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:1.1.1.41 (isocitrate dehydrogenase)
3,101 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tetrahymena pyriformis Wh 14 was grown in Erlenmeyer flasks under continuous stirring at 30 degrees C for three days . After the culture had produced dry matter of about 100 mg HCB was added in acetone at a dose level of 0, 0.001, 0.1 and 1.0 ppm to the culture and incubated for another 7 days. At a dose level of 0.001 ppm the activity of delta-aminolevulinate dehydratase, hexokinase, and pyruvate kinase remained unaffected but was increased for glutamic-oxaloacetic transaminase, glutamic dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase while 0.1 ppm HCB increased the activity of all enzymes studied, the only exception being glutamic-pyruvic transaminase, the activity of which was depressed by HCB exposure. A concentration of 1.0 ppm HCB depressed the activity of most of the enzymes below control values with the exception of the two mitochondrial enzymes, MDH and ICDH, studied here.
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PMID:Effect of hexachlorobenzene (HCB) on the activity of some enzymes from Tetrahymena pyriformis. 10 53

The content of the Krebs cycle substrates and activity of dehydrogenases corresponding to them were studied in the brain and myocardium tissues of the non-linear male rats adapted to acute hypoxia under conditions of the altered gas medium. The content of malate and succinic acid was studied in the liver and skeletal muscles only. In the brain the total activity of malate dehydrogenase (MDH, EC 1.1.1.37, 1.1.1.39) alpha-ketoglutarate dehydrogenase (KDH, EC 1.2.4.2) pyruvate dehydrogenase (PDH, EC 1.2.4.1) and isocitrate dehydrogenase (ICDH, EC 1.1.1.41-42) is shown to be decreased and kept to be lowered in all the periods of the study. No essential shifts in the activity of these dehydrogenases were found in the myocardium. The activity of succinate dehydrogenase (SDH, EC 1.3.99.1) in both tissues lowers 48 h after the effect of the mentioned factors. Simultaneously the greatest changes in the level of the substrates were observed in the myocardium, in the brain they were less developed. In the liver the content of malate increases without pronounced changes in the amount of succinic acid and in the skeletal muscles the level of malate and succinic acid lowers.
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PMID:[Krebs cycle in tissue of rats subjected to combined effect of hypercapnia, hypoxia and cooling]. 121 51

Seven-day exposure to clinostatic and antiorthostatic hypokinesia led to a significant decrease of Krebs cycle enxymes (malate dehydrogenase--MDH and isocitrate dehydrogenase) and creatine phosphokinase with no significant changes in lactate dehydrogenase (LDH), aspartate aminotransferase, alanine aminotransferase and MDH and LDH isoenzymes. This hypofermentemia returned to normal during 7-day readaptation. It was not associated with hemodynamic changes or emotional stress. The hypofermentemia was adaptive and induced by diminished motor activity.
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PMID:[Effect of clinostatic and anti-orthostatic hypokinesia on serum enzyme activity]. 322 98

Fetuses were decapitated in one uterine horn in each of 14 sows at 45 d of gestation. Control (C) and decapitated (D) fetuses were removed by Caesarean section from three sows at 65 d of gestation (total of 10 D and 10 C fetuses), two sows at 85 d (six D and six C fetuses) and nine sows at 110 d (nine C and nine D fetuses) of gestation (Exp. 1). In Exp. 2, four to six fetuses were removed from each of two Ossabaw (O) gilts and three crossbred (C, Landrace X Yorkshire) gilts at 70 d of gestation, from three C and O gilts at 90 d of gestation and from three C and two O gilts at 110 d of gestation. In Exp. 1, one semitendinosis muscle was removed for histochemistry, whereas the contralateral muscle was removed and weighed. A medial portion of biceps femoris muscle was removed and used for histochemistry in Exp. 2. In both experiments, transverse sections (cryostat) of muscle were stained for lipid, glycogen (PAS) and the following enzymes: acid ATPase, NADH-TR, NADPH-TR, malate dehydrogenase (NAD- and NADP-dependent reactions; MDH), succinate dehydrogenase (SDH), alpha-glycerol phosphate dehydrogenase (with and without NAD; alpha-GPDH), isocitrate dehydrogenase (NAD dependent; ICDH), esterase, lipoprotein lipase and lipase. In Exp. 1, body and muscle weights of the two groups were not significantly different (P greater than .05) at 65 d of gestation, whereas D fetuses were smaller and had lighter weight muscles (P less than .05) at 85 d of gestation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme histochemical studies in an ontogeny study of muscle development in Ossabaw and decapitated fetuses: cellular reactions. 401 46

The study of 165 rats exposed to 60-day hypokinesia demonstrated a decrease in the quantity of mitochondrial protein and a decline in the activity of mitochondrial forms of NADP-isocitrate dehydrogenase (NADP-ICDH) and NAD-malate dehydrogenase (NAD-MDH), as well as NAD-ICDH, succinate dehydrogenase (SDH) and alpha-ketoglutarate dehydrogenase (alpha-KGDH). The maximum decline in the protein content was seen on day 60, and in the enzyme activity on day 7. As the hypokinetic exposure continued, the activity of mitochondrial NAD-MDH and NADP-ICDH slightly increased. The NADP-MDH activity decreased only at later stages of hypokinesia. The changes in cytoplasmic NAD-MDH, NADP-ICDH and NADP-MDH were less expressed. On day 25 of the recovery period the activity of NAD-ICDH and NADP-ICDH was significantly higher than in the controls, that of mitochondrial NAD-MDH returned to the normal, and the activity of SDH and alpha-KGDH remained noticeably lowered.
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PMID:[Oxidative enzyme activity of the tricarboxylic acid cycle in rat skeletal muscles in hypokinesia]. 717 3

Exposure to simulated weightlessness (7-day water immersion and 7-day head-down tilt) caused a decrease in the activity of malate (MDH) and isocitrate dehydrogenase (ICDH), and creatine phosphokinase dehydrogenase (ICDH), and creatine phosphokinase (CPK) at the expense of its MM isoform whereas the activity of alanine (ALT) and aspartate aminotransferase (AST) and pattern of distribution of MDH isoforms remained unchanged. Exposure to acceleration of +3 Gz before and after simulated weightlessness revealed similar changes in the activity of MDH, ICDH, ALT, AST and MDH cytoplasmic fractions. However, the higher increase in the enzyme activity after simulated weightlessness may give evidence for a greater change in cell membrane permeability during acceleration effects that followed simulated weightlessness.
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PMID:[Energy-metabolism enzymes during combined exposure of the body to simulated weightlessness and gravitational overloads]. 728 61

Physiological concentrations [< 11 mM] of formate do not violate the metabolism of S. bovis and M. elsdenii. A significant inhibition is caused by concentrations of 22 and 44 mM. In this case the process of ammonia formation in S. bovis is inhibited more pronouncedly. Peculiar effects of formate (11 mM) on LDH, FDH, aconitase, isocitrate dehydrogenase, fumarase, L-MDH and malic-enzyme have been stated. The changes show that it enhances assimilation of sugars fermented to lactate in S. bovis, in contrast to M. elsdenii, where it activates the utilization of lactic acid. During the log-phase S. bovis utilized only 11.5% of [14C] H2O2, whereas M. elsdenii uses 33.4% of it. The major amount of the label is transferred from intracellular inclusions to nucleic acids (in S. bovis--74.7%, in M. elsdenii--87%) and then incorporated into low molecular substances (23.5 and 11.9%, respectively), the rest being incorporated into proteins and lipids.
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PMID:[Formate metabolism by lactate-producing and lactate-utilizing rumen bacteria]. 787 87

Indian River male broiler chickens growing from 7 to 28 d of age were fed on diets containing 120, 210 and 300 g crude protein/kg diet and 0, 1.67 or 16.7 g added tryptophan (TRP)/kg diet. The hypothesis tested was that crude protein levels and TRP would affect both growth and neurotransmitter metabolism. Heart, brain and pancreatic neurotransmitter (noradrenaline (NA), dopamine (DA), serotonin (5-HT) and 5-hydroxy-indole-3-acetic acid (5-HIAA)) concentrations were determined by HPLC separation and electrochemical detection. Malate dehydrogenase (2-oxoglutarate decarboxylating) (NADP+) (MDH(NADP+); EC 1.1.1.40), isocitrate dehydrogenase (NADP+) (ICD(NADP+); EC 1.1.1.42) and aspartate aminotransferase (AAT; EC 2.6.1.1) activities were also measured. Supplemental TRP decreased growth and feed intake. Increasing dietary crude protein decreased MDH(NADP+), but increased (ICD(NADP+) and AAT activities. Additional dietary TRP decreased MDH(NADP+) activity, but had no effect on other enzyme activities. Cardiac NA concentrations were directly related to dietary crude protein levels while pancreatic levels were inversely related. An increase in dietary crude protein decreased both brain NA and DA. Supplemental dietary TRP increased both 5-HIAA and 5-HT. Changes in feed intake caused by different levels of both dietary crude protein and TRP are accompanied by altered levels of neurotransmitters. The present study indicates that much larger amounts of TRP are required to make simultaneous changes in feed intake and neurotransmitters.
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PMID:Crude protein and supplemental dietary tryptophan effects on growth and tissue neurotransmitter levels in the broiler chicken. 877 19

Ultraviolet (UV) radiation is one of the major risk factors of cataract (loss of eye-lens transparency). The influence of UVB radiation (300 nm; 100 microW cm-2) on the activity and apparent kinetic constants (Km and Vmax) of rat lens hexokinase (HK;EC 2.7.1.1), phosphofructokinase (PFK; EC 2.7.1.11), isocitrate dehydrogenase (ICDH; EC 1.1.1.41) and malate dehydrogenase (MDH; EC 1.1.1.37) of energy metabolism has been investigated by irradiating the lens homogenate of three- and 12-month-old rats. In the three-month-old group specific activities of HK and PFK are reduced by 56 and 43%, respectively, and there is no change in ICDH and MDH activities after a 24 h exposure. On the other hand, in the 12-month-old group the decreases are 72, 71, 24 and 16% for HK, PFK, ICDH and MDH, respectively. UVB irradiation increases the apparent Km of HK and PFK (in both age groups), whereas the Km of ICDH and MDH is not altered. While the decrease in Vmax of these enzymes due to UVB exposure is only marginal in three-month-old rats, it is more pronounced (significant) in 12-month-old rats. A similar decrease in enzyme activities of HK and PFK is also observed upon UVB exposure of the intact rat lens. The photoinduced changes in energy metabolism may in turn have a bearing on lens transparency, particularly at an older age.
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PMID:UVB irradiation alters the activities and kinetic properties of the enzymes of energy metabolism in rat lens during aging. 949 95

The effects of iron deficiency and iron resupply on the metabolism of leaf organic acids have been investigated in hydroponically grown sugar beet. Organic acid concentrations and activities in leaf extracts of several enzymes related to organic acid metabolism were measured. Enzymes assayed included phosphoenol pyruvate carboxylase (PEPC; EC 4.1.1.31), different Krebs cycle enzymes: malate dehydrogenase (MDH; EC 1.1.1.37), aconitase (EC 4.2.1.3), fumarase (EC 4.2.1.2), citrate synthase (CS; EC 4.1.3.7) and isocitrate dehydrogenase (ICDH; EC 1.1.1.42), glucose-6-phosphate dehydrogenase (G6PDH; EC 1.1.1.49) and two enzymes related to anaerobic metabolism (lactate dehydrogenase [LDH]; EC 1.1.1.27, and pyruvate decarboxylase [PDC]; EC 4.1.1.1). Iron concentration in leaves was severely decreased by iron deficiency. Iron resupply caused an increase in iron concentrations, reaching levels similar to the controls in 96 h. Iron deficiency induced a 2.3-fold (from 16 to 37 mmol m-2) increase in leaf total organic acid concentration. Organic anion concentrations were still 4-fold higher than the controls 24 h after resupply and decreased to values similar to those found in the controls after 96 h. All measured enzymes had increased activities in extracts of iron-deficient leaves when compared to the controls and generally decreased to control values 24 h after iron addition. These data provide evidence that organic acid accumulation in iron-deficient leaves is likely not due to an enhancement in leaf carbon fixation. Instead, this accumulation could be associated with organic acid export from the roots to the leaves via xylem.
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PMID:Changes induced by Fe deficiency and Fe resupply in the organic acid metabolism of sugar beet (Beta vulgaris) leaves. 1131 12


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