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)

Effect of three antiandrogens: cyproterone acetate (5 mg/day, sc), flutamide (5 mg/day, sc) and STS-557 (5 mg/day, po) and an estrogen, estradiol dipropionate (5 micrograms/day, sc) on some key enzymes of carbohydrate metabolism was investigated in adult rat epididymis and ventral prostate. Antiandrogens were administered for 21 days and estrogen for 14 days. All of them caused a significant decrease in the weight of epididymis, seminal vesicles and ventral prostate. A significant decrease in the specific activities of enzymes (hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, pyruvate kinase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) occurred only in the organs of estrogen treated rats; activities of some of the enzymes were lowered also in the prostate of STS-557 treated rats. Flutamide and cyproterone acetate were ineffective in this regard. The possible factors responsible for the ineffectiveness of synthetic antiandrogens in influencing epididymal metabolism are discussed.
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PMID:Effect of antiandrogens on some key enzymes of glycolysis in epididymis and ventral prostate of rat. 253 Jan 66

The interactions of several glycolytic enzymes with muscle myofibrils in imidazole-chloride buffer (pH 6.8, I 0.158) have been investigated by equilibrium partition studies. Results for aldolase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and phosphofructokinase are interpreted in terms of a myofibrillar capacity of 76 nmol/g protein and a single intrinsic association constant for each tetravalent enzyme with matrix sites. The existence of separate myofibrillar sites for aldolase and glyceraldehyde-3-phosphate dehydrogenase is established by demonstrating independence of the binding of each enzyme upon the presence of the other. Although this investigation provides further physicochemical support for myofibrillar adsorption of glycolytic enzymes in the cellular environment, its findings are incompatible with the proposition (B. I. Kurganov, N. P. Sugrobova, and L. S. Mil'man (1985) J. Theor. Biol. 116, 509-526) that the phenomenon reflects the formation of a specific multienzyme complex attached to the myofibril.
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PMID:Equilibrium partition studies of the myofibrillar interactions of glycolytic enzymes. 253 Sep 35

In the past few years, very rapid advances have been made in the field of red cell enzymopathies associated with hereditary nonspherocytic hemolytic anemia, particularly in molecular basis. Nucleotide sequence and amino acid sequence of normal human red cell enzymes have been clarified in phosphofructokinase, aldolase, triosephosphate isomerase, phosphoglycerate kinase, pyruvate kinase, diphosphoglycerate mutase, glucose 6-phosphate dehydrogenase, adenylate kinase and adenosine deaminase. Furthermore, in aldolase-, triosephosphate isomerase-, diphosphoglycerate mutase-, glucose 6-phosphate dehydrogenase-, and adenylate kinase deficiency, single nucleotide changes which cause single amino acid substitutions and finally hemolysis, have been found.
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PMID:Molecular basis of red cell enzymopathies associated with hereditary nonspherocytic hemolytic anemia. 256 Apr 52

Fatigue of isolated gastrocnemius muscles from R. pipiens leads to a marked increase in the proportion of phosphofructokinase bound to the particulate fraction and a decrease in the binding of lactate dehydrogenase, pyruvate kinase, creatine phosphokinase and glyceraldehyde-3-phosphate dehydrogenase. Only the proportion of aldolase bound to the particulate fraction was unaffected by fatigue. This pattern was unchanged when fatigued muscles were extracted at pH 6.5 rather than 7.5. Thus, muscle fatigue leads to opposite changes in the binding of the glycolytic enzymes.
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PMID:The effect of fatigue on the binding of glycolytic enzymes in the isolated gastrocnemius of Rana pipiens. 280 95

A simple procedure has been elaborated to screen for the calmodulin antagonist effect of drugs. A covalently attached fluorescent probe was used to monitor the binding of enzymes known as target enzymes to calmodulin. Moreover, the probe made it possible to recognize a new target enzyme, aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13), for calmodulin among glycolytic enzymes. The calmodulin antagonist trifluoperazine prevented or eliminated the complex formation between calmodulin and enzymes studied in reconstituted systems; the Ca channel blockers had no effect. The functional consequences of the effect of drugs on calmodulin-phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) interaction were investigated as well. Whereas trifluoperazine suspended the calmodulin-mediated hysteretic inactivation of phosphofructokinase, Ca channel blockers (verapamil and nifedipine) were ineffective. Fendiline (regarded as a Ca channel blocker) seems to act as a functional calmodulin antagonist. Its binding to calmodulin does not prevent the complex formation of phosphofructokinase and calmodulin, but within this ternary complex phosphofructokinase preserves or recovers its original activity measured in the absence of calmodulin. The possible molecular effect of drugs on a calmodulin-enzyme complex is discussed.
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PMID:Functional in vitro test of calmodulin antagonism: effect of drugs on interaction between calmodulin and glycolytic enzymes. 283 37

Past work, including our computer simulation of cardiac energy metabolism, indicates that magnesium is an important coherent controller of glycolysis and the Krebs cycle. Many of the glycolytic enzymes are sensitive to Mg2+. The most important effect is due to MgATP2-being a cofactor for a number of these enzymes while other chelation forms are inactive or inhibitory. The means by which Mg2+ and Mg2+ chelates of adenine nucleotides regulate the most important glycolytic enzymes--hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, and pyruvate kinase--are described in detail. Creatine kinase, which is important in energy metabolism and highly sensitive to both metal ions and pH, is also discussed. It is necessary to properly control the composition of assay mixtures (particularly with regard to metal ions) in order to determine what actually regulates the activity of an enzyme.
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PMID:Magnesium regulation of the glycolytic pathway and the enzymes involved. 293 60

Selected glycolytic enzymes (including phosphoglucose isomerase, aldolase, glyceraldehyde phosphate dehydrogenase, enolase, pyruvate kinase and lactate dehydrogenase), as well as glycogen phosphorylase, creatine kinase, and adenylate kinase, bound to phosphofructokinase immobilized on an agarose gel. The affinity of phosphofructokinase to these various proteins differed, with phosphorylase exhibiting the strongest binding. Binding was reversed either by: (1) elution with high-ionic-strength buffer (0.4 M KCl); (2) the addition of a 5-10 mM concentration of ATP; or (3) high concentrations of fructose 6-phosphate (5 mM).
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PMID:Interaction of immobilized phosphofructokinase with soluble muscle proteins. 293 35

We have developed a method for the simultaneous purification of hexokinase, glucosephosphate isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, D-glyceraldehyde-phosphate dehydrogenase, phosphoglycerate kinase, glycerol-3-phosphate dehydrogenase and glycerol kinase from Trypanosoma brucei in yields varying over 8-55%. Crude glycosomes were prepared by differential centrifugation of cell homogenates. Subsequent hydrophobic interaction chromatography on phenyl-Sepharose resulted in six pools containing various mixtures of enzymes. These pools were processed via affinity chromatography (immobilized ATP), hydrophobic interaction chromatography (octyl-Sepharose) and ion-exchange chromatography (CM- and DEAE-cellulose) which resulted in the purification of all nine enzymes. The native enzyme and subunit molecular masses, as determined by gel filtration and gel electrophoresis under denaturing conditions, were compared with those of their homologous counterparts from other organisms. Trypanosomal hexokinase is a hexamer and differs in subunit composition from the mammalian enzymes (monomers) as well as in subunit size (51 kDa versus 96-100 kDa, respectively). Phosphofructokinase only differs in subunit size (51 kDa for T. brucei versus 80-90 kDa for mammals) but had identical subunit composition (tetrameric). The others all have the same subunit composition as their mammalian counterparts. Except for triosephosphate isomerase, all Trypanosoma enzymes have subunits which are 1-5 kDa larger in size. Together these nine enzymes contribute 3.3 +/- 1.6% to the total cellular protein of T. brucei and at least 90% to the total glycosomal protein. A comparison of calculated intraglycosomal concentrations of the enzymes with the glycosomal metabolite concentrations shows that in the case of aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, the concentration of active sites is of the same order of magnitude as that of their reactants. A common feature of the glycosomal glycolytic enzymes (with the exception of glucosephosphate isomerase) is that they are highly basic proteins with pI values between 8.8 and 10.2, values which are 1-4 higher than in the case of their mammalian cytosolic counterparts and 3-6 higher than in the case of the various unicellular organisms. It is suggested that both the larger subunit size and the basic character of the T. brucei glycolytic proteins are involved in the routing of the enzymes from their site of biogenesis (the cytosol) towards their site of action (the glycosome).
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PMID:Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties. 294 90

The affinity of baker's yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphate aldolase towards the metabolically related enzymes phosphofructokinase and glyceraldehyde-3-phosphate dehydrogenase was tested by using a fluorescence-probe technique with fluorescein isothiocyanate attached covalently to the enzymes. The dissociation constants of the enzyme-enzyme complexes, as well as the rate constants of association and dissociation, were determined. Data were compared with the parameters derived from a mammalian (rabbit muscle) system, known from the literature and determined under the same conditions (pH 7.5 or 8.5 in 0.05 M Tris/HCl buffer at 20 degrees C). The comparison reveals similarities in the supramolecular organization of these cytoplasmic enzymes in phylogenetically distant species. Moreover, the fact that in vitro hybrid complexes are formed of stability comparable to that of non-hybrid complexes indicates that this ancient characteristic is probably conserved during evolution. A possible regulatory mechanism is presented, based on the dynamic competition, with each other, of the enzymes involved in triosephosphate metabolism.
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PMID:Interaction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasmic systems. 294 91

The transmural distribution of five glucose metabolizing enzymes (hexokinase; glucose-6-phosphate dehydrogenase; phosphofructokinase; aldolase; and lactate dehydrogenase) were explored in the left and in the right ventricle wall of rat, ox and pig hearts. The levels of most of these enzyme activities were different in the different animal species and (within the same species) in the two ventricles. Most of these enzyme activities were found to be non-uniformly distributed across the left (but not across the right) ventricle wall. Differences in the transmural distribution of enzyme activities were detected among the three examined mammalian species.
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PMID:Transmural distribution of glucose metabolizing enzymes across the left and the right ventricle heart walls in three different mammalian species. 294 92


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