids were identified: pLC26-17 (16.3 kilobase pairs), pLC27-18 (16.35 kb) and pLC31-28 (26.0 kb). The citrate synthase activities of strains containing the hybrid plasmids were amplified 3- to 10-fold. Genetic studies indicated that the smaller plasmids may contain at least part of the succinate dehydrogenase gene (sdh). A physical map of a 19.4 kb region of the E. coli chromosome containing the citrate synthase gene (gltA) was constructed by restriction analysis with the isolated plasmids. The relative positions of 20 restriction sites were defined and a region (3.1 kb) containing the gltA+ gene was identified in the segment common to all three plasmids.
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PMID:Hybrid plasmids containing the citrate synthase gene (gltA) of Escherichia coli K12. 627 5

A fragment of DNA (3.1 kilobases [kb]) from a ColE1 Escherichia coli DNA hybrid plasmid containing the bacterial citrate synthase gene (gltA) was subcloned in both orientations into phage lambda vectors by in vitro recombination. The resulting phages were able to transduce gltA and, as prophages, complemented the lesion of a gltA mutant, showing that a functional gltA gene is contained in the 3.1-kb fragment. The segment of E. coli DNA cloned in these lambda gltA phages was extended in vivo by prophage integration and aberrant excision in the gltA region. Plaque-forming derivatives, carrying up to three additional tricarboxylic acid cycle genes, succinate dehydrogenase (sdh), 2-oxoglutarate dehydrogenase (sucA), and dihydrolipoamide succinyltransferase (sucB), were isolated and characterized by their transducing and complementing activities with corresponding mutants, and the order of the genes was confirmed as gltA-sdh-sucA-sucB. Physical maps of a variety of the transducing phages showed that the four tricarboxylic acid cycle genes are contained in a 12.8-kb segment of bacterial DNA. The four gene products, plus a possible succinate dehydrogenase small subunit, were identified in postinfection labeling studies, and the polarities of gene expression were defined as counterclockwise for gltA and clockwise for sdh, sucA, and sucB, relative to the E. coli linkage map.
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PMID:Molecular cloning of four tricarboxylic acid cyclic genes of Escherichia coli. 628 1

The effect of endurance training on skeletal muscle myoglobin concentration in man was investigated. 8 healthy sedentary males (20-31 yrs) trained on cycle ergometers 40 min/day, 4 days a week for 8 weeks. The work consisted of continuous exercise at a work load that during the last 5 weeks corresponded to 75% of the pretraining maximal oxygen uptake (VO2 max). The training program resulted in a 7% increase in VO2 max (p less than 0.01). The activities of the mitochondrial enzymes citrate synthase (CS), succinate dehydrogenase (SDH) and cytochrome c oxidase (Cyt-c-ox) in the quadriceps femoris muscle, as indicators of muscle respiratory capacity, increased by 62-82% (p less than 0.01). The metabolic adaptation of skeletal muscle was further indicated by a 17% increase in the work load corresponding to a blood lactate concentration of 4 mmol/l, as determined by a progressive exercise test (p less than 0.05). There was, however, no change in the myoglobin concentration of the thigh muscle with training (-1%, NS). It is suggested that endurance exercise in man at 75% of the maximal oxygen uptake does not severely tax the functions of myoglobin in skeletal muscle.
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PMID:Dissociation of training effects on skeletal muscle mitochondrial enzymes and myoglobin in man. 630 98

The nucleotide sequence of a 3614 base-pair segment of DNA containing the sdhA gene, encoding the flavoprotein subunit of succinate dehydrogenase of Escherichia coli, and two genes sdhC and sdhD, encoding small hydrophobic subunits, has been determined. Together with the iron-sulphur protein gene (sdhB) these genes form an operon (sdhCDAB) situated between the citrate synthase gene (gltA) and the 2-oxoglutarate dehydrogenase complex genes (sucAB): gltA-sdhCDAB-sucAB. Transcription of the gltA and sdhCDAB gene appears to diverge from a single intergenic region that contains two pairs of potential promoter sequences and two putative CRP (cyclic AMP receptor protein)-binding sites. The sdhA structural gene comprises 1761 base-pairs (587 codons, excluding the initiation codon, AUG) and it encodes a polypeptide of Mr 64268 that is strikingly homologous with the flavoprotein subunit of fumarate reductase (frdA gene product). The FAD-binding region, including the histidine residue at the FAD-attachment site, has been identified by its homology with other flavoproteins and with the flavopeptide of the bovine heart mitochondrial succinate dehydrogenase. Potential active-site cysteine and histidine residues have also been indicated by the comparisons. The sdhC (384 base-pairs) and sdhD (342 base-pairs) structural genes encode two strongly hydrophobic proteins of Mr 14167 and 12792 respectively. These proteins resemble in size and composition, but not sequence, the membrane anchor proteins of fumarate reductase (the frdC and frdD gene products).
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PMID:Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. 638 59

The nucleotide sequence of a 961 base-pair segment of DNA containing the sdhB gene, which encodes the iron-sulphur protein subunit of the E. coli succinate dehydrogenase, has been determined. The sdhB structural gene comprises 711 base pairs (237 codons, excluding the translational initiator and terminator). It is separated by a 15 base-pair intergenic region from the preceding flavoprotein gene (sdhA) and is the distal gene of an operon that also includes genes (sdhC and D) encoding two hydrophobic subunits, sdhCDAB. The distal end of the sdh operon is linked to the 2-oxoglutarate dehydrogenase gene (sucA) by a complex region of dyad symmetry that is homologous with several potential intercistronic regulatory elements or transcriptional attenuators. The sdhB structural gene encodes a polypeptide of Mr26637 that is strikingly homologous with the iron-sulphur protein subunit of fumarate reductase (38% identity, increasing to 58% when conservative changes are included). Both subunits contain 11 cysteine residues, 10 being conserved in three clusters resembling those found in ferredoxins. This work completes the sequence of a 9897 base-pair segment of DNA containing seven tricarboxylic acid cycle genes encoding three enzymes or enzyme complexes, citrate synthase (gltA), succinate dehydrogenase (sdh), and the 2-oxoglutarate dehydrogenase complex (suc), that are organized thus: gltA-sdhCDAB-sucAB.
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PMID:Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. 638 71

NADH:ubiquinone reductase (complex I) of the mitochondrial inner membrane respiratory chain binds a number of mitochondrial matrix NAD-linked dehydrogenases. These include pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, mitochondrial malate dehydrogenase, and beta-hydroxyacyl-CoA dehydrogenase. No binding was detected between complex I and cytosolic malate dehydrogenase, glutamate dehydrogenase, NAD-isocitrate dehydrogenase, lipoamide dehydrogenase, citrate synthase, or fumarase. The dehydrogenases that bound to complex I did not bind to a preparation of complex II and III, nor did they bind to liposomes. The binding of pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, and mitochondrial malate dehydrogenase to complex I is a saturable process. Based upon the amount of binding observed in these in vitro studies, there is enough inner membrane present in the mitochondria to bind the dehydrogenases in the matrix space. The possible metabolic significance of these interactions is discussed.
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PMID:Complex I binds several mitochondrial NAD-coupled dehydrogenases. 643 16


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