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 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

We determined the activities of selected enzymes involved in carbon metabolism in free-living cells of Rhizobium tropici CFN299 grown in minimal medium with different carbon sources and in bacteroids of the same strain. The set of enzymatic activities in sucrose-grown cells suggests that the pentose phosphate pathway, with the participation of the Entner-Doudoroff pathway, is probably the primary route for sugar catabolism. In glutamate- and malate-grown cells, high activities of the gluconeogenic enzymes (phosphoenolpyruvate carboxykinase, fructose-6-phosphate aldolase, and fructose bisphosphatase) were detected. In bacteroids, isolated in Percoll gradients, the levels of activity for many of the enzymes measured were similar to those of malate-grown cells, except that higher activities of glucokinase, glucose-6-phosphate dehydrogenase, and NAD-dependent phosphogluconate dehydrogenase were detected. Phosphoglucomutase and UDP glucose pyrophosphorylase showed high and constant levels under all growth conditions and in bacteroids.
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PMID:Carbon Metabolism Enzymes of Rhizobium tropici Cultures and Bacteroids. 1634 19

Two isoenzymes each of phosphoglucomutase, hexose phosphate isomerase, aldolase, fructose diphosphatase, phosphofructokinase, and 6-phosphogluconate dehydrogenase have been separated by DEAE-cellulose column chromatography of extracts from endosperm of germinating castor beans (Ricinus communis cv. Hale). One of each of the enzymes is localized in the cytosol and the other is confined to plastids. Developmental studies of these isoenzymes were carried out to clarify their roles in the endosperm. In extracts from ungerminated seeds the activities of marker enzymes of mitochondria (fumarase), plastids (ribulose bisphosphate carboxylase), and glyoxysomes (catalase) were low, but phosphoglucomutase, hexose phosphate isomerase, aldolase, and 6-phosphogluconate dehydrogenase were present in relatively high activity. The total amounts of these enzymes increased 3- to 4-fold during the first 5 days of growth. The activities of isoenzymes in the plastids rose in parallel with that of ribulose bisphosphate carboxylase to reach a maximum at day 4, and like the carboxylase they declined sharply thereafter. The activities of the cytosolic isoenzymes peaked at day 5. These changes are consistent with the roles previously proposed for the sequences present in plastid and cytosol.
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PMID:Isoenzymes of sugar phosphate metabolism in endosperm of germinating castor beans. 1666 46

The distribution of the glycolytic enzymes, phosphofructokinase, aldolase, triosephosphate isomerase, phosphoglycerate kinase, pyruvate kinase, and the oxidative pentose phosphate pathway enzymes, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, was determined in the leaf tissues of two C(3)-plants, pea and leek, and two C(4)-plants, maize and sorghum. All enzymes examined were found in epidermal tissue. In pea, maize, and sorghum leaves, the specific activities of these enzymes were usually higher in the nonphotosynthetic epidermal tissue than in the photosynthetic tissues of the leaves. In leek leaves, which were etiolated, specific activities were similar in both epidermal and mesophyll tissue. The distribution of the rate limiting enzymes of glycolysis and the oxidative pentose phosphate pathways probably reflects the capacity of each tissue to generate NADH, NADPH, and ATP from the oxidation of glucose. This capacity appears to be greater in leaf tissues unable to generate reducing equivalents and ATP by photosynthesis, that is, in epidermal tissues and etiolated mesophyll tissue.
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PMID:Enzymes of Glucose Oxidation in Leaf Tissues : The Distribution of the Enzymes of Glycolysis and the Oxidative Pentose Phosphate Pathway between Epidermal and Mesophyll Tissues of C(3)-Plants and Epidermal, Mesophyll, and Bundle Sheath Tissues of C(4)-Plants. 1666 59

White leaves of the mutant line albostrians and green leaves of the wild-type cultivar Salome of barley (Hordeum vulgare L.) were screened for the presence of plastidic and cytosolic isoenzymes of sugar-phosphate metabolism. Isoenzyme separation was achieved by anion-exchange chromatography on Fractogel TSK DEAE-650(S). The mutant tissue had a markedly reduced level of plastidic 3-phosphoglycerate kinase, triosephosphate isomerase, and aldolase activity. In contrast, the activity of plastidic glucosephosphate isomerase, fructose 1,6-bisphosphatase, 6-phosphogluconate dehydrogenase, starch phosphorylase, and ADP-glucose pyrophosphorylase was in the same range as in wild-type leaf tissue. The activity of the corresponding cytosolic isoenzymes (including UDP-glucose pyrophosphorylase) showed essentially no differences in mutant and wild type. The same trend was observed in dark-grown mutant and wild-type leaves. Interestingly, the total activity levels of all isoenzymes were about the same when comparing dark-grown and light-grown mutant or wild-type plants. From these data, it is concluded that mutant leaves exhibit a selective decrease of a subgroup of plastidic isoenzymes associated with the Calvin cycle.
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PMID:Repression of the Plastidic Isoenzymes of Aldolase, 3-Phosphoglycerate Kinase, and Triosephosphate Isomerase in the Barley Mutant "albostrians". 1666 17

We have examined the changes in carbohydrate metabolism in food yam (Dioscorea esculenta (Lour.) Burk.) tubers and in an economically important spice cum medicinal plant turmeric (Curcuma longa L.) rhizomes under storage. Both specimens showed varied levels of dormancy and sprouting appeared at the end of dormant period. Harvested, fully matured tubers of yam and rhizomes of turmeric were stored in wooden boxes under the conditions of 28+/-2 degrees C temperature and 65-75% relative humidity (RH) in dark. The starch, sugars, enzymes of starch degradation, respiration, glycolysis, tricarboxylic acid (TCA) cycle and oxidative pentose phosphate pathway (PPP) were studied during 1-70 days after harvest (DAH). This investigation revealed that, the starch degradation and the enzymes involved, viz. alpha-amylases and starch phosphorylase showed a lower level of activity during early period of dormancy, while sugar content and enzymes of carbohydrate metabolism increased rapidly during sprouting. The isoenzymic profiles of alpha-amylases showed marked variations in these two phases. The key enzymes of glycolysis, TCA cycle and PPP, viz. aldolase, succinic dehydrogenase, malic dehydrogenase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were increased even before the visible appearance of sprouting and their activities were at their maximum during sprouting. Based of the observations the dormancy period may be distinctly divided into peak period of rest and presprouting period.
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PMID:Carbohydrate metabolism in Dioscorea esculenta (Lour.) Burk. tubers and Curcuma longa L. rhizomes during two phases of dormancy. 1753 51

Decrease in intensity of lactate accumulation and activity of glycolytic enzyme such as: phosphofructokinase, fructose-1,6-bisphosphate aldolase, pyruvate kinase found in staphylococcus of the second group isolated at vaginosis in comparison with staphylococcus of the third group isolated at vaginosis and concomitant additional infection pathology as well in comparison with staphylococcus of the first control group. Minimal inhibitory effect (MIA) and increase of enzyme activity of pentosephosphate ways such as: glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, transketolase testify to an intensification pentose-phosphate ways and decrease in activity of found the second groups staphylococcus isolated at vaginosis in comparison with of the in third group isolated at vaginosis and additional infection pathology as well as in comparison with the first control group staphylococcus isolated at normal state of UGT.
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PMID:[Glycolysis and pentose-phosphate pathway ratio in staphylococcus from the female genitalia in norm and dysbiosis]. 1925 43

In order to provide a reference range for normal red blood cell enzyme activities in Thai, we analyzed data from 113 healthy non-anemic Thai people (55 males and 58 females) age 1-42 years, who all had a normal pattern of hemoglobin typing (HbA and HbA2 less than 3.5%). Hematological analysis was performed using an automated cell counter and the hemoglobin studies were carried out by low pressure liquid chromatography. Owing to a high frequency of alpha-thalassemia in Thailand, cases with an MCV < 75 fl were excluded from the study since these cases were likely to be heterozygotes for alpha0-thalassemia. Cases with reticulocytes > 2.5% were excluded from the study since reticulocytes have a higher enzyme activity than mature erythrocytes. Cases with abnormal red blood cell morphology, such as spherocytes and ovalocytes, were also excluded. These criteria were applied to select "normal" controls for our analysis. We assayed eight red blood cell enzyme activities in normal subjects: glucose-6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), pyruvate kinase (PK), hexokinase (HK), glucose phosphate isomerase (GPI), phosphofructokinase (PFK), aldolase (ALD) and phosphoglycerate kinase (PGK). The mean normal ranges (+/- SD) for G6PD, 6PGD, PK, HK, GPI, PFK, ALD and PGK were 12.7 (+/-2.2), 10.7 (+/-1.3), 18.5 (+/-4.0), 1.5 (+/-0.4), 80.5 (+/-11.8), 11.8 (+/-2.1), 4.5 (+/-1.6) and 370 (+/-43) IU/gHb, respectively. Age-dependent differences for the reference values for these enzyme activities were summarized. All red blood cell enzyme activities were highest during the early childhood period and slightly lower in the adult period. These values will be of clinically useful for future reference.
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PMID:Development of a comprehensive red blood cell enzymopathy laboratory in Thailand: the study of normal activity in eight erythroenzymes in Thais. 1932 17

Pb hyper-accumulated Carex putuoshan was taken as experimental material and subjected to combined stress of Pb and Zn. The differential expression of proteins in their roots were analyzed by Proteomic Approach. The protein that was directly involved in the cellular defense under the Pb and Zn combined stress was separated, and expression of those genes was analyzed with Carex Evergold as control. The results were obtained by MALDI-TOF/MS analysis. After applying Pb and Zn combined stress, the expression of 9 protein spots (including 7 different proteins, 2 identical proteins, 1 unknown protein) in Carex putuoshan root was found to be significantly up-regulated. Five proteins were obtained from the 9 proteins related to carbohydrate metabolism, including malate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, frutose-1,6-bisphosphate aldolase, enolase, and 6- phosphogluconate dehydrogenase. Two proteins were related to protein biosynthesis, including isoflavone reductase and phytochelatin synthase (PCS). From these proteins, the most important protein is PCS, which is a key enzyme in the synthesis of phytochelatins (PCs) and plays an important role in chelation. It is directly involved in cellular defense under Pb and Zn stress. After Pb and Zn combined stress, the CpPCS in Carex putuoshan was cloned. The full length of cDNA is 1461 bps, and it encodes 486 amino acids with molecular weight of 53.86 kD and pI value of 6.12. Two typical phytochelatin synthase subfamily domains constitute CpPCS protein, which includes three adjacent Cys-Cys elements in the C-terminal region. Phylogenetic analysis of PCS proteins from different species showed that it had the closest relationship with the Oryza sativa and Triticum aestivum. Real-time quantitative PCR analysis indicated that CpPCS and CePCS (Carex Evergold) genes were expressed in the root. The CpPCS and CePCS genes were up-regulated by Pb and Zn treatments. The expression of CpPCS was higher than that of CePCS under the same condition. The study found that CpPCS expression was increased by Pb and Zn stress in the Carex putuoshan enrichment process of Pb, which lead to high expression of PCS protein. CpPCS improved the accumulation ability and resistance of Carex putuoshan to heavy metals with the expression level of glucose metabolism related proteins increasing after Pb and Zn stress.
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PMID:Research on Root Responses to Pb and Zn Combined Stress of Carex putuoshan. 2700 5

In this paper is reported an example of extensive developmental changes in the isoenzymes controlling a biochemical pathway: more than half of the glycolytic enzymes of the grasshopper,Caledia captiva differ in electrophoretic phenotype between embryonic and adult stages. A similar pattern of changes is found in each of the taxa ofC. captiva, which is actually a species complex. The present example of developmental variation differs from that described for glycolytic enzymes in vertebrates in two main points. Firstly, the changes between the phenotypes of the embryos and adults are co-incident in time, occurring near hatching. Secondly, in contrast to vertebrates where embryospecific isoenzymes are rare, there exist inC. captiva isoenzymes of trehalase, glucosephosphate isomerase, aldolase, pyruvate kinase, lactate dehydrogenase and 6-phosphogluconate dehydrogenase which are found in the embryo but not in the adult. Some of the variable enzymes also exhibit tissue specificity in the adult. The existence of the changes, whatever their basis, shows that the theory that the expression of housekeeping genes is developmentally invariant is not generally correct.
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PMID:Developmental changes in the isoenzymes controlling glycolysis in the acridine grasshopper,Caledia captiva. 2830 56


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