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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chara fragilis possesses microbodies with a remarkably large size of up to 2 micro m in diameter. Many of the organelles contain huge nucleoids of amorphous material or paracrystalline inclusions. After isolation of the organelles by gradient centrifugation the specific density of the microbodies was determined to be 1.25 g cm-3. Catalase, glycolate oxidase and hydroxypyruvate reductase as well as enzymes of the fatty acid beta-oxidation pathway were demonstrated to be constituents of the microbodies in Chara indicating that they are similar to those in green leaves. The data obtained are in agreement with the view that the Charophyceae and especially the algae in the subgroup of Charales are very closely related to the land plants.
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PMID:Microbodies of the alga Chara. 1270 9

Catalase, glycolate oxidase, and hydroxypyruvate reductase, enzymes which are located in the microbodies of leaves, show different developmental patterns in the shoots of wheat seedlings. Catalase and hydroxypyruvate reductase are already present in the shoots of ungerminated seeds. Glycolate oxidase appears later. All three enzymes develop in the dark, but glycolate oxidase and hydroxypyruvate reductase have only low activities. On exposure of the seedlings to continuous white light (14.8 x 10(3) ergs cm(-2) sec(-1)), the activity of catalase is doubled, and glycolate oxidase and hydroxypyruvate reductase activities increase by 4- to 7-fold. Under a higher light intensity, the activities of all three enzymes are considerably further increased. The activities of other enzymes (cytochrome oxidase, fumarase, glucose-6-phosphate dehydrogenase) are unchanged or only slightly influenced by light. After transfer of etiolated seedlings to white light, the induced increase of total catalase activity shows a much longer lag-phase than that of glycolate oxidase and hydroxypyruvate reductase. It is concluded that the light-induced increases of the microbody enzymes are due to enzyme synthesis. The light effect on the microbody enzymes is independent of chlorophyll formation or the concomitant development of functional chloroplasts. Short repeated light exposures which do not lead to greening are very effective. High activities of glycolate oxidase and hydroxypyruvate reductase develop in the presence of 3-amino-1,2,4-triazole which blocks chloroplast development. The effect of light is not exerted through induced glycolate formation and appears instead to be photomorphogenetic in character.In senescing leaves excised from the plants decreases in activity of glycolate oxidase, and hydroxypyruvate reductase follow with some delay the decrease in chlorophyll content. The activity of catalase, however, is maintained at high levels, especially when the detached shoots are kept in light.
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PMID:Developmental studies on microbodies in wheat leaves : I. Conditions influencing enzyme development. 1665 92

A seven-step sequential grinding procedure was applied to leaves of Atriplex rosea, Sorghum sudanense, and Spinacia oleracea to study the distribution of carboxylases and microbody enzymes. In the extracts from C(4) species there were 7- to 10-fold reciprocal changes in specific activities of ribulose-1, 5-diphosphate carboxylase and phosphoenolpyruvate carboxylase. No such changes occurred in sequential extracts from spinach. No inhibitors of ribulose-1, 5-diphosphate carboxylase were detected when the mesophyll extracts of Sorghum were assayed together with spinach extracts. These results reaffirm the conclusion of others that phosphoenolpyruvate carboxylase is largely confined to the mesophyll in these species and ribulose-1, 5-diphosphate carboxylase to the bundle sheath. The specific activities of glycolate oxidase and hydroxypyruvate reductase in bundle sheath extracts were two to three times those in mesophyll fractions. Catalase behaved similarly in Atriplex rosea but in Sorghum the specific activity was virtually the same in all fractions. From the relative amounts of these enzymes present, and comparison with the data obtained from spinach, it is concluded that typical leaf peroxisomes are present in the bundle sheaths of both C(4) species and in the mesophyll of Atriplex rosea. The relative enzyme activities in the mesophyll of Sorghum suggest that the microbodies there are of the non-specialized type found in many nongreen tissues. The activities of the microbody enzymes in the bundle sheath of Sorghum seem quite inadequate to support photorespiration.
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PMID:Microbody enzymes and carboxylases in sequential extracts from c(4) and c(3) leaves. 1665 49

Ribulose-1,5-bisphosphate carboxylase/oxygenase, catalase, glycolate oxidase, and hydroxypyruvate reductase activities on a protein and fresh weight basis were measured over seven stages of tomato fruit development and ripening. Ribulose-1,5-bisphosphate carboxylase decreased steadily during fruit development from 23 +/- 8 nmoles per minute per milligram protein at the mature green stage to 13.4 +/- 2 at the table ripe stage. There was no change in partially purified preparations of the enzyme in the ratio of carboxylase to oxygenase activity, which was about 10. Catalase activity reached a maximum during the climacteric, simultaneously with increased ethylene and CO(2) formation. Glycolate oxidase activity decreased during early stages of development and was barely detectable at the climacteric. Hydroxypyruvate reductase, associated with serine formation by the glycerate pathway, increased in specific activity during early stages of tomato fruit ripening. In the fruit of the rin tomato mutant, which does not ripen normally, none of these changes in enzyme activity occurred.
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PMID:Changes in Activity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Three Peroxisomal Enzymes during Tomato Fruit Development and Ripening. 1666 Jul 53

1. In etiolated wheat (Triticum aestivum L.) leaves, the development of the microbody enzymes catalase, hydroxypyruvate reductase, and glycolate oxidase was specifically stimulated by short treatments of the seedlings with red light, although the increases were less than observed after treatment with continuous white light. A comparison of the effects of short red and far-red exposures indicated the involvement of phytochrome. 2. Continuous far-red light treatments also enhanced the development of microbody enzymes. Catalase activity continued to increase at a high rate even after return from a prolonged far-red illumination to darkness, while the increase in the activities of glycolate oxidase and hydroxypyruvate reductase fell to the dark rates when the tissue was removed from the light. However, even at higher intensities of continuous far-red light the microbody enzymes reached only considerably lower activities than in white light. During continuous irradiation of equal quantum flux, the microbody enzymes reached higher activities in red than in far-red light, but the highest activities were observed in blue light, which had similar effects as white light. The quantitative difference between the effects of prolonged red or blue light depended also on the seed material and growing conditions. In the presence of the herbicide 3-amino-1,2,4-triazole the increase of glycolate-oxidase activity was reduced in red light but was affected much less, if at all, in blue light. 3. Continuous irradiations with all three light qualities used (red, far-red, blue) influenced the properties of the microbody particles to form a distinct band sharply confined close to an equilibrium density of 1.25 g cm(-3) on sucrose gradients which was not observed in preparations from plant material raised in complete darkness. In preparations from all light-grown plants a special peak in the activity profile of malate dehydrogenase was found in the microbody fraction while it was lacking on gradients from dark-grown leaves. The heights of the activities of malate dehydrogenase as well as of the other enzymes found in the microbody fractions from plants grown in either far-red, red, or blue light differed in the same way as did the activities from total leaf homogenates. 4. Glycolate oxidation by segments of intact leaf tissue was higher with tissue from light- than from dark-grown plants, but after light treatments of different spectral quality its magnitude did not correspond to the extractable activities of glycolate oxidase.
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PMID:Developmental studies on microbodies in wheat leaves : III. On the photocontrol of microbody development. 2443 25

The crude homogenate of cells from Chlamydomonas reinhardii was placed on a linear gradient from 30% to 60% sucrose and centrifuged for 4 hours at 60 000 g. After fractionation of the gradient the distribution of enzymes was determined. Hydroxypyruvate reductase and glycolate dehydrogenase, two markers for peroxisomes, appeared with one sharp peak at density 1.185 g/cm(3) within the gradient. Twenty-five percent of the hydroxypyruvate reductase was particulate and 75% was found as solubles in the top fractions. The peaks of both enzymes matched exactly the peak of the cytochrome oxidase which is a marker for mitochondria. The profile for malate dehydrogenase was the same as that for hydroxypyruvate reductase. Catalase, however, showed two peaks. One coincided with the peak of cytochrome oxidase and the other appeared at density 1.22 g/cm(3). More than 50% of the catalase moved into the gradient during centrifugation.
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PMID:[Distribution of microbody enzymes from Chlamydomonas on sucrose gradients]. 2444 97