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Enzyme
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Query: EC:1.1.1.41 (
isocitrate dehydrogenase
)
3,101
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
After a brief exposition to glucose, Thiobacillus acidophilus was isolated from a culture of
iron
-grown T. ferrooxidans. Physicochemical analysis of its DNA showed a G+C content of 62.9-63.2%. The new isolate grows best at 25-30 degrees C and at pH 3.0. Growth is possible between pH 1.5 and 6.0. Thiobacillus acidophilus is apparently strictly aerobic. Ammonium salts are the only suitable source of nitrogen. The bacterium is a facultative autotroph. In addition to elemental sulfur, it obtains energy from organic compounds such as D-glucose, D-galactose, D-fructose, D-mannitol, D-xylose, D-ribose, D-arabinose, L-arabinose, sucrose, sodium citrate, malic acid,dl-aspartic acid, and dl-glutamic acid. Thiobacillus acidophilus possesses the key enzymes of the tricarboxylic acid (TCA) cycle including NAD-and NADP-linked
isocitric dehydrogenase
and alpha-ketoglutarate dehydrogenase, and the key enzymes of the hexose monophosphate pathway (glucose-6-phosphate and 6-phosphogluconate dehydrogenase, and fructose 1,6-diphosphate aldolase). NADH oxidase has been found in particulate fraction of extracts. Rhodanese and thiosulfate oxidase have also been detected.
...
PMID:Thiobacillus acidophilus sp. nov.; isolation and some physiological characteristics. 23 84
The possible involvement of Fe-S clusters in photodynamic reactions as endogenous sensitizing chromophores in cells has been investigated, by using an artificial non-heme
iron
protein (ANHIP) derived from bovine serum albumin and ferredoxins isolated from spinach and a red marine algae. Ferredoxins and ANHIP, when exposed to visible light, generate singlet oxygen, as measured by the imidazole plus RNO method. Irradiation with intense blue light of the ANHIP-entrapped liposomes caused severe membrane-damage such as liposomal lysis and lipid peroxidation. In the presence of ANHIP,
isocitrate dehydrogenase
and fructose-1,6-diphosphatase were photoinactivated by blue light. However, all of these photosensitized reactions were significantly suppressed by a singlet oxygen (1O2) quencher, azide, but enhanced by a medium containing deuterium oxide. Further, the Fe-S proteins with the prosthetic groups destroyed did not initiate the blue light-induced reactions. In addition, the action spectrum for 1O2 generation from ANHIP was very similar to the visible absorption spectrum of Fe-S centers. The results obtained in this investigation appear consistent with the suggestion that Fe-S centers are involved in photosensitization in cells via a singlet oxygen mechanism.
...
PMID:Iron-sulfur centers as endogenous blue light sensitizers in cells: a study with an artificial non-heme iron protein. 150 84
Early iron deficiency in rat does not affect the weight or the protein, DNA, and RNA content but results in a slight reduction in gamma-aminobutyric acid (GABA) (13%, p less than 0.01) and glutamic acid (20%, p less than 0.001) content of the brain. The activities of the two GABA shunt enzymes, glutamate dehydrogenase and GABA-transaminase, and of the NAD+-linked
isocitrate dehydrogenase
(ICDH) were inhibited whereas the glutamic acid decarboxylase, mitochondrial NADP+-linked ICDH, and succinic dehydrogenase activities remained unaltered in brain. On rehabilitation with the
iron
-supplemented diet for 1 week, these decreased enzyme activities in brain attained the corresponding control values. However, the hepatic nonheme
iron
content increased to about 80% of the control, after rehabilitation for 2 weeks. A prolonged iron deficiency resulting in decreased levels of glutamate and GABA may lead to endocrinological, neurological, and behavioral alterations.
...
PMID:Effect of early iron deficiency in rat on the gamma-aminobutyric acid shunt in brain. 287 Nov 28
It has been reported that the mitochondrial cytochromes and citrate cycle enzymes occur in constant proportions to each other and increase or decrease roughly in parallel in response to various stimuli. The purpose of this study was to determine whether this proportionality is an obligatory consequence of the way in which mitochondria are assembled. Severe iron deficiency was used to bring about decreases of the
iron
-containing constituents of the mitochondrial respiratory chain in skeletal muscle. Cytochrome c concentration and cytochrome oxidase activity were decreased approximately 50%, while succinate dehydrogenase and NADH dehydrogenase activities were decreased by 78% in
iron
-deficient muscle. On electron microscopic examination, mitochondria in
iron
-deficient muscles had relatively sparse numbers of cristae. The iron deficiency had little or no effect on the levels of a range of mitochondrial matrix enzymes, including citrate synthase,
isocitrate dehydrogenase
, fumarase, aspartate aminotransferase, 3-hydroxyacyl-CoA dehydrogenase, 3-ketoacid-CoA transferase, and acetoacetyl-CoA thiolase. These results show that the usual constant proportions between the constituents of the mitochondrial respiratory chain and matrix enzymes are not obligatory; they provide evidence that mitochondrial matrix enzymes and respiratory chain constituents can be incorporated into mitochondria independently and that the ratios between them can vary within wide limits.
...
PMID:Perturbation of mitochondrial composition in muscle by iron deficiency. Implications regarding regulation of mitochondrial assembly. 302 53
Young rats maintained on an
iron
-deficient diet developed severe anemia and had large decreases in the levels of the
iron
-containing flavoproteins and cytochromes of the mitochondrial respiratory chain in skeletal muscle. In contrast, the levels of a number of mitochondrial matrix marker enzymes, including citrate synthase,
isocitrate dehydrogenase
, 3-hydroxyacyl-CoA dehydrogenase, 3-ketoacid-CoA transferase, and aspartate aminotransferase, increased in red skeletal muscle but not in white muscle. Phosphocreatine concentration was decreased and inorganic phosphate concentration was increased in soleus muscle frozen in situ. We hypothesize that the increase in mitochondrial matrix enzymes reflects a stimulus to mitochondrial biogenesis in posture-maintaining and weight-bearing red muscle fibers in severely
iron
-deficient rats. It is our working hypothesis that this stimulus to mitochondrial biogenesis arises from mild activity of the red fibers and is due to the same perturbation in cellular homeostasis that is normally caused by vigorous exercise or hypoxia. In iron deficiency, the stimulus to mitochondrial biogenesis can induce an increase in only those enzymes not prevented from increasing by iron deficiency, resulting in formation of mitochondria of grossly abnormal composition.
...
PMID:Induction of an increase in mitochondrial matrix enzymes in muscle of iron-deficient rats. 347 8
In porcine areolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase,
isocitrate dehydrogenase
(NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that the enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an
iron
-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and
iron
transport.
...
PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41
Cellular metabolism and, in particular, oxidation-reduction systems are linked to responses to drugs and toxic agents in several ways. Major connections are given by the NADPH/NADP+ system and the GSH/GSSG system. Intracellular reductive pathways generally use NADPH as the electron donor. From a toxicological point of view, NADPH can be considered both as a "detoxicant" and as a "toxicant". In the former case, NADPH supports the glutathione redox cycle by maintaining a negative redox potential of GSH to permit its detoxication functions to occur. NADPH is also the main donor for reducing equivalents in drug oxidations by the cytochrome P-450-dependent monooxygenase system which, with some notable exceptions, serves important purposes in detoxication. The sources of NADPH reducing equivalents depend on the nutritional state: major sources in the fed state are represented by the cytosolic pentose phosphate shunt dehydrogenases, whereas mitochondrial sources linked to
isocitrate dehydrogenase
provide the bulk of NADPH reducing equivalents in the fasted state. As a "toxicant", NADPH supports redox cycling reactions involving various drugs and other compounds of quinoid structure, aromatic nitro compounds and
iron
chelates with formation of superoxide anion radicals and subsequent formation of other oxygen derived radical species. This presentation focuses on recent work carried out with isolated hepatocytes and perfused rat liver with respect to "oxidative stress". The noninvasive techniques of measurement of low-level chemiluminescence and of volatile hydrocarbons (ethane, pentane) as well as glutathione release and calcium release have been employed.
...
PMID:Cellular redox changes and response to drugs and toxic agents. 635 19
Reference intervals for some clinical chemistry parameters in the marmoset were calculated. The effects of age (250-300 days compared with 500-550 days) and sex on the values found was investigated. Alkaline phosphatase levels decreased with age, young males having higher plasma levels than young females, but no sex differences were discernible for older animals. Levels of gamma-glutamyl transpeptidase and sorbitol dehydrogenase were higher in older males than in younger females. Higher plasma
iron
levels were found in the males with increasing age. Age and sex effects for protein and albumin were interactive and further interpretation was therefore difficult. No significant age or sex effects were seen for cholinesterase, acetylcholinesterase,
isocitrate dehydrogenase
, malate dehydrogenase, lactate dehydrogenase, glutamate dehydrogenase, aspartate amino transferase, alanine aminotransferase or bilirubin.
...
PMID:Reference intervals for some clinical chemical parameters in the marmoset (Callithrix jacchus): effect of age and sex. 643 Nov 85
The effect of
iron
-deficiency anaemia and
iron
supplementation on the enzyme profile and conversion of specifically labelled glucose to 14CO2 and 14C-lipid was measured in rat adrenal glands. Enzymes involved in lipogenesis were severely depressed in iron deficiency, addition of Fe2+ to the diet resulted in increased activity of fatty acid synthetase (+75%), NADP
isocitrate dehydrogenase
(+466%), glucose-6-phosphate dehydrogenase (+27%) and malic enzyme (+46%). Parallel increases occurred in the flux of glucose into lipid. The effects of
iron
-deficiency anaemia on adrenal and thyroid function in relation to developmental processes are discussed.
...
PMID:Bio-inorganic regulation of pathways of carbohydrate and lipid metabolism. II. The effect of iron-deficiency on the profile of enzymes in the developing rat adrenal gland. 707 81
A new enzymatic method for assaying
iron
in serum samples, suitable for automated analyzers, is reported. Three reagent mixtures are used: dilution buffer (pH 3.0; ascorbate), reagent 1 (pH 6.7; apoaconitase), and reagent 2 (pH 7.7; citrate, magnesium, and
isocitrate dehydrogenase
). Sera are diluted with dilution buffer. Fe3+ is liberated from transferrin in sera under acidic conditions, and then reduced by ascorbate. Reagent 1 is added to diluted specimens, and apoaconitase is reactivated by Fe2+ at neutral pH. The resulting solutions are mixed with reagent 2, so that holoaconitase hydrolyzes citrate to isocitrate and the isocitrate and NADP+ are converted to 2-oxoglutarate, NADPH, and CO2. Serum
iron
is determined linearly up to 70 mumol/L, with within-run CVs < or = 2.4% and day-to-day CVs < or = 2.9%. This method (y) gives results correlating with those of a Reference Method (x) proposed by the International Committee for Standardization in Haematology: y = 0.98x + 0.38 mumol/L (n = 72, r = 0.996, Sylx = 0.63 mumol/L). The mean (+/- SD) serum
iron
concentrations measured by our method were 18.5 +/- 5.4 and 15.2 +/- 6.0 mumol/L for 63 males and 166 females, respectively.
...
PMID:New enzymatic assay of iron in serum. 817 49
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