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Results for “Phosphopyruvate Hydratase”

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At least 19 recordsLinked to original sources
PubMed1976

Expression of the human adenylate kinase isozymes, phosphopyruvate hydratase, 6-phosphogluconate dehydrogenase, and phosphoglucomutase-1 in man-rodent somatic cell hybrids.

The expression of the adenylate kinase isozymes and of phosphopyruvate hydratase was studied in man-mouse and man-hamster hybrid clones. Concordant segregation of the loci coding for AK-2 and PPH was observed in 54 of 55 primary hybrid clones, and these loci were demonstrated to be synthetic with the loci specifying PGM-1 and PGD. The pattern of expression of the four enzymes in discordant clone suggests the gene order 1pter-(PGD, PPH)-AK-2-PGM-1-centromere. In addition, AK-1 was found to be expressed independently of AK-2.

Adenylate Kinase↗
PubMed1975

Location of gluconeogenesis from phosphoenolpyruvate in cotyledons of Cucurbita pepo.

1. The aim of this work was to discover the location of the enzymes that convert phosphoenolpyruvate to fructose 6-phosphate during gluconeogenesis in fatty seeds. Cotyledons of 5-day-old dark-grown seedlings of marrow (Cucurbita pepo) were used as experimental material. 2. Cotyledons were separated into palisade and mesophyll tissue. Extracts of the two tissues had comparable activities of gluconeogenic enzymes. 3. Extracts of cotyledons were fractionated by density gradient centrifugation to yeild mitochondria and glyoxysomes, and by gel filtration to yield proplastids. The isolated organelles retained their characteristic ultrastructure and appreciable amounts of marker enzymes. The proportions of the total activities of phosphoglyceromutase and fructose-1, 6-diphosphatase recovered in the mitochondrial and glyoxysomal preparations were insignificant. The same was true for the activities of phosphoglyceromutase and phosphopyruvate hydratase found in the proplastid preparations. 4. Extracts of a number of other gluconeigenic plant tissues were centrifuged at 2500 times g to yield particulate preparations. None of these preparations contained a significant proportion of the total activity of phosphoglyceromutase. 5. It is suggested that gluconeogenesis from phosphoenolpyruvate in plants occurs in the cytoplasm.

Cell Fractionation↗
PubMed1976

Effect of sodium fluoride on glycolysis in human erythrocytes and Ehrlich ascites tumour cells in vitro.

In human erythrocytes and Ehrlich ascites tumour cells, NaF inhibites aerobic glucose utilization and lactate formation. The inhibition of glycolysis was accompanied by a decrease in cellular pyruvate and ATP, and by accumulation of 2-hosphoenolpyruvate. These results and direct enzymatic determinations showed that fluoride inhibits, in addition to enolase (phosphopyruvate hydratase, EC 4.2.1.11), also pyruvate kinase.

Animals↗
PubMed2001

Crystal structure of the Escherichia coli RNA degradosome component enolase.

The crystal structure of Escherichia coli enolase (EC 4.2.1.11, phosphopyruvate hydratase), which is a component of the RNA degradosome, has been determined at 2.5 A. There are four molecules in the asymmetric unit of the C2 cell, and in one of the molecules, flexible loops close onto the active site. This closure mimics the conformation of the substrate-bound intermediate. A comparison of the structure of the E. coli enolase with the eukaryotic enolase structures available (lobster and yeast) indicates a high degree of conservation of the hydrophobic core and the subunit interface of this homodimeric enzyme. The dimer interface is enriched in charged residues compared with other protein homodimers, which may explain our observations from analytical ultracentrifugation that dimerisation is affected by ionic strength. The putative role of enolase in the RNA degradosome is discussed; although it was not possible to ascribe a specific role to it, a structural role is possible.

Animals↗
PubMed1977

Setaria cervi: enzymes of glycolysis and PEP-succinate pathway.

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.

Animals↗
PubMed1975

Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina).

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.

Alcohol Oxidoreductases↗
PubMed1995

Steady-state content of glycolytic/tricarboxylic acid-cycle intermediates, adenine nucleotide pools and the cellular redox-status in the infective (L3) larvae of (homogonic) Strongyloides ratti.

Infective (L3) larvae of Strongyloides ratti (homogonic strain) were freeze-clamped (-196 degrees C) and the steady-state content of the glycolytic, Krebs tricarboxylic acid (KTA)-cycle intermediates and adenine nucleotides analysed. Comparison of the mass-action ratios (MARs) of the glycolytic enzymes with their apparent equilibrium constants (K9eq) indicate that phosphoglucomutase, glucosephosphate isomerase, triosephosphate isomerase, phosphoglyceromutase and phosphopyruvate hydratase reactions were all at or near equilibrium, whilst hexokinase, phosphofructokinase and pyruvate kinase were displaced from equilibrium. The S. ratti aldolase and myokinase appear to be somewhat displaced from equilibrium and thus may have pseudoregulatory roles. The adenylate energy charge (AEC), ATP/ADP ratio and the available adenylate energy (AAE) indices were 0.9 +/- 0.04, 8.76 +/- 1.5 and 397 +/- 43, respectively. The free [NAD+]/[NADH+H+] ratio of the cytoplasmic compartment of S. ratti L3 larvae calculated employing the steady-state content of the oxidised and reduced substrates of lactate dehydrogenase (E.C. 1.1.1.27) and the combined glyceraldehyde 3-phosphate dehydrogenase (E.C. 1.2.1.12)/3-phosphoglycerate kinase (E.C. 2.7.2.3) system were ca. 523 and 1200, respectively. The free[NAD+]/[NADH+H+] ratio in the mitochondrial compartment of S. ratti L3 larvae calculated using the malate dehydrogenase (E.C. 1.1.1.37) equilibrium was found to be 1962:1. The data is discussed with respect to the predominantly aerobic nature of the energy metabolism of the L3 larvae.

Adenine Nucleotides↗
PubMed1989

Blood glucose partition and levels of glycolytic enzymes in erythrocytes and somatic tissues of penguins.

1. A comparative study was carried out on blood glucose partition and glucose metabolism of penguin erythrocytes and somatic tissues. Pygoscelidae penguins (Pygoscelis antarctica and P. papua) were used in these experiments. 2. Blood glucose partition was established by assaying whole blood and plasma glucose in several individuals of the gentoo and chinstrap penguins. 3. It was found that almost all the whole blood sugar is compartmentalized at the plasma site, the red blood cells being ineffective in regard to glucose metabolism. 4. Levels of hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose bisphosphate aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, phosphopyruvate hydratase (enolase), pyruvate kinase, alpha-glycerolphosphate dehydrogenase and fructose bisphosphate phosphatase were estimated in the erythrocytes of both gentoo and chinstrap penguins, the same determinations being carried out also on the somatic tissues (leg muscle, breast muscle, heart muscle, liver and brain) of the gentoo.

Animals↗
PubMed2002

Identification of protein degradation during post-mortem storage of pig meat.

Eighteen proteins and peptides that were found to change post-mortem in Longissimus dorsi from pig muscle were identified by the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The 18 peptides originate from 9 different proteins including the 3 structural proteins (actin, myosin heavy chain, and troponin T) and the 6 metabolic proteins glycogen phosphorylase, creatine kinase, phosphopyruvate hydratase, myokinase, pyruvate kinase, and dihydrolipoamide succinyltransferase. The molecular weight and estimated sequence length of the identified spots show that these fragments result from proteolytic activity in meat. Identification of the parent proteins and the enhanced post-mortem appearance of the degradation products make these specific peptides good candidates for meat quality markers, and further studies of these specific fragments will lead to a better understanding of the proteolytic activities involved in the post-mortem conversion of muscle to meat.

Animals↗