Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mutants of mucoid Pseudomonas aeruginosa defective in fructose-bisphosphate aldolase (FBA), NADP-linked glyceraldehyde-3-phosphate dehydrogenase (GAP) or 3-phosphoglycerate kinase (PGK) were unable to grow on gluconeogenic precursors like glutamate, succinate or lactate. The gap and pgk mutants could grow on glucose, gluconate or glycerol, but fba mutants could not. This suggests that the metabolism of glucose or gluconate does not require either PGK or NADP-linked GAP but does require the operation of the aldolase-catalysed step. For gluconeogenesis, however, all three steps are essential. Recombinant plasmids carrying genes for FBA, PGK, GAP or phospho-2-keto-3-deoxygluconate aldolase (EDA) activities were constructed from a genomic library of mucoid P. aeruginosa selecting for complementation of deficiency mutations. Analysis of their complementation profile indicated that one group of plasmids carried fba and pgk genes, while another group carried eda, 6-phosphogluconate dehydratase (edd) and glucose-6-phosphate dehydrogenase (zwf) genes. The gap gene was not linked to any of these markers. Partial restoration of FBA activity in spontaneous revertants of Fba- mutants was accompanied by a concomitant loss of PGK activity. These experiments indicate a linkage between the fba and pgk genes on the P. aeruginosa chromosome.
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PMID:Gluconeogenic mutations in Pseudomonas aeruginosa: genetic linkage between fructose-bisphosphate aldolase and phosphoglycerate kinase. 311 66

Glycosomes and mitochondrial vesicles from cultured promastigotes of Leishmania mexicana mexicana have been separated using isopycnic centrifugation on linear sucrose gradients. Hexokinase (EC 2.7.1.2), glucose phosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), and phosphoenolpyruvate carboxykinase (EC 4.1.1.49) were recovered largely in association with glycosomes (density; 1.215 g/ml). Phosphoglycerate kinase (EC 2.7.2.3) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) had some small glycosomal activity, but were mostly recovered in the soluble fractions. Malate dehydrogenase (EC 1.1.1.37) showed a broad peak corresponding to that of the mitochondrial marker oligomycin-sensitive ATPase (EC 3.6.1.4) (density; 1.190 g/ml). Glutamate dehydrogenase (EC 1.4.1.3) and alanine aminotransferase (EC 2.6.1.2) both showed small mitochondrial peaks, but most of the activities were recovered elsewhere on the gradient and in the soluble fractions. The subcellular location of enzymes in L.m. mexicana amastigotes was investigated by following the release of soluble enzymes from digitonin-treated amastigotes. This revealed distinct cytosolic, mitochondrial, and glycosomal compartments. The findings give an insight into the organization and control of L.m. mexicana promastigote and amastigote energy metabolism.
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PMID:Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. 315 38

The influence of prolactin (Prl) and bromocriptine on the specific activities of neural and glial cellular enzymes involved in carbohydrate metabolism in cerebral cortex, hypothalamus, cerebellum and pons-medulla was studied. Both Prl and bromocriptine stimulated the activity of hexokinase (HK) in the neural as well as in the glial cells. While Prl increased the activity of phosphofructokinase (PFK), glyceraldehyde-3-phosphate dehydrogenase (G-3-PDH) and pyruvate kinase (PK) in the neural cells, it decreased the same in the glial cells. On the other hand, bromocriptine elevated the activity of all these enzymes in the neural cells without any effect on the glial cells. The activities of neural cellular glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH) were inhibited by Prl, whereas bromocriptine increased the same. The activities of these enzymes in the glial cells were enhanced by both Prl and bromocriptine. Thus, the present study suggests that Prl has a differential effect on the activities of enzymes involved in Embden-Meyerhoff pathway (EMP) and hexosemonophosphate shunt (HMP) in the neural and glial cells of immature male bonnet monkeys.
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PMID:Role of prolactin on neural and glial cellular enzymes involved in carbohydrate metabolism. I. Studies on immature male bonnet monkeys. 340 16

Three anaesthetics (halothane, CF3CHClBr; Ethrane, F2 HCOF2CCHClF; cyclopropane) and one other halogenated, short-chain hydrocarbon (F-12, Cl2F2C) were tested under various conditions to determine their effects on the viability of cells of Escherichia coli and the activities of some of its enzymes. When any of the test chemicals were applied for 60 min at concentrations slightly in excess of saturation, the number of surviving cells decreased substantially, with halothane being the most biocidal of the four chemicals and F-12 the least. Three enzymes (malate dehydrogenase, MD; NADH dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase, GPD) were tested for activity after treatment of E. coli with the test chemicals. In all instances, GPD was least resistant to inactivation and MD was most resistant. Halothane was most inhibitory followed in order by Ethrane, cyclopropane and F-12. Treatment of E. coli with halothane for 60 min at 23 degrees C and a concentration slightly in excess of saturation, resulted in nearly complete inhibition of all three enzymes.
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PMID:Effect of anaesthetics and dichlorodifluoromethane on the viability of the cells of Escherichia coli and the activities of some of its enzymes. 391 44

Monospecific (affinity-purified) anti-(yeast glucose-6-phosphate dehydrogenase) IgG inhibits three different NADPH-requiring enzymes, chicken liver dihydrofolate reductase, pigeon liver fatty acid synthetase and chicken liver malic enzyme. The inhibition of all three enzymes was approx. 50% in a 2h incubation with 100 micrograms of IgG. Similarly, with several different NADH-requiring enzymes, an immunocrossreactivity was observed. Monospecific anti-(rabbit muscle glyceraldehyde-3-phosphate dehydrogenase) IgG inhibited yeast alcohol dehydrogenase and pig heart malate dehydrogenase by 39% and 55% respectively. The cross-reactivity observed was tested by affinity chromatography. Immunoaffinity columns made with each monospecific IgG were able to bind each of the enzymes it immunotitrated. Enzymes were eluted with a nondenaturing solvent with little loss of activity. The immunoaffinity column with monospecific anti-(glucose-6-phosphate dehydrogenase) IgG as the bound ligand was also used to purify partially (over 150-fold) both isocitrate dehydrogenase and dihydrofolate reductase from crude rat liver homogenate.
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PMID:Purification of nucleotide-requiring enzymes by immunoaffinity chromatography. 398 38

Cathepsins M and B from rabbit liver lysosomes were separated by chromatography on Ultrogel AcA34 at low ionic strength and purified to homogeneity, and their catalytic and molecular properties were compared. Cathepsin M was relatively inactive with synthetic peptide substrates. Thus, it hydrolyzed benzoyl arginine naphthylamide at only one-fifth the rate observed with cathepsin B, and no activity was detected with Gly-Phe naphthylamide which is a relatively good substrate for cathepsin B. On the other hand, cathepsin M exhibited a preference for protein substrates. It was more active than cathepsin B in catalyzing the inactivation of the following enzymes: rabbit muscle or liver fructose-1,6-bisphosphate aldolases, rabbit liver fructose-1,6-bisphosphatase and pyruvate kinase, yeast glucose-6-phosphate dehydrogenase, and rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. With glucagon as substrate, both enzymes showed similar peptidyl dipeptidase activities with some minor differences in peptide bond specificity. Cathepsins M and B are similar in size, with apparent molecular weights of 30,200 for cathepsin M and 28,800 for cathepsin B, and in amino acid composition and carbohydrate content. Each contains approximately 2-3 equivalents/mol glucosamine, 3 equivalents/mol mannose, and no fucose or galactosamine. They also show similar microheterogeneity in sodium dodecylsulfate-gel electrophoresis and isoelectric focusing; this microheterogeneity is probably related to differences in glycosylation. Extensive homology in primary structure for the two proteins was indicated by the similar patterns of peptides formed on digestion with trypsin.
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PMID:Purification and properties of rabbit liver cathepsin M and cathepsin B. 406 7

Crude extracts of both vegetative cells and glycerol-induced microcysts of Myxococcus xanthus contained the following enzyme activities: phosphofructokinase, phosphoglucoisomerase, fructose-1,6-diphosphatase, fructosediphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate carboxylase, citrate synthase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and uridine diphosphate glucose pyrophosphorylase. With the exception of isocitrate dehydrogenase, which was present at a fivefold higher concentration in microcysts, all activities in extracts from both types of cells were essentially equal. Hexokinase and pyruvate kinase could not be detected in extracts from either type of cell. Microcysts metabolized acetate at a lower rate than did vegetative cells. Most of this decrease was reflected in a substantial decrease in ability of microcysts to oxidize acetate to CO(2). In addition, microcysts and vegetative cells showed a different distribution of (14)C-label from incorporated acetate.
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PMID:Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. 430 96

Kanetsuna, Fuminori (Instituto Venezolano de Investigaciones Cientificas, Caracas, Venezuela), and Luis M. Carbonell. Enzymes in glycolysis and the citric acid cycle in the yeast and mycelial forms of Paracoccidioides brasiliensis. J. Bacteriol. 92:1315-1320. 1966.-Enzymatic activities in glycolysis, the hexose monophosphate shunt, and the citric acid cycle in cell-free extracts of the yeast and mycelial forms of Paracoccidioides brasiliensis were examined comparatively. Both forms have the enzymes of these pathways. Activities of glucose-6-phosphate dehydrogenase and malic dehydrogenase of the mycelial form were higher than those of the yeast form. Another 15 enzymatic activities of the mycelial form were lower than those of the yeast form. The activity of glyceraldehyde-3-phosphate dehydrogenase showed the most marked difference between the two forms, its activity in the mycelial form being about 20% of that in the yeast form.
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PMID:Enzymes in glycolysis and the citric acid cycle in the yeast and mycelial forms of Paracoccidioides brasiliensis. 592 67

Histochemical studies have been conducted by applying hexokinase (HK), aldolase (AD), glyceraldehyde-3-phosphate dehydrogenase (G3), succinate dehydrogenase (SDH), glucose-6-phosphate dehydrogenase (G6PD), and thiamine pyrophosphatase (TPPase) methods, as well as Nissl staining and Gomori's chrome-alum-hematoxylin-phloxine (CHP) methods to intercalated neurons of the supraoptic nucleus (SO) on Wistar strain rats. Intercalated neurons reacted weakly to the AD, G3, G6PD, and SDH tests, indicating that they belong to the category of ordinary neurons with low carbohydrate metabolism. Many fibrous astrocytes showing strong HK reactions surround neurosecretory neurons. However, they do not surround intercalated neurons with mild HK activity. These results indicate that the latter receive a poor supply of energy from glucose in the circulating blood in contrast to the former. Intercalated neurons are very rich in Nissl substance but lack CHP-positive material. They may have a high potential for synthesizing protein. The principal morphological features of the TPPase-positive Golgi material are peculiar and heterogeneous shape and poor development. These findings together with mild G6PD activity suggest that intercalated neurons are very likely to have poor synthesizing activity.
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PMID:Histochemical studies on the distribution of thiamine pyrophosphatase and enzymes related to carbohydrate metabolism in the intercalated neurons of the rat supraoptic nucleus. 613 41

Red cell enzymes, 2,3-diphosphoglycerate (2,3-DPG) and adenosine triphosphate (ATP), were evaluated in a 23-mo-old boy with juvenile chronic myelocytic leukemia (JCML) at the onset of his illness and 6 mo later during the accelerated phase. The activities of the age-dependent red cell enzymes, hexokinase, aldolase, pyruvate kinase, and glucose-6-phosphate dehydrogenase, were elevated, as were the concentrations of red cell 2,3-DPG and ATP, consistent with a young red cell population metabolizing at an increased glycolytic rate. The activities of the non-age-dependent enzymes, glyceraldehyde-3-phosphate dehydrogenase (G3PD), phosphoglycerate kinase, and enolase, were also increased to levels similar to or greater than those observed in term infants. As the illness progressed, the activity of red cell G3PD increased further, and phosphoglucose isomerase activity increased markedly. These results are consistent with the prior suggestion that JCML represents a reversion to "fetal" erythropoiesis.
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PMID:Fetal erythropoiesis in juvenile chronic myelocytic leukemia. 622 20


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