Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Dopac increases tyrosinase activity and exerts cytotoxic effects in cultures of human melanoma cells. The possible role of hydrogen peroxide in these actions was examined. Catalase (100 micrograms/ml) completely reversed the cytotoxic action of 0.3 mM dopac and reduced its tyrosinase-stimulating effect by approximately one half. The results show that extracellular hydrogen peroxide is a mediator of both the tyrosinase-stimulating and cytotoxic actions of dopac. Analysis of the degradation products of melanin from dopac-treated melanoma cells after hydriodic acid (HI) hydrolysis revealed the presence of aminohydroxy-phenylacetic acid (AHPAc). This substance is obtained by HI hydrolysis of melanin formed by oxidation of cysteinyl-dopac. Thus, the presence of AHPAc indicates that dopac is transported into the melanocytes where it serves as a substrate for tyrosinase.
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PMID:Hydrogen peroxide as a mediator of dopac-induced effects on melanoma cells. 189 44

The medium of cultured melanoma cells was studied for tyrosine hydroxylation and dopa-oxidizing activity. The supernatant obtained after centrifugation at 100 000 g for 2 hours was treated with ammonium sulphate, and the precipitate obtained between 35 and 50% saturation was used. Dopa was determined as the product of tyrosine hydroxylation and 5-S-cysteinyldopa as the product of dopa oxidase activity. Determinations were performed with HPLC and electrochemical detection. Our preparation of culture medium of cells showed the following. 1) No hydroxylation of tyrosine in the absence of co-factor. 2) Hydroxylation of L-tyrosine in the presence of dopamine. No hydroxylation with boiled medium. Minimal effect of catalase on hydroxylation. 3) Hydroxylation of tyrosine in the presence of ascorbic acid. Hydroxylation was catalyzed also with boiled medium. Catalase strikingly diminished hydroxylation. 4) Oxidation of L-dopa to dopaquinone determined as its main reaction product with cysteine, 5-S-cysteinyl-dopa. There was negligible oxidation with boiled medium. 5) With dopamine as co-factor the catalysis of tyrosine hydroxylation was stereospecific for L-tyrosine. Dopa oxidase activity was also stereospecific for L-dopa.
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PMID:Tyrosinase activity in the medium of human melanoma cell cultures. 619 32

The effects of systems generating active oxygen species (superoxide anion, hydrogen peroxide, hydroxyl radical) on tyrosinase have been studied in cultured human melanoma cells. Tyrosinase activity was determined by measuring the quantity of 5-S-L-cysteinyl-L-dopa (5-S-CD) formed in the presence of D,L-dopa and L-cysteine. In some experiments, the enzyme protein was determined by radio immunoassay [RIA]. Exposure of cells to xanthine/xanthine oxidase or glucose/glucose oxidase resulted in a dose-related elevation of tyrosinase. Catalase, but not superoxide dismutase, prevented this increase indicating that hydrogen peroxide may be the agent responsible for the action, whereas superoxide anion is not involved. Hydroxyl radicals formed by the Haber-Weiss or Fenton type reactions were not found to produce elevation of tyrosinase. Catalase determinations showed no enzyme in the medium but a high concentration in the cells. Inhibition of intracellular catalase by 3-amino-1,2,4-triazole caused an increase in the tyrosinase level. The effects of dopac, xanthine/xanthine oxidase, and glucose/glucose oxidase all producing hydrogen peroxide, and increasing tyrosinase, were enhanced by the inhibition of catalase. It is concluded that hydrogen peroxide, formed by the systems, accounts for the elevation of tyrosinase level. When tyrosinase activities determined by 5-S-CD formation were compared to enzyme amounts found by RIA, the ratios of these values were always constant. This fact indicates that the increase in the tyrosinase activities was not due to an activation of the enzyme, but mirrored the quantities of enzyme protein present in the samples. On the basis of our findings, it is assumed that hydrogen peroxide is a regulator of tyrosinase in normal melanocytes and melanoma cells.
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PMID:Hydrogen peroxide as an inducer of elevated tyrosinase level in melanoma cells. 843 9

The effect of ferrous ions on the monophenolase activity of tyrosinase has been studied. Although a shortening of the lag period which characterizes this hydroxylation reaction was observed, no direct effect on the enzyme was found. The reaction between ferrous ions and molecular oxygen in the presence of chelating agents, such as phosphate or EDTA, produces hydroxyl radicals. These radicals can hydroxylate tyrosine to generate L-3,4-dihydroxyphenylalanine (dopa). Catalase and scavengers of hydroxyl radicals inhibited both the shortening of the lag period and dopa formation. On the basis of these results, it is proposed that the influence of ferrous ions on tyrosinase is due to the formation of dopa in the chemical hydroxylation of tyrosine. Dopa transforms the Emet form of the enzyme (Cu2+Cu2+) into the Edeoxy form (Cu1+Cu1+) and, thus, shortens the lag period.
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PMID:Effect of ferrous ions on the monophenolase activity of tyrosinase. 850 69

Photosystem II (PSII) membranes exhibit catalase and polyphenol oxidase (PPO) activities. Mild heat treatment of PSII membranes for 90 min at 30 degrees C releases most of these enzyme activities into the supernatant, accompanied by a 7-fold activation of PPO. In contrast, mild heat treatment of thylakoid membranes does not release significant amounts of either activity, indicating that both enzymes are bound to the luminal surface of the thylakoid membrane. The heat-released PSII membrane-associated catalase and PPO have been purified and characterized. Catalase activity was correlated with a 63 kDa polypeptide which was purified by batch adsorption to anion-exchange beads followed by gel filtration. The PSII membrane-associated catalase is unstable in solution, probably due to irreversible aggregation. The enzyme was characterized in terms of molecular and subunit size, amino-acid composition, UV-visible absorption, heme content, pH optimum, inhibitor sensitivity, and K(m) value for H2O2. Its properties indicate that the PSII membrane-associated catalase is a luminal thylakoid membrane-bound heme enzyme that has not been identified previously. The residual catalase activity of PSII membranes after mild heat treatment is irreversibly inhibited with 3-amino-1,2,4-triazole, a specific inhibitor of heme catalases, without inhibition of O2-evolution activity. This result indicates that little, if any, of the catalase activity from PSII membranes in the dark is catalyzed by the O2-evolving center of PSII. PPO activity was correlated with a 48 kDa polypeptide. However, the 48 kDa polypeptide and another heat-released polypeptide of 72 kDa have the same N-terminal sequence, which is also identical to that of a known 64 kDa protein [Hind, G., Marshak, D. R., & Coughlan, S. J. (1995) Biochemistry 34, 8157-8164]. During heat treatment of PSII membranes and further manipulations it was found that the 72 kDa polypeptide was largely converted into the 48 kDa polypeptide. Thus, the 72 kDa polypeptide appears to be a latent precursor of the active 48 kDa PPO. The PSII membrane-associated PPO was purified by anion-exchange chromatography and was characterized in terms of substrate specificity, pH optimum, inhibitor sensitivity and native molecular weight. The heat-released PPO appears to be identical to the enzyme previously isolated from spinach thylakoid membranes [Golbeck, J. H., & Cammarata, K. V. (1981) Plant Physiol. 67, 977-984].
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PMID:Isolation and characterization of spinach photosystem II membrane-associated catalase and polyphenol oxidase. 897 99

Tetrahydroisoquinolines (TIQs) are endogenous alkaloid compounds detected in urine, central nervous system and some peripheral tissues in Mammalia. No data are at present available on TIQ levels in skin, although in vitro biochemical evidences indicate that they may undergo auto-oxidation with production of reactive oxygen species or may be enzymatically converted into melanin pigments. The effect of two catechol-bearing TIQs, salsolinol (SAL) and tetrahydropapaveroline (THP), on the viability of melanotic or amelanotic melanoma cell lines was investigated. Both SAL and THP were well tolerated up to roughly 30 microM and became overtly toxic at higher concentrations, with SAL being better tolerated than THP. Intracellular activity of some antioxidant enzymes, tyrosinase and alpha-ketoglutarate dehydrogenase was also evaluated to assess the cell response to oxidative and metabolic challenge of TIQs treatment. Catalase and superoxide dismutase pre-treatment only partially prevented TIQs toxicity while a complete protection was obtained with N-acetylcysteine and GSH. TIQs were able to provoke upregulation of the scavenging enzymes catalase and DT-diaphorase and to determine a decrease of the alpha-ketoglutarate dehydrogenase activity. SAL and THP enhanced tyrosinase activity and melanin production, suggesting that they were indeed tyrosinase substrates leading to melanin formation. The results support the evidence that TIQs were toxic toward melanoma cells, leading to their death by necrosis. TIQs toxicity was likely due to increased oxidative stress by generation of reactive oxygen species and oxidative metabolites. Our study represents an intent to furnish an additional contribution for the comprehension of catechol cytotoxicity.
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PMID:Cytotoxicity of dopamine-derived tetrahydroisoquinolines on melanoma cells. 1241 63

Mushroom tyrosinase exhibits catalase activity with hydrogen peroxide (H(2)O(2)) as substrate. In the absence of a one-electron donor substrate, H(2)O(2) is able to act as both oxidizing and reducing substrate. The kinetic parameters V(max) and K(m) that characterize the reaction were determined from the initial rates of oxygen gas production (V(0)(O)()2) under anaerobic conditions. The reaction can start from either of the two enzyme species present under anaerobic conditions: met-tyrosinase (E(m)) and deoxy-tyrosinase (E(d)). Thus, a molecule of H(2)O(2) can reduce E(m) to E(d) via the formation of oxy-tyrosinase (E(ox)) (E(m) + H(2) <==> O(2) right harpoon over left harpoon E(ox)), E(ox) releases oxygen into the medium and is transformed into E(d), which upon binding another molecule of H(2)O(2) is oxidized to E(m). The effect of pH and the action of inhibitors have also been studied. Catalase activity is favored by increased pH, with an optimum at pH = 6.4. Inhibitors that are analogues of o-diphenol, binding to the active site coppers diaxially, do not inhibit catalase activity but do reduce diphenolase activity. However, chloride, which binds in the equatorial orientation to the protonated enzyme (E(m)H), inhibits both catalase and diphenolase activities. Suicide inactivation of the enzyme by H(2)O(2) has been demonstrated. A kinetic mechanism that is supported by the experimental results is presented and discussed.
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PMID:Mushroom tyrosinase: catalase activity, inhibition, and suicide inactivation. 1585 23

The synthesis and involvement of H(2)O(2) during the early stages of melanogenesis involving the oxidations of DOPA and dopamine (diphenolase activity) were established by two sensitive and specific electrochemical detection systems. Catalase-treated reaction mixtures showed diminished rates of H(2)O(2) production during the autoxidation and tyrosinase-mediated oxidation of both diphenols. Inhibition studies with the radical scavenger resveratrol revealed the involvement in these reactions of additional reactive intermediate of oxygen (ROI), one of which appears to be superoxide anion. There was no evidence to suggest that H(2)O(2) or any other ROI was produced during the tyrosinase-mediated conversion of tyrosine to DOPA (monophenolase activity). Establishing by electrochemical methods the endogenous production H(2)O(2) in real time confirms recent reports, based in large part on the use of exogenous H(2)O(2), that tyrosinase can manifest both catalase and peroxidase activities. The detection of ROI in tyrosinase-mediated in vitro reactions provides evidence for sequential univalent reductions of O(2), most likely occurring at the enzyme active site copper. Collectively, these observations focus attention on the possible involvement of peroxidase-H(2)O(2) systems and related ROI-mediated reactions in promoting melanocytotoxic and melanoprotective processes.
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PMID:Production and utilization of hydrogen peroxide associated with melanogenesis and tyrosinase-mediated oxidations of DOPA and dopamine. 1588 91

Effects of petroleum contamination on bacterial diversities and enzymatic activities in paddy soils were investigated in the Shenfu irrigation area, the largest area irrigated by oil-containing wastewater for more than 50 yr in northeastern China. Bacterial diversities were determined by conventional colony morphology typing techniques and 16S rDNA polymerase chain reaction (PCR)-denaturing gradient gel electrophoresis (DGGE). Dehydrogenase, hydrogen peroxidase, polyphenol oxidase, urease, and substrate-induced respiration (SIR) were measured to evaluate the effects of petroleum-containing wastewater irrigation on soil biochemical characteristics. Results showed that paddy soil total petroleum hydrocarbon (TPH) concentration in the irrigation area varied from 277.11 to 5213.37 mg kg(-1) dry soil. Soil TPH concentration declined along the gradient of the irrigation channel from up- to downstream. At the current pollution level, the paddy soil TPH concentration was positively correlated with the colony forming units (CFU) of aerobic heterotrophic bacteria (AHB) (r = 0.928, p < 0.001) and the genetic diversity based on DGGE profiles (r = 0.655, p < 0.05). The bacterial diversities in the soils based on colony morphotypes of AHB also increased with TPH concentration (r = 0.598), but not significant statistically (p = 0.052). Analysis of soil enzyme activities indicated a significant positive correlation between soil TPH concentration and activities of dehydrogenases (r = 0.974, p < 0.001), hydrogen peroxidases (r = 0.957, p < 0.001), polyphenol oxidases (r = 0.886, p < 0.001), and SIR (r = 0.916, p < 0.001). On the contrary, the urease activity showed a negative correlation with paddy soil TPH concentration (r = -0.814, p = 0.002), and could be used as a sensitive indicator of petroleum contamination.
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PMID:Effect of petroleum-containing wastewater irrigation on bacterial diversities and enzymatic activities in a paddy soil irrigation area. 1588 93

The effects of metsulfuron-methyl, a sulfonylurea herbicide, on the wheat soil microorganisms were evaluated by the methods of microbial inoculation culture, and the activities of three enzymes were measured using the colorimetric method. The tolerant microorganisms that can resist 500 microg x g(-1) metsulfuron-methyl in the counting culture medium were studied specially. Metsulfuron-methyl distinctly inhibited the common aerobic heterotriphic bacteria, but the effects on common fungi and common actinomycete were not evident. In the meantime, the number of tolerant fungi increased greatly in the rhizosphere after the application of metsulfuron-methyl in contrast to the significant decrease of the amount of tolerant actinomycete. It indicates that fungi might turn into the dominant microbial type and actinomycete is the sensitive factor in the soil polluted by sulfonylurea residues. The population of aromatic compounds-decomposing bacteria, aerobic azotobacter, and nitrite bacteria all increased in the earlier period, but the aerobic azotobacter decreased rapidly in number 30 days later, and the amount of nitrite bacteria also showed a temporary decrease with time 15 days later. However, the denitrifying bacteria just began to increase significantly after the crops had grown for 50 days. The amount of sulfur-oxidizing bacteria gradually decreased with the growth of crops, and so were the sulfate-reducing bacteria after metsulfuron-methyl application. To all types of microorganisms, there were more microbes in rhizosphere samples than those in nonrhizosphere except aerobic azotobacter. It means the growth of wheat root system can stimulate the growth of most microorganisms. The activities of hydrogen peroxidase and polyphenol oxidase in soil samples after metsulfuron-methyl application were notably lower than those in the control, and the difference of the activities between the samples of rhizosphere and nonrhizosphere was evident. On the contrary, the activity of dehydrogenase was not inhibited by the application of metsulfuron-methyl, and the rhizosphere effect was not obvious either.
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PMID:Effects of metsulfuron-methyl on the microbial population and enzyme activities in wheat rhizosphere soil. 1648 87


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