Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Modification by covalent FAD attachment to a histidine residue via an 8 alpha-(N3-histidyl)-riboflavin linkage occurs in several flavoenzymes. Among them is 6-hydroxy-D-nicotine oxidase (6-HDNO) of Arthrobacter oxidans and the flavoprotein subunits of the fumarate reductase and succinate dehydrogenase complex of Escherichia coli and other bacterial and eukaryotic cells. We found that 6-HDNO holoenzyme formation from apo-6-HDNO, monitored by [14C]FAD incorporation and increase in enzyme activity, can be mediated not only by phosphoenolpyruvate [Nagursky, H., Bichler, V. and Brandsch, R. (1988) Eur. J. Biochem. 177, 319-325], but also by one of the glycolytic intermediates glyceraldehyde-3-P, glycerate-3-P, or the intermediate in glycerol utilization by bacteria, glycerol-3-P. Apoflavoprotein of fumarate reductase and succinate dehydrogenase was obtained in an E. coli riboflavin-requiring strain (E. coli RR28rf) overexpressing the frdABCD or the sdhCDAB operon from the recombinant plasmids pGS39 and pGS141, respectively. In extracts obtained from these cells, flavoprotein flavinylation, analyzed as covalent [14C]FAD incorporation into the apoflavoprotein polypeptide by polyacrylamide gel electrophoresis and fluorography, was stimulated severalfold by the citric acid cycle intermediates citrate, isocitrate, succinate and fumarate. Our results suggest that covalent modification and thus activation of these enzymes is dependent on specific metabolic intermediates which may act as allosteric effectors in the reaction.
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PMID:Covalent cofactor binding to flavoenzymes requires specific effectors. 265 51

The possible significance of food composition connected with the alpha-glycerophosphate (alpha GP) shuttle, a putative metabolic pathway of energy dissipation, was investigated at the level of enzyme activities. Liver, adipose tissue, slow-twitch and fast-twitch muscle of weaned male Wistar rats fed ad libitum for seven and for forty weeks a normal-protein (NP), a low-protein (LP), and a high-fat (HF) diet were examined. No striking dietary influences on cytosalic (NAD-linked glycerophosphate dehydrogenase, glyceraldehyde-phosphate dehydrogenase) and mitochondrial (succinate dehydrogenase, cytochrome c oxidase) enzyme activities could be detected, but mitochondrial alpha-glycerophosphate dehydrogenase (m-GPDH) showed an about twofold increase of its activity in the liver of LP-fed animals after seven weeks. A relationship between the "gross efficiency of food energy utilization" and tissue m-GPDH levels could not be established in general. The proposed inducing effect of a LP diet on the magnitude of the GP shuttle observed in the liver of young and adult rats seems to be interconnected reciprocally with the degree of metabolic energy dissipation only under the conditions of growth. The calculated capacities of the alpha GP shuttle are compatible with the assumption of its function as an energy dissipating pathway which is restricted in its magnitude.
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PMID:Relations between enzyme activities connected with energy metabolism and parameters of food energy utilization in young and adult rats. Part 2. Enzyme activities related to alpha-glycerophosphate shuttle in various tissues. 368 15

The effects of physical training on skeletal muscle morphology and enzyme activities were compared in 10 male, type I diabetic subjects and 10 healthy, male, control subjects. The training program consisted of running for 45 min, three times per week for 8 wk. Muscle biopsies were obtained before and after the training period from the lateral portion of the gastrocnemius muscle. Pretraining maximal oxygen uptake was similar in the two groups (diabetic subjects 42 +/- 1 versus control subjects 43 +/- 2 ml X kg-1 X min-1), and the training resulted in an identical increase (+ 13%, P less than 0.01). Muscle capillarization (number of capillaries per muscle fiber) increased on the average in the control group (+ 14 +/- 4%, P less than 0.01), but was unchanged in the diabetic group (0 +/- 4%). Capillary density, expressed as number of capillaries per unit muscle cross sectional area, also increased on the average in controls (8 +/- 4%, P less than 0.05) but failed to do so in the diabetic patients (-8 +/- 6%, NS). The activities of the mitochondrial enzymes citrate synthase (+ 26-27%, P less than 0.01-0.05) and succinate dehydrogenase (+ 24-25%, P less than 0.05) increased significantly and similarly in the two groups, whereas training did not result in significant changes in the activities of the glycolytic enzymes 6-phosphofructokinase and glyceraldehyde-phosphate dehydrogenase. Glycemic control in the diabetic group did not improve with the training, as evaluated from hemoglobin A1 and home-monitored blood glucose.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Influence of physical training on formation of muscle capillaries in type I diabetes. 646 66

Phosphorylating glyceraldehyde-3-P dehydrogenase (GAPC-1) is a highly conserved cytosolic enzyme that catalyzes the conversion of glyceraldehyde-3-P to 1,3-bis-phosphoglycerate; besides its participation in glycolysis, it is thought to be involved in additional cellular functions. To reach an integrative view on the many roles played by this enzyme, we characterized a homozygous gapc-1 null mutant and an as-GAPC1 line of Arabidopsis (Arabidopsis thaliana). Both mutant plant lines show a delay in growth, morphological alterations in siliques, and low seed number. Embryo development was altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. The gapc-1 line shows a decrease in ATP levels and reduced respiratory rate. Furthermore, both lines exhibit a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, as well as increased reactive oxygen species levels. Transcriptome analysis of the gapc-1 mutants unveils a differential accumulation of transcripts encoding for enzymes involved in carbon partitioning. According to these studies, some enzymes involved in carbon flux decreased (phosphoenolpyruvate carboxylase, NAD-malic enzyme, glucose-6-P dehydrogenase) or increased (NAD-malate dehydrogenase) their activities compared to the wild-type line. Taken together, our data indicate that a deficiency in the cytosolic GAPC activity results in modifications of carbon flux and mitochondrial dysfunction, leading to an alteration of plant and embryo development with decreased number of seeds, indicating that GAPC-1 is essential for normal fertility in Arabidopsis plants.
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PMID:Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. 1882 81

Proteins synthesized within the endoplasmic reticulum (ER) are transported to the Golgi via coat protein complex II (COPII)-coated vesicles. The formation of COPII-coated vesicles is regulated by the GTPase cycle of Sar1. Activated Sar1 is recruited to ER membranes and forms a pre-budding complex with cargoes and the inner-coat complex. The outer-coat complex then stimulates Sar1 inactivation and completes vesicle formation. The mechanisms of forming transport carriers are well-conserved among species; however, in mammalian cells, several cargo molecules such as collagen, and chylomicrons are too large to be accommodated in conventional COPII-coated vesicles. Thus, special cargo-receptor complexes are required for their export from the ER. cTAGE5/TANGO1 complexes and their isoforms have been identified as cargo receptors for these macromolecules. Recent reports suggest that the cTAGE5/TANGO1 complex interacts with the GEF and the GAP of Sar1 and tightly regulates its GTPase cycle to accomplish large cargo secretion.
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PMID:Regulation of the Sar1 GTPase Cycle Is Necessary for Large Cargo Secretion from the Endoplasmic Reticulum. 2887 81