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)

Cell suspensions of Bacteroides fragilis were allowed to ferment glucose and lactate labeled with (14)C in different positions. The fermentation products, propionate and acetate, were isolated, and the distribution of radioactivity was determined. An analysis of key enzymes of possible pathways was also made. The results of the labeling experiments showed that: (i) B. fragilis ferments glucose via the Embden-Meyerhof pathway; and (ii) there was a randomization of carbons 1, 2, and 6 of glucose during conversion to propionate, which is in accordance with propionate formation via fumarate and succinate. The enzymes 6-phosphofrucktokinase (pyrophosphate-dependent), fructose-1,6-diphosphate aldolase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, fumarate reductase, and methylmalonyl-coenzyme A mutase could be demonstrated in cell extracts. Their presence supported the labeling results and suggested that propionate is formed from succinate via succinyl-, methylmalonyl-, and propionyl-coenzyme A. From the results it also is clear that CO(2) is necessary for growth because it is needed for the formation of C4 acids. There was also a randomization of carbons 1, 2, and 6 of glucose during conversion to acetate, which indicated that pyruvate kinase played a minor role in pyruvate formation from phosphoenolpyruvate. Phosphoenolpyruvate carboxykinase, oxaloacetate decarboxylase, and malic enzyme (nicotinamide adenine dinucleotide phosphate-dependent) were present in cell extracts of B. fragilis, and the results of the labeling experiments agreed with pyruvate synthesis via oxaloacetate and malate if these acids are in equilibrium with fumarate. The conversion of [2-(14)C]- and [3-(14)C]lactate to acetate was not associated with a randomization of radioactivity.
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PMID:Pathway of succinate and propionate formation in Bacteroides fragilis. 14 60

Spirillum bengal is unable to grow on sugars, but can utilize different organic acids as carbon sources. Dehydrogenase activities were tested with different substrates and were found highest with lactate, glutamate, acetate, succinate and malate. A low aldolase activity was also detectable.
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PMID:Aldolase and dehydrogenase activities in Spirillum bengal. 42 15

A mutant of Rhizobium meliloti selected as unable to grow on L-arabinose also failed to grow on acetate or pyruvate. It grew, but slower than the parental strain, on many other carbon sources. Assay showed it to lack alpha-ketoglutarate dehydrogenase (kgd) activity, and revertants of normal growth phenotype contained the activity again. Other enzymes of the tricarboxylic acid cycle and of the glyoxylate cycle were present in both mutant and parent strains. Enzymes of pyruvate metabolism were also assayed. L-Arabinose degradation in R. meliloti was found to differ from the known pathway in R. japonicum, since the former strain lacked 2-keto-o-deoxy-L-arabonate aldolase but contained alpha-ketoglutarate semialdehyde dehydrogenase; thus, it is likely that R. meliloti has the L-arabinose pathway leading to alpha-ketoglutarate rather than the one to glycolaldehyde and pyruvate. This finding accounts for the L-arabinose negativity of the mutant. Resting cells of the mutant were able to metabolize the three substrates which did not allow growth.
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PMID:alpha-Ketoglutarate dehydrogenase mutant of Rhizobium meliloti. 76 18

Treatment with the polyene antibiotic, filipin, renders the spermatozoan cell membrane permeable to small molecules, but not to the intracellular enzymes aldolase and lactate dehydrogenase. Pyruvate (10 mM) as the sole substrate was metabolized very slowly. L-Carnitine increased pyruvate metabolism 3- to 4-fold and allowed limited rates of oxidative phosphorylation. When spermatozoa treated with filipin were supplemented with malate, there was a rapid, almost linear rate of pyruvate metabolism which was slightly increased by L-carnitine. In the absence of malate, 20 to 30% of the pyruvate used was reduced to lactate; this increased to 57% in the presence of malate. Without malate, about 90% of the pyruvate metabolized was converted to lactate and acetate or L-acetylcarnitine. Rutamycin or rotenone increased both the rate of pyruvate use and the delta lactate/deltapyruvate ratio. Under all treatments, L-carnitine consistently reduced the percentage of pyruvate converted to lactate by about 10%; part of the pyruvate was preferentially shunted into L-acetylcarnitine rather than lactate. The mitochondrial inhibitors, rotenone or rutamycin, did not change the amount of pyruvate that was converted to metabolites other than lactate, or L-acetylcarnitine, or both. Pyruvate-supported State 3 respiration was linear only if L-carnitine, or malate, or both, were added to the incubation medium. Added malate was necessary to produce a rapid State 3 respiratory rate and was also required for significant respiratory activity in the presence of rotenone or rutamycin. From cells metabolizing [2-14C]pyruvate (1.4 mM), 14C-labeled acid-extractable metabolites were separated by ion exchange column chromatography. All of the [2-14C]pyruvate (+/-5%) used was recovered in 14C-labeled metabolites and 14CO2. In the presence of malate, citrate accumulation was significant, and was always large in comparison to flux through the citric acid cycle. Glutamate, beta-hydroxybutyrate, acetoacetate, fumarate, aspartate, and alpha-ketoglutarate did not accumulate in significant amounts. Some 14C-labeled succinate was produced but only in the presence of malate. Alkaline hydrolysis of a fraction containing carnitine esters yielded acetate and a compound tentatively identified as beta-hydroxybutyrate or lactate. As in intact cells, intramitochondrial lactate dehydrogenase competes successfully with the electron transport system for the NADH generated by pyruvate metabolism. The role of lactate and L-carnitine, and conclusions suggested by the accumulation of certain metabolites are discussed in relation to control of citric acid cycle activity.
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PMID:Mitochondrial metabolism of pyruvate in bovine spermatozoa. 83 19

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.
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PMID:[Carbohydrate metabolism enzymes of purple sulfur-bacteria during growth in the dark]. 88 7

Activities of both aldolases were distinctly decreased in acute kidney insufficiency, caused by administration of uranyl acetate. The decrease in the activity of fructose-1,6-diphosptate aldolase was more distinct which led to alteration in ratio between fructose -1,6-diphosphate and ketose-1-phosphate aldolases. The isozyme spectra of the enzymes were also altered. Isozymes of fructose-1,6-diphosphate aldolase AB2 and of ketose-1-phosphate aldolase form 22 possessed the same electrophoretic mobility but their relative activity was increased 2-3-fold under conditions of the acute kidney insufficiency. At the same time, the more electrophoretically mobile isozymes were not detected.
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PMID:[Fructose-1,6-diphosphate aldolase and ketose-1-phosphate aldolase isoenzyme spectra in the kidneys normally and in uranyl acetate poisoning]. 102 33

The contents of collagen, hexosamine, phospholipids, and cholesterol and the activities of acid and alkaline phosphatases, glutamic oxalo-acetate transaminase, glutamic pyruvate transminase, aldolase, hexokinase, and lactic dehydrogenase were determined in the lungs of rats 150 days after the intratracheal injection of amosite, anthophyllite, and chyrsotile. Anthophyllite did not cause any significant change, while amosite and chrysotile caused significant increases in the contents of collagen and mucopolysaccharides. Lactic dehydrogenase and acid phosphatase activities were increased by all the dusts, while the othe enzymes were not seriously affected. The biochemical significance of the findings in relation to abestosis was discussed.
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PMID:Biochemical changes caused by asbestos dust in the lungs of rats. 123 58

Embryonal nervous tissue from Wistar rats was transplanted into male rats of Wistar and August strains. Activity of eight enzymes belonging to various systems was estimated in brain cortex of rats recipients within 36 days after the transplantation. Lactate dehydrogenase, alanine aminotransferase, acid phosphatase, 5'-nucleotidase, ATPase and aldolase exhibited the dissimilarly decreased rate of activity in brain cortex of Wistar rats after transplantation as compared with the enzymatic activity in intact animals of this strain, while activity of alkaline phosphatase and esterases hydrolyzing alpha-naphthyl acetate was increased. Activation of almost all the enzymes studied was found within 36 days in Wistar rats after the transplantation. The rate of activity of zonal esterase isoenzymes was higher in brain cortex of August rats after transplantation of embryonal nervous tissue from Wistar strain as compared with that of Wistar to Wistar rats transplantation. The data obtained suggest that tissues of donors affected definitely the enzymatic activity in brain cells of rats-recipients as activity of most enzymes studied was higher in brain cortex of donors as compared with that of recipients.
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PMID:[Specifics of changes in various groups of enzymes in rat cerebral cortex after interstrain transplantation of embryonal nerve tissue]. 141 28

A method for the preparative high-yield electroelution of proteins from sodium dodecyl sulphate (SDS) polyacrylamide gel strips was established. The method consisted of SDS-polyacrylamide gel electrophoresis, detection of proteins with sodium acetate and electrophoretic elution at 200 V for 3 h by utilizing a horizontal flat-bed gel electrophoresis apparatus. Standard proteins with molecular masses of 14-66 kilodalton (cytochrome c, aldolase, ovalbumin and bovine serum albumin) were recovered with an average yield of 73.6 +/- 2.3%. A membrane-bound protein, rat skeletal muscle Ca(2+)-ATPase (100 kilodalton) was also well recovered (over 60%). This method was applicable to the purification of proteins required for N-terminal amino acid sequencing and to raise antibodies.
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PMID:Preparative high-yield electroelution of proteins after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and its application to analysis of amino acid sequences and to raise antibodies. 166 9

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


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