Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of key glycolysis enzymes (hexokinase, glucose-6-phosphatase, phosphofructokinase, fructose-diphosphatase and ketose-1-phosphate aldolase) in the kidney tissue and its subcellular structures was studied in normal rats and in rats with experimental acute renal insufficiency. It is established that considerable biochemical changes in the kidney tissues affecting all the elements of cellular structures occur under acute lesion of the kidneys. The activity of the enzymes under study under acute renal insufficiency lowers to a greater extent in those subcellular structures of the kidneys where they are mainly localized. The arising disturbances in permeability of the kidneys cellular membranes intensify the release of the mentioned enzymes to blood serum and urine, that in its turn disturbs the coordination of certain glycolysis stages.
 ...
PMID:[Activity of glycolysis key enzymes in subcellular structures of normal kidneys and under acute renal insufficiency]. 22 62

The Clarke-Carbon clone bank carrying ColE1-Escherichia coli DNA has been screened by conjugation for complementation of glycolysis and hexose monophosphate shunt mutations. Plasmids were identified for phosphofructokinase (pfkA), triose phosphate isomerase (tpi), phosphoglucose isomerase (pgi), glucose-6-phosphate dehydrogenase (zwf), gluconate-6-phosphate dehydrogenase (gnd), enolase (eno), phosphoglycerate kinase (pgk), and fructose-1,6-P2 aldolase (fda). Enzyme levels for the plasmid-carried gene ranged, for the various plasmids, from 4- to 25-fold the normal level.
 ...
PMID:ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. 36 27

Several glycolytic enzymes were observed to have between 40-90% of their activities associated with the particulate fractions of lysed nerve endings. The enzymes showing high particulate activity in lysed nerve endings were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), glucosephosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-phosphate dehydrogenase (EC 1.2.1.12), pyruvate kinase (EC 2.7.1.40) and lactate dehydrogenase (EC 1.1.27). With the exception of phosphofructokinase, 80% or more of the particle associated activity of each enzyme was solubilized by salt treatment indicating the association with particles was ionic. Sub-fractionation of lysed nerve endings showed hexokinase and fumarase (EC 4.2.1.2) had the highest specific activity in the same fractions which is consistent with observations indicating that hexokinase is associated with mitochondria. The other glycolytic zymes having high particulate activity, aldolase, glucosephosphate isomerase, phosphofructokinase, glyceraldehyde-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase, showed enrichment in fractions containing synaptosomal membranes, i.e. the fractions having highest specific activity of acetylcholinesterase (EC 3.1.1.7) and (Na+ + K+)-ATPase (EC 3.6.1.3).
 ...
PMID:Association of glycolytic enzymes with particulate fractions from nerve endings. 62 35

Evidence is presented that the antitumor agent helenalin, a sesquiterpene lactone, suppresses anaerobic glycolytic enzymes of tumor cells at a number of sites and not exclusively at glycogen synthetase and phosphofructokinase, previously proposed sites for inhibition by alpha-methylene-gamma-lactones. Of the enzymes tested, the sulfhydryl-containing enzyme hexokinase was inhibited the maximum, i.e., 83%, by helenalin treatment, whereas phosphofructokinase and glycogen synthetase were suppressed approximately 45%. Another sulfhydryl-bearing enzyme, aldolase, was decreased approximately 43%. Phosphorylase a was inhibited 65%, glucose-6-phosphatase was inhibited 46%, and succinic dehydrogenase was inhibited 59% by helenalin treatment. Mitochondrial oxidative phosphorylation processes were also significantly depressed in the presence of helenalin in vitro with either succinate or alpha-ketoglutarate as substrates. Thus, a number of enzymes of anaerobic and aerobic carbohydrate metabolism of Ehrlich ascites cells appear to be inhibited by helenalin, which supposedly can alkylate functional groups, e.g., sulfhydryl groups of these enzymes, by a rapid Michael-type addition.
 ...
PMID:Antitumor agents XXVII: Effects of helenalin on anaerobic and aerobic metabolism of Ehrlich ascites cells. 64 68

Others have concluded that beta-fructose 1, 6-bisphosphate is a substrate for muscle aldolase on the basis of rapid kinetic measurements. In view of new data showing excellent aldol cleavage of an analog of the keto form and a very high rate of spontaneous ring opening, Midelfort et al. (Midelfort, C. F., Gupta, R., and Rose, I.A. (1976) Biochemistry 15, 2178-2185) have suggested that the beta form may be used only after spontaneous conversion to the keto form in solution, followed by reaction of the keto form with the aldolase. In order to determine whether beta-fructose-1, 6-P2 is itself a substrate a steady state approach was devised in which the beta form is specifically produced by phosphofructokinase for use by the aldolase present. Since aldolase binds very tightly to bisphosphates similar in size to beta-fructose-1, 6-P2, it was expected that if a spontaneous ring opening were essential for catalysis, it would be possible to decrease the rate of production of triose-Ps by using very high concentrations of aldolase. If the beta form were itself a substrate, the rate would reach a constant value with increasing aldolase, limited by the phosphofructokinase rate. It was found that under conditions where only approximately 2 per cent of the total fructose-1, 6-P2 present in the steady state would be free, the turnover of the complexed fructose-1, 6-P2 was about 20-fold greater than that in which spontaneous ring opening is a required step. Using similar methods, the turnover of enzyme-bound glyceraldehyde-P and dihydroxyacetone-P were determined. It was concluded that at saturation both the beta and acyclic forms have about the same rates as substrates.
 ...
PMID:Specificity of fructose-1, 6-P2 aldolase (muscle) and partition of the enzyme among catalytic intermediates in the steady state. 83 39

In 38 patients with chronic renal insufficiency of different degree of severity examinations of the stationary concentration of the adenine nucleotides in the erythrocytes were carried out. It was shown that in the red blood cells of uraemics a genuine increase of the concentration of these compounds occurs, in which case the adenosine triphosphate dominates absolutely as well as relatively. In individual cases erytho-cyctic ATP-values of more than 3 micron mol pro ml cells may be achieved. The increase of the ATP-concentration in the red blood cells correlates with the degree of severity of the renal insufficiency and the renal anaemia. The hyperphosphataemia occurring as a rule in renal insuficiency is of causal importance for the increase of ATP. By a consecutive increase of the intracellular phosphate level and by influence on different steps of enzymes (phosphofructokinase, aldolase, glycerin aldehyde phosphate dehydrogenase) and changed regulations it effected an activation of the glycolysis. The increase of the plasma adenine and plasma adenosine concentration plays apparantly an accessory role for the increase of the concentration of the adenine nucleotides existing in the erythrocytes. Together with an increased concentration of 2,3-diphosphogycerate (2,3-DPG) the increase of the ATP-level has an effect on the oxygen transport function function of haemoglobin in the sense of a facilitation of the O2-output. These processes explain the relative adaption of patients with chronic renal insufficiency to renal anaemias of partly high degree.
 ...
PMID:[Adenine nucleotide- and 2,3-diphosphoglycerate metabolism in human erythrocytes in chronic kidney insufficiency]. 84 44

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.
 ...
PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72

Ectothiorhodospira shaposhnikovii, Chromatium minutissimum and Thiocapsa roseopersicina were grown in the dark under anaerobic conditions on media containing glucose or fructose and organic acids. Their cell contained the following enzymes of the fructose diphosphate pathway: phosphofructokinase, fructose diphosphate aldolase, and 3-phosphoglyceraldehyde dehydrogenase. The activity of fructose diphosphate aldolase was higher in the cells grown in the dark than in the cells grown in the light. The same enzymes of the tricarboxylic acid cycle were found in the cells cultivated in the dark on media containing organic acids as in the cells grown in the light, though the activity of some enzymes was lower. Only the activity of isocitrate lyase increased in the cells cultivated in the dark on a medium containing acetate.
 ...
PMID:[Carbohydrate metabolism enzymes of purple sulfur-bacteria during growth in the dark]. 88 7

Activities of leucylaminopeptidase, aspartyl aminopeptidase, gamma-glutamyl transpeptidase, oxytocinase, phosphohexoisomerase, phosphofructokinase and aldolase were studied in amniotic cells from cases of pregnancy complicated by threatening intrauterine fetal asphyxia. Leucylaminopeptidase and oxytocinase activities were much higher in the group of pregnancies complicated by threatening fetal asphyxia than in the control group. It was concluded that elevated activity of the aforementioned enzymes in cells of the amniotic fluid from pregnancies complicated by threatening intrauterine asphyxia is due to acute hypoxia of the fetus.
 ...
PMID:Activities of some peptidases and glycolytic enzymes in cells of the amniotic fluid. II. Pregnancies complicated by threatening intrauterine fetal asphyxia. 88 30

Fifteen red cell enzyme activities of growth-retarded patients with and without growth hormone (GH) deficiency were investigated before and after GH administration. The 15 enzymes were Hexokinase, phosphoglucomutase, glucose phosphate, isomerase, phosphofructokinase, fructose diphosphate aldolase, glyceraldehyde-3-phosphae dehydrogenase, triosephosphate isomerase, 2,3-diphosphoglycerate mutase, 3-phosphoglycerate kinase, 3-phosphoglycerate mutase, enolase, pyruvate kinase, glycose-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase, glutathione reducase. Sixty-six subjects were studied: 30 normal control subjects (group N) and 36 patients (aged 5-23 years) with short stature. Complete endocrine evaluation showed 21 (group I) to have GH deficiency (10 patients with isolated GH deficiency) and 15 (group II) to have normal hypothalamic and pituitary function except for two patients with a moderate hypothyroidism. Both had been receiving thyroid hormone treatment for a long time before our studies. All 36 patients were treated with 2 mg human growth hormone intramuscularly for 7 days. Before GH treatment no significant difference was observed between hematologic data in group I (GH deficiency) and group II (no GH deficiency). After GH therapy there was a significant increase in reticulocyte count in both groups of patients with short stature. The mean pretreatment value in group I was 1.294% +/- 0.084 (SEM); the mean post-treatment value was 2.081% +/- 0.287 (SEM)< P less than 0.005. The mean pretreatment value in group II was 1.0% 0.184 (SEM); the mean post-treatment value was 1.407% +/- 0.193 (SEM), P less than 0.01. In group II (no GH deficiency) mean pretreatment erythrocyte enzyme activities were not significantly different from those activities observed in normal control subjects (group N). However, in patients who lacked GH, the pretreatment activities of five red cell enzymes (glucose phosphate isomerase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, 2,3-diphosphoglycerate mutase, 3-phosphoglycerate kinase) were significantly decreased before GH administration compared with the values in normal control subjects...
 ...
PMID:Action of growth hormone on erythropoiesis: changes in red blood cell enzyme activities in growth-retarded patients with and without growth hormone deficiency. 95 53


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>