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

Cell-free extracts of Methanobacterium thermoautotrophicum were found to contain high activities of the following oxidoreductases (at 60 degrees C): pyruvate dehydrogenase (coenzyme A acetylating), 275 nmol/min per mg of protein; alpha-ketoglutarate dehydrogenase (coenzyme A acylating), 100 nmol/min per mg; fumarate reductase, 360 nmol/min per mg; malate dehydrogenase, 240 nmol/min per mg; and glyceraldehyde-3-phosphate dehydrogenase, 100 nmol/min per mg. The kinetic properties (apparent V(max) and K(M) values), pH optimum, temperature dependence of the rate, and specificity for electron acceptors/donors of the different oxidoreductases were examined. Pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase were shown to be two separate enzymes specific for factor 420 rather than for nicotinamide adenine dinucleotide (NAD), NADP, or ferredoxin as the electron acceptor. Both activities catalyzed the reduction of methyl viologen with the respective alpha-ketoacid and a coenzyme A-dependent exchange between the carboxyl group of the alpha-ketoacid and CO(2). The data indicate that the two enzymes are similar to pyruvate synthase and alpha-ketoglutarate synthase, respectively. Fumarate reductase was found in the soluble cell fraction. This enzyme activity coupled with reduced benzyl viologen as the electron donor, but reduced factor 420, NADH, or NADPH was not effective. The cells did not contain menaquinone, thus excluding this compound as the physiological electron donor for fumarate reduction. NAD was the preferred coenzyme for malate dehydrogenase, whereas NADP was preferred for glyceraldehyde-3-phosphate dehydrogenase. The organism also possessed a factor 420-dependent hydrogenase and a factor 420-linked NADP reductase. The involvement of the described oxidoreductases in cell carbon synthesis is discussed.
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PMID:Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum. 91 79

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

We have analyzed the proteins that are oxidatively damaged when Saccharomyces cerevisiae cells are exposed to stressing conditions. Carbonyl groups generated by hydrogen peroxide or menadione on proteins of aerobically respiring cells were detected by Western blotting, purified, and identified. Mitochondrial proteins such as E2 subunits of both pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, aconitase, heat-shock protein 60, and the cytosolic fatty acid synthase (alpha subunit) and glyceraldehyde-3-phosphate dehydrogenase were the major targets. In addition we also report the in vivo modification of lipoamide present in the above-mentioned E2 subunits under the stressing conditions tested and that this also occurs with the homologous enzymes present in Escherichia coli cells that were used for comparative analysis. Under fermentative conditions, the main protein targets in S. cerevisiae cells treated with hydrogen peroxide or menadione were pyruvate decarboxylase, enolase, fatty acid synthase, and glyceraldehyde-3-phosphate dehydrogenase. Under the stress conditions tested, fermenting cells exhibit a lower viability than aerobically respiring cells and, consistently, increased peroxide generation as well as higher content of protein carbonyls and lipid peroxides. Our results strongly suggest that the oxidative stress in prokaryotic and eukaryotic cells shares common features.
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PMID:Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. 1085 12

The triplicate intracerebroventricular (icv) application of the diabetogenic compound streptozotocin (STZ) in low dosage was used in 1-year-old male Wistar rats to induce a damage of the neuronal insulin signal transduction (IST) system and to investigate the activities of hexokinase (HK), phosphofructokinase (PFK), glyceraldehyde-3-phosphate dehydrogenase (GDH), pyruvate kinase (PK), lactate dehydrogenase (LDH) and alpha-ketoglutarate dehydrogenase (alpha-KGDH) in frontoparietotemporal brain cortex (ct) and hippocampus (h) 9 weeks after damage. In parallel, the concentrations of adenosine triphosphate (ATP), adenosine diphosphate (ADP), guanosine triphosphate (GTP) and creatine phosphate (CrP) were determined. We found reductions of HK to 53% (ct) and 60% (h) of control, PFK to 63/64% (ct/h); GDH to 56/61% (ct/h), PFK to 57/59% (ct/h), alpha-KGDH to 37/35% (ct/h) and an increase of LDH to 300/240% (ct/h). ATP decreased to 82/87% (ct/h) of control, GTP to 69/81% (ct/h), CrP to 82/81% (ct/h), approximately P to 82/82% (ct/h), whereas ADP increased to 189/154% (ct/h). The fall of the activities of the glycolytic enzymes HK, PFK, GDH and PK was found to be more marked after 9 weeks of damage when compared with 3- and 6-week damage whereas the diminution in the concentration of energy rich compound was stably reduced by between 20 and 10% relative to control. The abnormalities in glucose/energy metabolism were discussed in relation to tau-protein mismetabolism of experimental animals, and of sporadic AD.
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PMID:Long-term abnormalities in brain glucose/energy metabolism after inhibition of the neuronal insulin receptor: implication of tau-protein. 1798 95

Pseudomonas sp. C27 is a facultative autotrophic bacterium that can effectively conduct mixotrophic and heterotrophic denitrification reactions using organic matters and sulfide as electron donors. There is no experimental confirmation on proteomic levels the pure C27 strain can have the capability to simultaneous removal of sulfide, nitrate and organic carbon from waters. The proteome in total C27 cell extracts was observed by two-dimensional gel electrophoresis. The 160mg/L sulfide up-regulated or specifically expressed succinate dehydrogenase, iron-sulfur protein, oxidoreductase, serine hydroxymethyltransferase, and iron superoxide dismutase for sulfide metabolism, 2-oxoglutarate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, NAD(+)-dependent aldehyde dehydrogenase, malate dehydrogenase and succinate dehydrogenase for carbon metabolism, and nitrous-oxide reductase and respiratory nitrate reductase for nitrogen metabolism. The study confirmed that the C27 strain has an effective enzyme system to conduct denitrifying sulfide removal reactions. Also, sulfide stress can enhance energy consumption rate and rates of nitrate reduction and sulfide oxidation by C27. Conversely, sulfide stress repressed the sulfate-reducing power of C27, evidenced by down-regulation or specific un-expression of sulfate ABC transporter, periplasmic sulfate-binding protein in the (C+N+S) sample.
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PMID:Sulfur-nitrogen-carbon removal of Pseudomonas sp. C27 under sulfide stress. 2368 98

Flooding negatively affects the growth of soybeans. Recently, omic approaches have been used to study abiotic stress responses in plants. To explore flood-tolerant genes in soybeans, an integrated approach of proteomics and computational genetic modification effectiveness analysis was applied to the soybean (Glycine max L. (Merrill)). Flood-tolerant mutant and abscisic acid (ABA)-treated soybean plants were used as the flood-tolerant materials. Among the primary metabolism, glycolysis, fermentation, and tricarboxylic acid cycle were markedly affected under flooding. Fifteen proteins, which were related to the affected processes, displayed similar protein profiles in the mutant and ABA-treated soybean plants. Protein levels of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aconitase 1, and 2-oxoglutarate dehydrogenase were higher in flood-tolerant materials than in wild-type soybean plants under flood conditions. These three proteins were positioned in each of the three enzyme groups revealed by our computational genetic modification effectiveness analysis, and the three proteins configured a candidate set of genes to promote flood tolerance. Additionally, transcript levels of GAPDH were similar in flood-tolerant materials and in unstressed plants. These results suggest that proteins related to energy metabolism might play an essential role to confer flood tolerance in soybeans.
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PMID:An Integrated Approach of Proteomics and Computational Genetic Modification Effectiveness Analysis to Uncover the Mechanisms of Flood Tolerance in Soybeans. 2970 10