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)

The presence of 14 enzymes was investigated using purified spores of the microsporidian Nosema grylli from fat body of the crickets Gryllus bimaculatus. Glucose 6-phosphate dehydrogenase (EC 1.1.1.49), phosphoglucomutase (EC 5.4.2.2), phosphoglucose isomerase (EC 5.3.1.9), fructose 6-phosphate kinase (EC 2.7.1.11), aldolase (EC 4.1.2.13), 3-phosophoglycerate kinase (EC 2.7.2.3), pyruvate kinase (EC 2.7.1.40) and glycerol 3-phosphate dehydrogenase (EC 1.1.1.8) were detected with activities of 15 +/- 1, 7 +/- 1, 1,549 +/- 255, 10 +/- 1, 5 +/- 1, 16 +/- 4, 6 +/- 1 and 16 +/- 2 nmol/min mg protein, respectively. Hexokinase (EC 2.7.1.1), NAD-dependent malate dehydrogenase (EC 1.1.1.37), malic enzyme (EC 1.1.1.40), lactate dehydrogenase (EC 1.1.1.27), alcohol dehydrogenase (EC 1.1.1.1) and succinate dehydrogenase (EC 1.3.99.1) were not detectable. These results suggest the catabolism of carbohydrates in microsporidia occurs via the Embden-Meyerhof pathway. Glycerol 3-phosphate dehydrogenase may reoxidize NADH which is produced by glyceraldehyde 3-phosphate dehydrogenase in glycolysis.
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PMID:Activities of enzymes of carbohydrate and energy metabolism of the spores of the microsporidian, Nosema grylli. 918 13

A new analytical approach has been applied to the determination and characterization of mercury-accessible -SH groups in pure native protein samples (ovalbumin, hemoglobin, glyceraldehyde-3-phosphate dehydrogenase, aldolase, pyruvate kinase, hexokinase, lactate dehydrogenase, alcohol dehydrogenase, creatine phosphokinase, lysozyme, and cytochrome c). The method is based on the selective reduction of Hg(II) in the presence of Hg(II)-thiol complexes with alkaline sodium tetrahydroborate, to give Hg(0) in a continuous flow reaction system coupled with atomic fluorescence spectrometric (AFS) detection. The method is fast and specific and allows one to work with nanomole amounts of a single protein without any preliminary incubation and without any separation of Hg(II) from thiol-complexed mercury. The meaning of the results obtained in the determination of the accessible -SH groups in native proteins by using chemical probes is discussed.
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PMID:Application of mercury cold vapor atomic fluorescence spectrometry to the characterization of mercury-accessible -SH groups in native proteins. 1052 12

Intrinsic chemical properties of the zinc(II) ion in zinc enzymes have been investigated by the model of 1:1 Zn2+-macrocyclic polyamine complexes, including Zn2+-1,5,9-triazacyclododecane ([12]aneN3) and 1,4,7,10-tetraazacyclododecane (cyclen). The physiologically most suitable pKa values for the Zn2+-bound H2O in enzymes were illustrated by the first model Zn2+-[12]aneN3 complex, which mimics the essential kinetic and thermodynamic roles of Zn2+ in carbonic anhydrase. The activation of proximate serine residues (in alkaline phosphatase) and activation of alcohols for hydride transfer to NAD+ (in alcohol dehydrogenase) were also mimicked by Zn2+ -[12]aneN3 complexes. The functions of two zincs in dinuclear metallophosphatases were explained by a new dinuclear Zn2+-cryptate. For an aldolase type II model, a Zn2+-cyclen derivative showed facile enolate formation from a proximate carbonyl pendant under physiological conditions. The strong anion affinities, which Zn2+ intrinsically possesses, were exploited into novel selective nucleobase thymine (or uracil) recognition of Zn2+-cyclen complexes by the strong Zn2+ -imido anion bond formation. The Zn2+-aromatic-pendant cyclen complexes selectively bind to T (or U) in single- and double-stranded DNA (or RNA). Thus, Zn2+ complexes act like molecular zippers to break A-T pairs in DNA, which was proven by various physicochemical measurements and DNA footprinting assays. These Zn2+ complexes showed some relevant biochemical and biological properties such as inhibition of transcriptional factor, TATA binding protein, or strong antimicrobial activities to gram-positive bacterial strains.
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PMID:Why zinc in zinc enzymes? From biological roles to DNA base-selective recognition. 1081 60

The purpose of this study was to further examine the hypothesis that variations in hepatic fructose-metabolizing enzymes between males and females might account for the differences in the severity of copper (Cu) deficiency observed in fructose-fed male rats. Weanling rats of both sexes were fed high-fructose diets either adequate or deficient in copper for 45 days. Cu deficiency decreased sorbitol dehydrogenase activity and dihydroxyacetone phosphate levels and increased glyceraldehyde levels in both sexes. Gender effects were expressed by higher activities of glycerol 3-phosphate dehydrogenase and aldehyde dehydrogenase in male than in female rats and higher levels of dihydroxyacetone phosphate and fructose 1,6-diphosphate (F1,6DP) in female than in male rats. The interactions between dietary Cu and gender were as follows: alcohol dehydrogenase activities were higher in female rats and were further increased by Cu deficiency in both sexes; aldehyde dehydrogenase activities were decreased by Cu deficiency only in male rats; sorbitol levels were higher in male rats and were further increased by Cu deficiency in male rats; fructose 1-phosphate (F1P) levels were increased by Cu deficiency in both sexes, but to a greater extent in male rats; glyceraldehyde 3-phosphate levels were higher in female rats, but were decreased by Cu deficiency in female and increased in male rats. Though most of the examined hepatic fructose-metabolizing enzymes and metabolites showed great differences between rats fed diets either adequate or deficient in Cu, it is the activity of fructokinase and aldolase-B, and the concentrations of their common metabolites, F1P and notably F1,6DP, that could be in part responsible for differences in the severity of pathologies associated with Cu deficiency observed between female and male rats.
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PMID:Hepatic fructose-metabolizing enzymes and related metabolites: role of dietary copper and gender. 1104 32

The introns-early view has been challenged for several genes; prominent instances are triose phosphate isomerase (TPI), aldolase, pyruvate kinase (PK), alcohol dehydrogenase (ADH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and myosin heavy chain. While some of their introns appear to be phylogenetically ancient and/or to delineate exons corresponding to protein modules, a considerable number seemingly do not. But it is argued here that many of these anomalous introns are periodic, that is, relics of internal sequence repetitions within the ancestral gene. Some of these periodic-intron patterns are shared between related genes, as in the alphabeta -barrels of TPI, aldolase and PK, or the Rossmann nucleotide-binding domain common to PK, ADH and GAPDH. This is further evidence for the ancestral status of these introns. The myosin heavy chain C-terminal rod region is paradoxical in that its sequence is clearly periodic but its intron placements are not; however, they exhibit a remarkable coherence of intron translational phases, suggesting that these introns may also have originally had a periodic arrangement now obscured by intron slipping.
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PMID:Split gene origin and periodic introns. 1109 33

Two different strains of mice with different susceptibilities to systemic candidiasis (BALB/c and CBA/H) were infected with Candida albicans SC5314. Immune sera were obtained on different days post-infection and assayed against two-dimensional polyacrylamide gel electrophoresis separation of cytoplasmic extracts obtained from protoplasts. More than 31 immunoreactive proteins were detected. Some of them were identified and found to correspond to (i) glycolytic enzymes, such as fructose biphosphate aldolase, triose phosphate isomerase (TPIS), glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase (PGK), enolase (ENO1) and pyruvate kinase, (ii) other metabolic enzymes, such as methionine synthase (METE), inosine-5'-monophosphate dehydrogenase (IMH3), alcohol dehydrogenase and aconitate hydratase and (iii) heat shock proteins: HS71 (or Ssa1p) and HS75 (or Ssb1p), both from the HSP70 family. This work reports for the first time antigenic properties for IMH3 and TPIS. Different profiles of antibody expression, depending on the mouse strain and the course of infection, were observed. ENO1 was the most immunogenic protein in infected BALB/c mice (the most resistant strain). On the other hand, sera from CBA/H mice (a more susceptible strain) showed a strong increase in reactivity along the infection against METE, HS75 and PGK. Many of these immunoreactive proteins have also been detected using sera from human patients with systemic candidiasis, thus indicating the usefulness of the murine model for studying the antibody response in systemic candidiasis. In this work we demonstrate that the combination of two-dimensional electrophoresis with immunoblotting using murine immune sera can be an important tool for the identification of C. albicans antigens and for monitoring the evolution of the disease.
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PMID:Analysis of the serologic response to systemic Candida albicans infection in a murine model. 1168 Dec 8

To compare the regulation of anaerobic metabolism during germination in anoxia-tolerant and intolerant plants, enzymes associated with anaerobic metabolism such as sucrose synthase, aldolase, enolase, pyruvate decarboxylase (PDC), alcohol dehydrogenase (ADH), and aldehyde dehydrogenase (ALDH) were assayed in two varieties of Echinochloa crus-galli, formosensis (tolerant) and praticola (intolerant). The initial and intervening enzymes of the pathway (sucrose synthase and aldolase) and enzymes in the last part of the pathway (PDC, ADH and ALDH) revealed similar changing patterns in activities during germination. This implies that each group of enzymes may be controlled by an identical regulatory mechanism. During anoxia, activities of all enzymes increased 1.5-30-fold in both varieties compared to their activities under aerobic conditions. Activities of sucrose synthase, enolase and ADH exhibited the same induction patterns under anoxia in formosensis and praticola. However, the activities of aldolase, ALDH and PDC were more strongly induced in formosensis under anoxia (1.2-2-fold) than in praticola. These enzymes were also assayed in F(3) families which varied in their anaerobic germinability. For PDC, activities under anoxia in anoxia-tolerant families were similar to those of an anoxia-intolerant family during the whole period although the family did not exhibit anaerobic germinability. This suggests that there is no correlation between PDC activity and anaerobic germinability. For ALDH, activities were more strongly induced under anoxia in anoxia-tolerant families than in anoxia-intolerant families, a trend also exhibited by the parents. This indicates that ALDH may play a role in detoxifying acetaldehyde formed through alcoholic fermentation during anaerobic germination.
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PMID:Genetic and biochemical analysis of anaerobically-induced enzymes during seed germination of Echinochloa crus-galli varieties tolerant and intolerant of anoxia. 1270 89

The irreversible oxidation of cysteine residues can be prevented by protein S-thiolation, a process by which protein SH groups form mixed disulphides with low-molecular-mass thiols such as glutathione. We report here the target proteins which are modified in yeast cells in response to H(2)O(2). In particular, a range of glycolytic and related enzymes (Tdh3, Eno2, Adh1, Tpi1, Ald6 and Fba1), as well as translation factors (Tef2, Tef5, Nip1 and Rps5) are identified. The oxidative stress conditions used to induce S-thiolation are shown to inhibit GAPDH (glyceraldehyde-3-phosphate dehydrogenase), enolase and alcohol dehydrogenase activities, whereas they have no effect on aldolase, triose phosphate isomerase or aldehyde dehydrogenase activities. The inhibition of GAPDH, enolase and alcohol dehydrogenase is readily reversible once the oxidant is removed. In addition, we show that peroxide stress has little or no effect on glucose-6-phosphate dehydrogenase or 6-phosphogluconate dehydrogenase, the enzymes that catalyse NADPH production via the pentose phosphate pathway. Thus the inhibition of glycolytic flux is proposed to result in glucose equivalents entering the pentose phosphate pathway for the generation of NADPH. Radiolabelling is used to confirm that peroxide stress results in a rapid and reversible inhibition of protein synthesis. Furthermore, we show that glycolytic enzyme activities and protein synthesis are irreversibly inhibited in a mutant that lacks glutathione, and hence cannot modify proteins by S-thiolation. In summary, protein S-thiolation appears to serve an adaptive function during exposure to an oxidative stress by reprogramming metabolism and protecting protein synthesis against irreversible oxidation.
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PMID:Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. 1275 85

Possible target proteins of cytosolic thioredoxin in higher plants have been investigated in the cell lysate of dark-grown Arabidopsis thaliana whole tissues. We immobilized a mutant of cytosolic thioredoxin, in which an internal cysteine at the active site was substituted with serine, on CNBr activated resin, and used the resin for the thioredoxin-affinity chromatography. By using this resin, the target proteins for thioredoxin in the higher plant cytosol were efficiently acquired. The obtained proteins were separated by two-dimensional gel electrophoresis and analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Thus we have identified proteins of the anti-oxidative stress system proteins (ascorbate peroxidase, germin-like protein, and monomeric type II peroxiredoxin), proteins involved in protein biosynthesis (elongation factor-2 and eukaryotic translation initiation factor 4A), proteins involved in protein degradation (the regulatory subunit of 26S proteasome), and several metabolic enzymes (alcohol dehydrogenase, fructose 1,6-bis phosphate aldolase-like protein, cytosolic glyceraldehyde 3-phosphate dehydrogenase, cytosolic malate dehydrogenase, and vitamin B(12)-independent methionine synthase) together with some chloroplast proteins (chaperonin 60-alpha and 60-beta, heat shock protein 70, and glutamine synthase). The results in this study and recent proteomics studies on the target proteins of chloroplast thioredoxin indicate the versatility and the physiological significance of thioredoxin as reductant in plant cell.
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PMID:Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. 1474 82

In terms of gene expression and carbohydrate metabolism, the response of wheat seedlings to hypoxia is dramatically different from the anoxic response. Total carbohydrate content of roots increased 4-fold during 6 days of hypoxia, with a 17-fold increase in fructans. In contrast, anoxically treated roots depleted all soluble carbohydrates and died within 72 h. Gas exchange measurements (CO(2) release vs. O(2) uptake) demonstrate that hypoxia establishes a new balance between fermentation and aerobic respiration in the roots without altering the flux of carbon through glycolysis. Furthermore, the respiratory component of this new balance is 55% higher in roots that have been hypoxically pretreated compared to non-hypoxically pretreated roots. The establishment of this new homeostasis under hypoxia involves the induction of glycolytic (aldolase and enolase) and fermentative enzymes (pyruvate decarboxylase, alcohol dehydrogenase, and lactate dehydrogenase). Enzyme induction is generally complete within 24 h with mRNA induction occurring primarily during Period I (0-6 h of hypoxia), and maximal enzymes activities attained during Period II (6-24 h of hypoxia). Accumulation rates of Suc, hexoses, and fructans also change during Periods I and II. By the start of Period III (24-144 h of hypoxia), the metabolic adjustments are complete and fructans are the major carbohydrate accumulated. In anoxia, the pattern of enzyme induction was dramatically different: aldolase was not induced and declined throughout the treatment. Alcohol dehydrogenase, pyruvate decarboxylase, and lactate dehydrogenase were induced as in hypoxia, but rapidly declined within 72 h of anoxia. Only enolase exhibited a similar expression pattern in both anoxia and hypoxia.
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PMID:Sugar and fructan accumulation during metabolic adjustment between respiration and fermentation under low oxygen conditions in wheat roots. 1503 81


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