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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of estradiol-17 beta on the activities of glycolytic enzymes from female rat brain was studied. The following enzymes were examined: hexokinase (HK, EC 2.7.1.1), phosphofructokinase (PFK, EC 2.7.1.11), aldolase (EC 4.1.2.13), glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12), phosphoglycerate kinase (EC 2.7.2.3), phosphoglycerate mutase (EC 2.7.5.3), enolase (EC 4.2.1.11) and pyruvate kinase (PK, EC 2.7.1.40). The activities of HK (soluble and membrane-bound), PFK and PK were increased after 4 h of hormone treatment, while the others remained constant. The changes in activity were not seen in the presence of actinomycin D. The significant rise of the activities of the key glycolytic enzymes was also observed in the cell culture of mouse neuroblastoma C1300 treated with hormone. Only three of the studied isozymes, namely, HKII, B4 and K4 were found to be estradiol-sensitive for HK, PFK and PK, respectively. The results obtained suggest that rat brain glycolysis regulation by estradiol is carried out in neurons due to definite isozymes induction.
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PMID:Rat brain glycolysis regulation by estradiol-17 beta. 153 2

We have studied the effect of T3 administration (50 micrograms/Kg/day) on the phenotype expression of several glucose-metabolizing enzymes (hexokinase, HK, glucose-6-phosphate dehydrogenase, G6P-DH, aldolase, ALD, phosphofructokinase, PFK, lactate dehydrogenase, LDH) in the different myocardial layers of the left ventricle wall. In the control rats, most of these enzyme activities are uniformly distributed across the left ventricle wall, G6P-DH being the only exception. In the rats given T3 for 14 days, the mean levels of PFK, HK and ALD activities increased significantly. With regard to the transmural distribution patterns, that of PFK was unchanged, unlike those of HK and ALD which exhibited their maximum increase in activity in the midmyocardium or in the mid- and subepicardial myocardium. With LDH, a significant increase in activity was found in the subepicardial layers which escaped detection on the whole homogenate. It is concluded that the administration of thyroid hormone has different effects on enzyme phenotype expression of cardiomyocytes in different regions of the cardiac wall.
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PMID:Regional differences in the response of cardiac cells to triiodothyronine administration across the left ventricle free wall of rat heart. 231 6

Exposure of foundry workers to mixtures of different heavy metals is a very important toxicological problem. In this paper the estimation of the effects of lead, zinc, and copper on erythrocyte metabolism is presented. Concentrations of copper and zinc at work posts of the group examined did not exceed TLV, while lead concentration was 1.5 to 4 times higher than TLV. Erythrocyte metabolism was measured through activities of such glycolytic pathway enzymes as PFK, PGI, PK, aldolase and G6-PD from the hexose monophosphate pathway. Additionally the free erythrocyte protoporphyrin (FEP) level, D-ALA activity, serum GSH level, 2,3 DPG level in erythrocytes and lactic acid production during a 2-h incubation of red blood cells (RBC) was estimated. The blood-lead level, FEP level, copper concentration in erythrocytes in exposed group were significantly higher than in control group while the zinc level in erythrocytes was significantly lower. Measuring erythrocyte metabolism we showed that the activity of PGI, PFK, aldolase, lactic production and 2,3 DPG levels was significantly higher in the exposed group, probably as a result of anaerobic glycolysis activation.
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PMID:Influence of heavy metal mixtures on erythrocyte metabolism. 234 40

The age-related changes in the activities of five glucose-metabolizing enzymes (hexokinase, HK; glucose-6-phosphate dehydrogenase, G6P-DH; aldolase, ALD; phosphofructokinase, PFK; and lactate dehydrogenase, LDH) were investigated in the walls of left and right ventricles of rats of various age-groups (1-24 months). Age-related changes were found in the activities of all of the enzymes in both ventricles during growth (with significant decreases between 2 and 6 months of age) and in the levels of PFK and LDH in the left ventricle during ageing (with a significant increase between 12 and 24 months of age). The distribution of the enzyme activities across the wall of both ventricles was quite uniform in young, adult and mature rats (the distribution of G6P-DH activity in the left ventricle wall at 2 months of age was the only notable exception) but became non-uniform in the old rats with regard to G6P-DH, PFK, LDH and probably HK in the left ventricle and G6P-DH and HK in the right ventricle. These data support the hypothesis that alterations connected with ageing do not lead to a generalized decline of cardiac metabolic capacity, and that they are also the result of specific adaptive modifications, perhaps related to alteration in the distribution of the work load and/or of nutrition across the ventricular wall.
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PMID:Changes in the transmural distribution of glucose-metabolizing enzymes across the left and right ventricular wall of rat heart during growth and ageing. 296 12

Eight enzymes, e.g. lactate dehydrogenase, malate dehydrogenase, fructose-diphosphate aldolase, sorbitol dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were estimated quantitatively in the rat lens from 37 to 1,211 days of age, by spectrophotometric methods. The activity was expressed as mU/g LWW. All enzymes measured showed declining activities, but LDH, ALD, SDH, G-6-PDH, HK and PFK gave a significant decrease during ageing when plotted semi-logarithmically from 37 to 1,211 days. SDH and G-6-PDH showed a statistically significant difference between the enzymes from the male and the female lenses. The female lens always had a lower activity than the male lens. Of all enzymes the specific activity, expressed as mU/l mg protein, was calculated. This specific activity appeared to be rather constant during ageing, except for ALD. In the female lenses, the specific activity of 7 enzymes was lower than in the male lenses. For ALD the specific activity decreased significantly in the male lens from 5.32 at 37 days to 0.88 at 1,211 days. In the female lens this significant decrease was from 4.97 to 0.81.
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PMID:The quantification of eight enzymes from the ageing rat lens, with respect to sex differences and special reference to aldolase. 340 13

In investigating the influence of vibrational energy on the metabolism of the erythrocyte, it was hypothesized that under conditions of normal PaO2 and SaO2 in arterial blood, vibration induced vasoconstriction would decrease local blood flow and induce hypokinetic hypoxia. This decreased blood flow and therefore decreased delivery of oxygen to the tissue would markedly lower tissue PO2 (hypokinetic hypoxia), which would influence the energetics and metabolism of the erythrocyte. The metabolism of the red blood cell (RBC) was evaluated by measuring the enzymatic activities of PFK (2.7.1.11), PGI (5.3.1.9), PK (2.7.1.40), and aldolase (4.1.3.13) from the anaerobic glycolytic cycle and D-G-6-P (1.1.1.49) from the pentose cycle. Also measured were the levels of ATP and 2,3 DPG and the in-vitro production of lactic acid. In the group of workers showing early changes (vibration angioneurosis) associated with the vibration syndrome, changes in RBC metabolism were demonstrated. Statistically significant were increases of PFK, PK and the production of lactic acid, indicating the activation of anaerobic glycolysis. Furthermore statistically significant were the increased 2,3 DPG and decreased ATP levels.
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PMID:Effect of vibration on red cell metabolism. 623 27

Deficiencies in around 20 enzymes, associated with widely different degrees of severity and complexity, have been identified for human erythrocytes. The fact that glycolysis is crucial for erythrocyte function is reflected by the large number of inherited glycolytic enzymopathies. Triosephosphate isomerase (TPI) deficiency, a rare autosomal disease, is usually associated with nonspherocytic hemolytic anemia, progressive neurologic dysfunction, and death in childhood. The two affected Hungarian brothers studied by us have less than 3% TPI activity and enormously (30-50-fold) increased dihydroxyacetone phosphate (DHAP) concentration in their erythrocytes. The well-established concept of the metabolic control theory was used to test the contribution of TPI and some related enzymes to the control of a relevant segment of the glycolytic pathway in normal and deficient cells. Deviation indices, DEJ = (delta J/delta E) E(r)/J(r), which give a good estimation of flux control coefficients using a single large change in enzyme activity, were determined from the fluxes in the absence and presence of exogeneous enzymes. We found that PFK and aldolase are the enzymes that predominantly control the flux, however, the quantitative values depend extensively on the pH: DEJ values are 0.85 and 0.14 at pH 8.0 and 0.33 and 0.67 at pH 7.2 for aldolase and PFK, respectively. Neither the flux rates nor the capacities of the enzymes seem to be significantly different in normal and TPI deficient cells. There is a discrepancy between DHAP levels and TPI activities in the deficient cells. In contrast to the experimental data the theoretical calculations predict elevation in DHAP level at lower than 0.1% of the normal value of TPI activity. Several possibilities suggested fail to explain this discrepancy. Specific associations of glycolytic enzymes to band-3 membrane proteins with their concomitant inactivation have been demonstrated. We propose that the microcompartmentation of TPI that could further decrease the reduced isomerase activity of the deficient cells, is responsible for the high DHAP level.
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PMID:Triosephosphate isomerase deficiency: predictions and facts. 894 78

The hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324, rather than the type strain VC16, was found to grow on starch and sulfate as energy and carbon source. Fermentation products and enzyme activities were determined in starch-grown cells and compared to those of cells grown on lactate and sulfate. During exponential growth on starch, 1 mol of glucose-equivalent was incompletely oxidized with sulfate to approximately 2 mol acetate, 2 mol CO2 and 1 mol H2S. Starch-grown cells did not contain measurable amounts of the deazaflavin factor F420 (<0.03 nmol/mg protein) and thus did not show the F420-specific green-blue fluorescence. In contrast, lactate (1 mol) was completely oxidized with sulfate to 3 mol CO2 by strain 7324, and lactate-grown cells contained high amounts of F420 (0.6 nmol/mg protein). In extracts of starch-grown cells, the following enzymes of a modified Embden-Meyerhof pathway were detected: ADP-dependent hexokinase (ADP-HK), phosphoglucose isomerase, ADP-dependent 6-phosphofructokinase (ADP-PFK), fructose-1,6-phosphate aldolase, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase (GAP:FdOR), phosphoglycerate mutase, enolase, and pyruvate kinase (PK). Specific activities of ADP-HK, ADP-PFK, GAP:FdOR, and PK were significantly higher in starch-grown cells than in lactate-grown cells, indicating induction of these enzymes during starch catabolism. Pyruvate conversion to acetate involved pyruvate:ferredoxin oxidoreductase and ADP-forming acetyl-CoA synthetase. The findings indicate that the archaeal sulfate reducer A. fulgidus strain 7324 converts starch to acetate via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). This is the first report of growth of a sulfate reducer on starch, i.e. on a polymeric sugar.
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PMID:Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and CO2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). 1170 74

The effect of sodium acetate was studied on the change of the growth yield, the production of L- and D-lactic acid, and the activity of lactate dehydrogenases (LDHs; L-lactate dehydrogenase [EC 1.1.1.27, L-LDH] plus D-lactate dehydrogenase [EC 1.1.1.28, D-LDH]), fructose-1, 6-bisphosphate aldolase [EC 4.1.2.13, FBP-aldolase], and phosphofructokinase [EC 2.7.1.11, PFK] of Lactobacillus sakei NRIC 1071(T) and Lactobacillus plantarum NRIC 1067(T). The growth yield of L. sakei NRIC 1071(T) was increased 1.6 times in the presence of sodium acetate compared with its absence. The activity of LDHs in L. sakei NRIC 1071(T) and L. plantarum NRIC 1067(T) was retained longer under the addition of sodium acetate in the reaction mixture. As a result, these strains produced much more lactic acid in the presence of sodium acetate compared with its absence. Furthermore, the activity of L-LDH in L. sakei NRIC 1071(T) cultivated in the presence of sodium acetate increased three times or more compared with the activity of the cells cultivated in its absence. Consequently, the type of stereoisomers of lactic acid produced by L. sakei shifted from the DL-type to the L-type because the ratio of L-lactic acid to D-lactic acid produced became larger with the addition of sodium acetate to culture media. This phenomenon was not observed in L. plantarum NRIC 1067(T). Further, the participation of lactate racemase is discussed from the viewpoint of the production of D-lactic acid by L. sakei.
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PMID:The effect of sodium acetate on the growth yield, the production of L- and D-lactic acid, and the activity of some enzymes of the glycolytic pathway of Lactobacillus sakei NRIC 1071(T) and Lactobacillus plantarum NRIC 1067(T). 1246 5

Previous work has shown that GAPDH (glyceraldehyde-3-phosphate dehydrogenase), aldolase, PFK (phosphofructokinase), PK (pyruvate kinase) and LDH (lactate dehydrogenase) assemble into a GE (glycolytic enzyme) complex on the inner surface of the human erythrocyte membrane. In an effort to define the molecular architecture of this complex, we have undertaken to localize the binding sites of these enzymes more accurately. We report that: (i) a major aldolase-binding site on the erythrocyte membrane is located within N-terminal residues 1-23 of band 3 and that both consensus sequences D6DYED10 and E19EYED23 are necessary to form a single enzyme-binding site; (ii) GAPDH has two tandem binding sites on band 3, located in residues 1-11 and residues 12-23 respectively; (iii) a PFK-binding site resides between residues 12 and 23 of band 3; (iv) no GEs bind to the third consensus sequence (residues D902EYDE906) at the C-terminus of band 3; and (v) the LDH- and PK-binding sites on the erythrocyte membrane do not reside on band 3. Taken together, these results argue that band 3 provides a nucleation site for the GE complex on the human erythrocyte membrane and that other components near band 3 must also participate in organizing the enzyme complex.
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PMID:Mapping of glycolytic enzyme-binding sites on human erythrocyte band 3. 1683 85


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