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

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

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

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

Rabbit muscle aldolase (RMA) is 96 per cent inhibited in the presence of beta-bromopyruvic acid (BPA) in a molar ratio of 1/250, during 60 minutes incubation. The chemical reaction of higher significance in this phenomenon is the alkylation of -SHgroups of both apparent and buried types, with formation of S-pyruvil-cystein. The previous treatment of the enzyme with FDP protects aldolase, decreasing the rate of inhinition by BPA to about 56 per cent. FDP protection of the enzyme protects nearly 5-SH groups against the alkylating effect of BPA. Cyanogen bromide hydrolysis of the carboxymethylated protein results in the classical formation of 4 fragments, peptides F1, the NH-2terminal; F2, the COOH-terminal; F3, the active site containing peptide; and F4, a small peptide located between F2 F3. The protection bestowed upon the enzyme by FDP, against the alkylating effect of BPA, is located in the F1, F2, and F3 either in BPA treated aldolases or in the BPA treated FDP-aldolase. Part of the inhibiting effect of BPA is then attributed to the possible interaction between this compound and the basic aminoacids in the aldolase molecule.
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PMID:The effect of beta-bromopyruvic acid on fructose-1, 6-diphosphate aldolase from rabbit muscle. 123 83

Three aldolase isoenzymes; aldolase A, B and C were found in various human tissues including gastric mucosa, by means of substrate specificities (the fuctose-1, 6-diphosphate aldolase/fructose-1-phosphate aldolase activity ratio) and electrophoresis. The basic pattern of aldolase isoenzyme in man consisted of nine active bands, which were designated as I, II, III, IV, V, VI, VII, VIII and IX band from anode side respectively. The I band corresponded to aldolase C, V to aldolase A and IX to aldolase B. The II, III and IV band are hybrid molecules composed of subunit of aldolase A and C, and the VI, VII and VIII of subunit of aldolase A and B. The V band was present in all tissues, while IX was detected in the liver, kidney and stomach. The I, II, III and IV band were found in all tissues except for muscle. These findings were extremely different from those in other species. In normal gastric mucosa, active bands were composed of I, II, III, IV, V, VIII and IX band, while in gastric cancerous tissue, I, II, III, VIII and IX band were absent or markedly decreased in activity. In contrast, the V band increased. In fetal gastric mucosa, they showed the same pattern as cancerous. In extract of cancerous tissues, the FDP/F1P activity ratio was 20.5+/-2.2, as compared with 7.2+/-0.1 in normal gastric mucosa. In serum of patients with gastric cancer, the FDP/F1P activity ratio was 9.7+/-1.2, while it was 2.9+/-0.4 in normal human serum. These results suggest that the elevation in serum of the FDP/F1P ratio in gastric cancer is due to increase in muscle type isoenzyme (aldolase A) which is derived from cancerous tissue. Furthermore, the analysis of serum aldolase isoenzyme will save for cancer diagnosis.
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PMID:[The distribution of the aldolase isoenzymes in various human tissues and the anomaly in cancerous tissues -especially in gastric cancer- (author's transl)]. 124 Aug 53

Enzymatic studies on aldolase isozymes have been carried out by techniques of protein engineering. Site-directed mutagenesis helps us to verify the roles of amino acid residues in catalytic reactions. Chimeric fusion proteins give us information about the regions which specify the characteristics of the isozymes. The results are: (1) In aldolase A, COOH terminal Tyr and Lys-107 residues play important roles in catalysis, especially in binding of FDP. (2) Aspartic acid at the 128th residue in aldolase A is essential to thermostability; no other residue such as glutamic acid can substitute for it. (3) Studies on chimeric fusion proteins indicate that the C-terminal region (including C-terminus Tyr) or aldolase A is responsible for its substrate specificity, which is not seen in aldolase B. (4) A region near NH2 terminus in aldolase B determines its specific structure. (5) The region including His-107, Asp-128, and Tyr-137 (B-A junction of BA137) is located in a turn which is exposed outward (a model architecture by Sygusch et al [1987]). In BA137, this region would be constrained, and play a significant role in catalysis, thermostability, etc. (6) Tertiary structure of aldolase B seems to be dissimilar to that of aldolase A.
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PMID:Structural studies on aldolase isozymes through protein engineering. 220 67

Effects of n-octane and n-nonane (1 ml per kg body weight daily) on hepatic and serum enzymes, which reflect abnormal liver function and concentration of lipid and nucleic acid (serum and liver), were studied after 2 and 7 days intraperitoneal administration to albino rats. Decreased activities of serum acetylcholine esterase and carboxyl esterase were observed, together with an increase in FDP aldolase activity. Significant decrease in the concentration of albumin, total protein, and total and esterified cholesterol in serum have been noted after n-octane and n-nonane administration for 7 days. Also, free cholesterol content of liver was elevated significantly after solvents exposure.
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PMID:Hepatotoxicity in albino rats exposed to n-octane and n-nonane. 258 19

E. coli expression plasmids for human aldolases A and B (EC 4.1.2.13) have been constructed from the pIN-III expression vector and their cDNAs, and expressed in E. coli strain JM83. Enzymatically active forms of human aldolase have been generated in the cells when transfected with either pHAA47, a human aldolase A expression plasmid, or pHAB 141, a human aldolase B expression plasmid. These enzymes are indistinguishable from authentic enzymes with respect to molecular size, amino acid sequences at the NH2- and COOH-terminal regions, the Km for substrate, fructose 1,6-bisphosphate and the activity ratio of fructose 1,6-bisphosphate/fructose 1-phosphate (FDP/F1P), although net electric charge and the Km for FDP of synthetic aldolase B differed from those for a previously reported human liver aldolase B. In addition, both the expressed aldolases A and B complement the temperature-sensitive phenotype of the aldolase mutant of E. coli h8. These data argue that the expressed aldolases are structurally and functionally similar to the authentic human aldolases, and would provide a system for analysis of the structure-function relationship of human aldolases A and B.
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PMID:Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host. 264 52


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