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)

FDP aldolase was found to be present in the cell-free extracts of Rhizobium leguminosarum, Rhizobium phaseoli, Rhizobium trifolii, Rhizobium meliloti, Rhizobium lupini, Rhizobium japonicum and Rhizobium species from Arachis hypogaea and Sesbania cannabina. The enzyme in 3 representative species has optimal activity at pH 8.4 in 0.2M veronal buffer. The enzyme activity was completely lost by treatment at 60 degrees C for 15 min. The Km values were in the range from 2.38 to 4.55 X 10(-6)M FDP. Metal chelating agents inhibited enzyme activity, but monovalent or bivalent metal ions failed to stimulate the activity. Bivalent metal ions in general were rather inhibitory.
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PMID:Fructose 1,6-bisphosphate aldolase activity of Rhizobium species. 0 Feb 83

Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phyosphate-lyase, EC 4.1.2.13) was isolated from buffalo muscle by fractionation with ammonium sulphate and subsequent purification by phosphocellulose column chromatography using a linear salt gradient. As judged by gel filtration and electrophoresis in polyacrylamide gel, the enzyme was homogeneous with respect to size and charge. The molecular weight and Stokes radius of the enzyme were determined from its elution profile on a calibrated Sephadex column and the respective values were 162000 and 4.55 nm. The diffusion coefficient and frictional ratio were computed to be 4.8-10(7) cm2-s-1 and 1.27, respectively. The molecular weight of the polypeptide chain as measured by aodium dodecyl sulphate polyacrylamide gel electrophoresis was 40750. This taken together with the native molecular weight suggested a four-subunit model for the protein. The N- AND C-terminal residues of polypeptide chains were identified to be proline and tyrosine, respectively. At pH 8.0 the Michaelis-Menten constant and maximum attainable velocity were found to be 8.1 muM and 27 muM Fru-1,6-P2 split/min per mg, respectively. The buffalo muscle aldolase was found to be similar to rabbit muscle aldolase in physico-chemical properties. However, the two enzymes differ significantly in pH optimum; the p optima of the buffalo and rabbit enzymes were determined under identical conditions to be 8.0 and 8.6, respectively.
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PMID:Isolation of buffalo muscle aldolase and comparison of its properties with those of rabbit muscle aldolase . 1 72

Crude hemolysates, partially purified aldolase and aldolase purified to homogeneity from reticulocytes and mature erythrocytes, were incubated with a specific antiserum raised against crystalline rabbit muscle aldolase. We show that the same aldolasic activity corresponds to a greater amount of antigen in older than in younger cells, in crude hemolysates as well as in the above mentioned preparations; that is to say, old-cell aldolase contains cross-reacting material (CRM). Properties of purified enzyme from reticulocytes and mature erythrocytes were compared to those of muscle crystalline aldolase: -- the molecular specific activity of purified aldolase from erythrocytes is lower than with crystalline muscle aldolase, i.e. CRM is maintained throughout the purification steps. -- the specific activity of red cell aldolase towards both substrates (FDP and F1P) is lower than that of crystalline muscle aldolase. However, the ratio of activity towards the two substrates FDP/F1P is decreased in erythrocytes and reticulocytes. -- no other difference was found: Michaelis constant towards FDP, thermodenaturation constant and C terminal extremities are identical as are the molecular weights.
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PMID:Modifications of aldolase during in vivo aging of rabbit red cells. 10 73

Fructose 1,6-bisphosphate aldolase inactivation by L- and D-glyceraldehyde 3-phosphate (Ga 3-P) obeys pseudo first-order kinetics. L-Ga 3-P is much more effective than the D-isomer: the Ki values obtained are 0.032 mM and 0.54 mM respectively. Kinetic analysis suggests that one residue of the active center region is involved in the inactivation mechanism: specifically, a cysteine residue appears to be responsible for the initial inactivation by L-Ga 3-P. Lysine and arginine residues become involved at further steps of the inactivation mechanism. No correlation between loss of thiol groups and decay of catalytic activity was observed for the enzyme treated with D-Ga 3-P. The role of lysine and arginine residues in this reaction is discussed.
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PMID:Comparative aspects of the inactivation of fructose 1,6 bisphosphate aldolase by D- and l-glyceraldehyde 3-phosphate. 12 96

The properties of 12 enzymes related to the glycolytic and oxidative metabolism of glucose were examined in normal and malignant epithelium of human uterine tissues to develop optimised assays suitable for both types of tissue and to delineate important kinetic differences that may exist between them. All assays gave acceptable long-term precision, although instability of phosphofructokinase and 6-phosphogluconate dehydrogenase prevented proper assessment; and all were linear with concentration to an absorbance change of 0.04/min, or more in the case of several enzymes. Notable differences between pyruvate kinase of normal and malignant uterine epithelium were found with D-fructose-1,6-diphosphate (FDP) which caused significantly greater activation of the latter as well as a dramatic reduction in Km for phosphoenol pyruvate; inhibition by DL-alanine was greater for pyruvate kinase of malignant than normal cervix epithelium, whereas endometrium did not show this difference. The ratio of aldolase activity with FDP to that with D-fructose-1-phosphate was greater in malignant than in normal cervix epithelium, no significant difference being apparent in endometrium.
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PMID:Properties of glycolytic and related enzymes of normal and malignant human uterine tissues studied to optimise assay conditions. 15 96

Paracatalytic enzyme modifications result from the oxidation of enzyme-substrate carbanions by extrinsic oxidants. During the oxidation of enzyme-activated substrates, transiently reactive intermediates are generated which, without being released from the enzyme, modify groups at the active site. For enzymes producing carbanion intermediates, the combination of the normal substrate with a suitable electron acceptor has thus been proposed as a highly specific binary system for their active site-directed modification. In this study, the structural features of paracatalytically modified fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) from rabbit muscle have been elucidated. This enzyme is completely inactivated within 60 min in the presence of fructose 1,6-bisphosphate in saturating concentration and 0.5 mM hexacyanoferrate(III) (pH 7.6, 25 degrees C). The inactivation is caused by covalent incorporation of one triosephosphate derivative per subunit. Peptide analysis showed that the triosephosphate derivative forms an intrachain crosslink between lysine-146 and lysine-227. According to previous independent experimental evidence, both lysyl residues are located at the active site: the epsilon-amino group of lysine-227 forms a Schiff base intermediate with the carbonyl group of the substrate [Lai, C. Y., Nakai, N. & Chang, D. (1974) Science 183, 1204-1206] and alkylation of lysine-146 by the affinity labeling reagent N-bromoacetylethanolamine phosphate inactivates the enzyme [Hartman, F. C. & Brown, J. P. (1976) J. Biol. Chem. 251, 3057-3062]. The present data thus establish paracatalytic modification as a mode of active site-directed enzyme modification.
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PMID:Paracatalytic modification of aldolase: a side reaction of the catalytic cycle resulting in irreversible blocking of two active-site lysyl residues. 28 42

Relations between clinical course and change in aldolase (ALD) isoenzyme pattern were investigated on the peripheral and bone marrow blood of normal subjects and patients suffering from leukemia, multiple myeloma, hypoplastic anemia and other hematological disorders. Similar examination was performed on human leukemia cells and on sera and leukocytes from Donryu rats inoculated with rat leukemia cells (DBLA-6), induced by NBU. In addition to the enzyme activity, isoenzyme pattern was analyzed electrophoretically. The results obtained were as follows: 1) FDP/F1P ratios of the peripheral and marrow blood were high in untreated leukemia. After the induction therapy, the ratio in the marrow blood was high, but decreased in peripheral blood. 2) In complete remission, both ratios were decreased to normal level. 3) In the early relapse of leukemia, the marrow blood showed a high ratio in spite of normal value in the peripheral blood. During full relapse or reinduction therapy, FDP/F1P ratio remained high in both the peripheral and marrow blood. 4) Atypical hypoplastic leukemia showed a significantly high ratio in the marrow, but a low ratio in the periphery. No difference in either ratio was detected between hypoplastic anemia and normal subjects. 5) Zymogram of leukemia cells from leukemia patients showed that ALD-A was predominant more clearly than in normal leukocytes. ALD in normal leukocytes was composed mainly of ALD-A and its hybrids with ALD-B and ALD-C. 6) The ratio in sera and leukocytes from rats inoculated with DBLA-6 cells was increased with exacerbation of leukemia. ALD-A was predominant in rat leukemia cells on the zymogram. It is concluded that aldolase isoenzymes, especially the FDP/F1P ratio, are useful in estimating clinical course of leukemia, particularly in deciding early relapse of leukemia in bone marrow. These laboratory findings are also useful in differentiating atypical leukemia from hypoplastic anemia.
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PMID:[Clinical and experimental studies on aldolase and its isoenzymes in leukemia and allied hematological disorders (author's transl)]. 29 6

1. Levels of glycolytic enzymes were determined in terms of units of enzyme/mg protein in rat striated muscle, carp lateral muscle, holothuria longitudinal muscle of the body wall, and a snail foot muscle. 2. An attempt has been made to correlate levels of glycolytic enzymes as a parameter to establish a "biochemical distance" at molecular level and correlate this with the phylogenetic position in animals sufficiently separated in the animal tree of evolution. 3. The possibility of a peculiar kinetic behaviour of the glycolytic pathway in each muscle tissue studied, has been analyzed as the profiles of the ratios of pairs of enzymes bearing a substrate-product dependence. 4. A possible "futile synthesis" of some glycolytic enzymes, such as FDP-aldolase in the case of fish muscle, is proposed.
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PMID:Comparative levels of muscle glycolytic enzymes in mammals, fish, echinoderm and molluscs. 31 26

Fructose 1,6-bisphosphate aldolase from rabbit muscle forms by reaction with dihydroxyacetone phosphate a pyruvaldehyde-aldolase-orthophosphate complex that is in equilibrium with the eneamine intermediate. The new intermediate accumulates in two phases. The first one is practically complete in 40ms, and the second occurs with an apparent first-order rate constant of 4.6 +/- 0.5s-1. The new intermediate breaks down slowly with the release into the medium of pyruvaldehyde and Pi. The rate of the spontaneous release is higher at acidic than at neutral pH.
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PMID:A new intermediate of the aldolase reaction, the pyruvaldehyde-aldolase-orthophosphate complex. 74 1

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.
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PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72


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