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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Perfused rat hearts show a markedly increased binding of phosphofructokinase and fructose-bisphosphate aldolase as a consequence of ischaemia, but little change in binding of pyruvate kinase, lactate dehydrogenase or glyceraldehyde-3-phosphate dehydrogenase. After 10 min ischaemia over one quarter of the phosphofructokinase and three quarters of the aldolase are bound. The effect of anoxia is less well marked in its influence on binding with only aldolase showing a significant increase in binding. These results suggest that one factor involved in the increased binding during ischaemia is the fall in pH of the heart. Binding studies with isolated myofibrils confirm that the affinity and stoichiometry of aldolase binding are considerably increased as the pH is lowered over a range comparable to that which occurs in ischaemic heart. The low level of binding of glyceraldehyde-3-phosphate dehydrogenase in perfused rat hearts correlates with the relatively low affinity of this enzyme for binding to rat or rabbit cardiac myofibrils. There are species differences in the enzyme binding response to ischaemia. Sheep hearts show rapid and large increases in the binding of glyceraldehyde-3-phosphate dehydrogenase in addition to changes in aldolase and phosphofructokinase binding. The greater binding of glyceraldehyde-3-phosphate dehydrogenase reflects the greater affinity of sheep cardiac myofibrils. It is suggested that the altered metabolic demands of ischaemia are satisfied by changes in glycolytic enzyme organisation as the enzymes shift from the soluble to the particulate phase of cardiac muscle.
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PMID:Metabolic dependence of glycolytic enzyme binding in rat and sheep heart. 669 39

Hemoglobin, aldolase and glyceraldehyde 3-phosphate dehydrogenase are known to bind to the cytoplasmic domain of band 3 protein. Binding of glycolytic enzymes to band 3 protein is inhibited by its amino-terminal fragments. To precisely localize the sequence portion of band 3 protein to which hemoglobin binds and to see whether the same region of amino-acid sequence binds both hemoglobin and glycolytic enzymes, a simple, direct solid-phase binding assay was developed. Peptides generated from the 23-kDa fragment by trypsin, cyanogen bromide and mild acid hydrolysis were used as inhibitors to determine the minimal sequence structure involved in the binding of the 23-kDa fragment to hemoglobin. The shortest peptide which inhibits the binding of the 23-kDa fragment is an acid cleavage peptide containing the sequence positions 1 to 23. This sequence is unusual as 14 of its residues are negatively charged, it contains no basic residues and has its amino terminus blocked. Using aldolase, glyceraldehyde-3-phosphate dehydrogenase and hemoglobin as competitive inhibitors in the binding of 23-kDa fragment, the affinity of hemoglobin to this fragment appears several-fold weaker than that of both the enzymes. These findings demonstrate that glycolytic enzymes and hemoglobin bind competitively to the same polyanionic sequence region of band 3 protein.
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PMID:Hemoglobin binds to the amino-terminal 23-residue fragment of human erythrocyte band 3 protein. 671 38

Thermoanaerobium brockii was shown to catabolize glucose via the Embden-Meyerhof-Parnas pathway into ethanol, acetic acid, H(2)-CO(2), and lactic acid. Radioactive tracer studies, employing specifically labeled [(14)C]glucose, demonstrated significant fermentation of (14)CO(2) from C-3 and C-4 of the substrate exclusively. All extracts contained sufficient levels of activity (expressed in micromoles per minute per milligram of protein at 40 degrees C) to assign a catabolic role for the following enzymes: glucokinase, 0.40; fructose-1,6-diphosphate aldolase, 0.23; glyceraldehyde-3-phosphate dehydrogenase, 1.73; pyruvate kinase, 0.36; lactate dehydrogenase (fructose-1,6-diphosphate activated), 0.55; pyruvate dehydrogenase (coenzyme A acetylating), 0.53; hydrogenase, 3.3; phosphotransacetylase, 0.55; acetaldehyde dehydrogenase (coenzyme A acetylating), 0.15; ethanol dehydrogenase, 1.57; and acetate kinase, 1.50. All pyridine nucleotide-linked oxidoreductases examined were specific for nicotinamide adenine dinucleotide, except ethanol dehydrogenase which displayed both nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-linked activities. Fermentation product balances and cell growth yields supported the glucose catabolic pathway described. Representative balanced end product yields (in moles per mole of glucose fermented) were: ethanol, 0.94; l-lactate, 0.84; acetate, 0.20; CO(2), 1.31; and H(2), 0.50. Growth yields of 16.4 g of cells per mole of glucose were demonstrated. Both growth and end product yields varied significantly in accordance with the specific medium composition and incubation time.
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PMID:Glucose fermentation pathway of Thermoanaerobium brockii. 676 5

Two dimensional gel analysis of skeletal muscles from normal pigs and from pigs which were homozygous for halothane sensitivity showed no obvious differences in the patterns of spots attributed to the major contractile proteins and glycolytic enzymes. In muscle from a sensitive pig which died of heat shock under anaesthesia there was a selective loss of glyceraldehyde-3-phosphate dehydrogenase and aldolase, presumably owing to proteolytic activity. The progressive loss of these enzymes under anaesthesia could contribute to the mechanism of heat production by diverting fructose 1,6 diphosphate into a futile cycle.
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PMID:Investigation of malignant hyperthermia: analysis of skeletal muscle proteins from normal and halothane sensitive pigs by two dimensional gel electrophoresis. 684 31

NAD-Sepharose 4B gel was used to study the complexation between glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating) EC 1.2.1.12) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13). An affinity sorbent specific for glyceraldehyde-3-phosphate dehydrogenase was utilised in a batch system. The dissociation constant of the enzyme complex was calculated. The method elaborated in our laboratory was used to investigate the effects of temperature and pH on the complex formation.
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PMID:Characterization of enzyme-enzyme interaction using an affinity batch system. 710 69

Effects of sulfaguanidine, leucine, or leucine plus isoleucine in a niacin free diet on body weight changes, liver weight, pyridine nucleotide concentrations, and activities of enzymes in mature female or immature Japanese quail were measured. The inclusion of .5% of sulfaguanidine or a high level of leucine in a niacin free diet had no influence during an 8-week period on liver pyridine nucleotide levels and the development of niacin deficiency symptoms in mature female quail. This would suggest that the mature female quail has a low requirement for dietary niacin. Immature quail were also tested to study the effects of amino acid imbalance on the induction of niacin deficiency. Although there was a marked reduction in body weight gains by the administration of leucine or leucine plus isoleucine, these treatments did not appear to accentuate niacin deficiency symptoms in these animals. Also pyridine nucleotide levels and malic enzyme, glyceraldehyde-3-phosphate dehydrogenase, and aldolase activities in liver tissues were not affected by these treatments.
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PMID:Effects of sulfaguanidine and amino acid imbalances on the induction of niacin deficiency in mature and immature Japanese quail (Coturnix coturnix japonica). 713 12

Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.
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PMID:Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. 759 26

Antigens closely resembling or identical to the three glycolytic enzyme proteins phosphate-glycerate kinase, glyceraldehyde-3-phosphate dehydrogenase, and aldolase are found in situ in the nucleus of the leaf mesophyll cells of pea (Pisum sativum L.). These proteins have already been identified in vertebrate nuclei. Apparently, these enzymes are nuclear proteins with "secondary" roles not directly related to their enzymatic function in carbon metabolism in both animals and plants.
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PMID:Three enzymes of carbon metabolism or their antigenic analogs in pea leaf nuclei. 761 Jan 63

African trypanosomes are motile unicellular eukaryotes that can cause diseases such as sleeping sickness in humans and nagana in animals, debilitating millions of people and livestock. All members of the Trypanosomatidae family contain subpellicular microtubules cross-linked to each other and to the plasma membrane by unique trypanosomal microtubule-associated proteins (MAPs). These MAPs may serve as specific intracellular target sites for therapeutic attack against trypanosomiasis. A trypanosomal MAP (p52) copurifies with two glycosomal enzymes (aldolase and GAPDH) on phosphocellulose columns. Rats and mice vaccinated with antigen preparation p52 containing the glycosomal enzymes were protected against a potentially fatal Trypanosoma brucei infection. Sera of protected animals caused in vitro aggregation of trypanosomes, and immunoelectron microscopy of these aggregates located antibodies in the cytoplasm of the trypanosomes.
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PMID:Intracellular antigens (microtubule-associated protein copurified with glycosomal enzymes)--possible vaccines against trypanosomiasis. 765 80

In the facultative chemoautotroph Alcaligenes eutrophus H16, most of the genes (cbb genes) encoding enzymes of the Calvin carbon reduction cycle are organized within two highly homologous cbb operons, one located on the chromosome and the other on the megaplasmid pHG1. Nucleotide sequencing of the promoter-distal part of the operons revealed three open reading frames, designated cbbG, cbbK, and cbbA. Similarity searches in databases and heterologous expressions of the subcloned genes in Escherichia coli identified them as genes encoding the Calvin cycle enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and a class II fructose-1,6-bisphosphate aldolase, respectively. The aldolase could be grouped together with the enzymes from Rhodobacter sphaeroides and Bacillus subtilis as a new subtype of class II aldolases. A phenotypic complementation analysis with a cbb operon mutant of A. eutrophus showed that the cbbG product is essential for autotrophic growth of the organism, whereas the products of cbbK and cbbA can apparently be substituted by isoenzymes encoded elsewhere on the chromosome. No or only low constitutive promoter activity was associated with cbbK and cbbA, respectively, confirming the two genes as parts of the cbb operon. Downstream of cbbA, the very high overall nucleotide sequence identity (about 94%) prevailing throughout the two cbb operons discontinues, suggesting that cbbA is the most promoter-distal gene of the operon.
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PMID:Analysis of the genes forming the distal parts of the two cbb CO2 fixation operons from Alcaligenes eutrophus. 776 37


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