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:1.10.3.2 (laccase)
4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

One oxidase (EC 1.10.3.2) and three lignin peroxidases (EC 1.11.1.-) were purified from the culture liquid of the white-rot fungus Phlebia radiata Fr. All the enzymes were glycoproteins. The oxidase had Mr 64,000 and the lignin peroxidases I, II and III had Mr values 42,000, 45,000 and 44,000 respectively. The lignin peroxidases were found to share common antigenic determinants: lignin peroxidases II and III were serologically indistinguishable and lignin peroxidase I was related but distinguishable. The oxidase did not share any immunological properties with the lignin peroxidases. Lignin peroxidases of Phlebia contain protoporphyrin IX as a prosthetic group. In the presence of H2O2 and an electron donor, veratryl alcohol, lignin peroxidases exhibit spectral shifts analogous to those of animal catalase (EC 1.11.1.6). Phlebia enzymes show optimal activity at pH 3-4.5 at 40 degrees C and are stable in the pH range 5-6. They modify Kraft lignin and phenolic compounds containing hydroxy and methoxy groups.
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PMID:Ligninolytic enzymes of the white-rot fungus Phlebia radiata. 319 1

The ability to degrade oligo- and polysaccharides by enzymes of the glycosidase and glucan-glucan hydrolyse type, and esterase, phosphatase, proteinase, peroxidase, catalase, laccase and tyrosinase activities were tested in 35 strains of 11 sections of the genus Fusarium.
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PMID:Enzyme apparatus of the genus Fusarium. 624 4

A fluorometric procedure has been developed for detection and estimation of laccase activity in fungal broth cultures. Laccase solution was pretreated with catalase for 1 h at 37 degrees C and pH 5. Homovanillic acid was then added and the reaction mixture incubated for a further hour at 37 degrees C. The fluorescence was then developed by addition of 0.1 M glycine buffer at pH 10. Laccase preparations from Pyricularia oryzae, Coriolus hirsutus and Pycnoporus cinnabarinus catalysed formation of a fluorescent product of HVA but the optimum pH values of enzyme activities varied. The culture fluids of several other fungi also catalysed development of fluorescence in solutions containing HVA. p-Hydroxyphenylacetic acid was a poor substrate for all laccases in vivo except that produced by Perennipora tephropora.
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PMID:Phenolic substrates for fluorometric detection of laccase activity. 927 77

The influence of cadmium chloride and/or high temperature on the level of selected parameters were examined in both medium and mycelium of some Basidiomycetes belonging to white-rot fungi: Abortiporus biennis, Trametes versicolor and Cerrena unicolor. We investigated changes in the formaldehyde (FA) level and in the level of superoxide radical anions (SR). Accordingly, the capacity of three enzymes was also studied: two enzymes of the cellular antioxidative system - superoxide dismutase (SOD; EC 1.15.1.1), and catalase (CAT; EC 1.11.1.6), and laccase (LAC; EC 1.10.3.2) the main lignin-modifying enzyme, which is produced by white-rot fungi. During the first 24 hours after application of separate stressors, or jointly with two stressors to 10-day-old cultivation, changes in all selected parameters were observed. Moreover, we found significant changes in the levels of extracellular SR, FA and extra- and intracellular activity of LAC. Simultaneous action of two stressors in the fungal cultures decreased the extracellular LAC level, intracellular CAT activity and the level of SR in the medium compared to the control values, while using the two stress factors separately would strongly make these values increase. Stressful conditions brought a rapid increase in the level of FA in all fungal species. The results of our study, carried out on selected strains of Basidiomycetes, seem to have shown that: (I) LAC, the lignin-modifying enzyme, may have an important application in fungal stress response, and take part in the cross-protection between responses to heat shock and cadmium resistance; (2) the oxidative burst as a result of cadmium and high temperature treatment is an additional factor to damage fungal cells; (3) FA may be a determining factor in the phases of fungal stress syndrome.
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PMID:Formaldehyde as a proof and response to various kind of stress in some Basidiomycetes. 1052 85

The amounts of intra- and extracellular guaiacol peroxidase, ascorbic peroxidase, glutathione peroxidase, superoxide dismutase, laccase, and catalase present in Botrytis cinerea, cultured in three different media: Kovac synthetic medium, Sabouraud fluid medium, and a medium containing malt extract, were determined. The activity of two enzymes, ascorbic peroxidase and glutathione peroxidase, has not been previously described in B. cinerea. The detected amount of the enzymes showed considerable variability in the three different culture media. The presence of an array of enzymes capable of metabolizing hydrogen peroxide, whose levels are determined by the conditions under which the fungus grows, shows that B. cinerea is well equipped to contend with the occurrence of host-produced active oxygen species.
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PMID:Enzymes of Botrytis cinerea capable of breaking down hydrogen peroxide. 1098 1

The effect of a beta-1,3-glucanase (Glucanex) on cultures of Botrytis cinerea was examined. The enzyme released reducing sugars from the mycelium and from the glucan secreted into the culture medium. The morphology of the mycelium was changed in the presence of Glucanex. The measured activity of guaiacol peroxidase, laccase, and catalase was increased when the mycelium was treated with Glucanex. Culture of the mycelium in the presence of Glucanex resulted in an increase in catalase activity. We suggest that the glucan plays a role in protecting the fungus from host response and may assist in the initial stages of host infection.
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PMID:The possible function of the glucan sheath of Botrytis cinerea: effects on the distribution of enzyme activities. 1135 76

Catalase is a highly conserved heme-containing antioxidant enzyme known for its ability to degrade hydrogen peroxide into water and oxygen. In low concentrations of hydrogen peroxide, the enzyme also exhibits peroxidase activity. We report that mammalian catalase also possesses oxidase activity. This activity, which is detected in purified catalases, cell lysates, and intact cells, requires oxygen and utilizes electron donor substrates in the absence of hydrogen peroxide or any added cofactors. Using purified bovine catalase and 10-acetyl-3,7-dihydroxyphenoxazine as the substrate, the oxidase activity was found to be temperature-dependent and displays a pH optimum of 7-9. The Km for the substrate is 2.4 x 10(-4) m, and Vmax is 4.7 x 10(-5) m/s. Endogenous substrates, including the tryptophan precursor indole, the neurotransmitter precursor beta-phenylethylamine, and a variety of peroxidase and laccase substrates, as well as carcinogenic benzidines, were found to be oxidized by catalase or to inhibit this activity. Several dietary plant micronutrients that inhibit carcinogenesis, including indole-3-carbinol, indole-3-carboxaldehyde, ferulic acid, vanillic acid, and epigallocatechin-3-gallate, were effective inhibitors of the activity of catalase oxidase. Difference spectroscopy revealed that catalase oxidase/substrate interactions involve the heme-iron; the resulting spectra show time-dependent decreases in the ferric heme of the enzyme with corresponding increases in the formation of an oxyferryl intermediate, potentially reflecting a compound II-like intermediate. These data suggest a mechanism of oxidase activity involving the formation of an oxygen-bound, substrate-facilitated reductive intermediate. Our results describe a novel function for catalase potentially important in metabolism of endogenous substrates and in the action of carcinogens and chemopreventative agents.
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PMID:Characterization of the oxidase activity in mammalian catalase. 1607 30

It has been widely reported that the white rot basidiomycete Phanerochaete chrysosporium, unlike most other white rot fungi, does not produce laccase, an enzyme implicated in lignin biodegradation. Our results showed that P. chrysosporium BKM-F1767 produces extracellular laccase in a defined culture medium containing cellulose (10 g/liter) and either 2.4 or 24 mM ammonium tartrate. Laccase activity was demonstrated in the concentrated extracellular culture fluids of this organism as determined by a laccase plate assay as well as a spectrophotometric assay with ABTS [2,2(prm1)-azinobis(3-ethylbenzathiazoline-6-sulfonic acid)] as the substrate. Laccase activity was observed even after addition of excess catalase to the extracellular culture fluid to destroy the endogenously produced hydrogen peroxide, indicating that the observed activity is not due to a peroxidase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by activity staining with ABTS revealed the presence of a laccase band with an estimated M(infr) of 46,500.
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PMID:Demonstration of Laccase in the White Rot Basidiomycete Phanerochaete chrysosporium BKM-F1767. 1653 82

A novel bifunctional catalase with an additional phenol oxidase activity was isolated from a thermophilic fungus, Scytalidium thermophilum. This extracellular enzyme was purified ca. 10-fold with 46% yield and was biochemically characterized. The enzyme contains heme and has a molecular weight of 320 kDa with four 80 kDa subunits and an isoelectric point of 5.0. Catalase and phenol oxidase activities were most stable at pH 7.0. The activation energies of catalase and phenol oxidase activities of the enzyme were found to be 2.7 +/- 0.2 and 10.1 +/- 0.4 kcal/mol, respectively. The pure enzyme can oxidize o-diphenols such as catechol, caffeic acid, and L-DOPA in the absence of hydrogen peroxide and the highest oxidase activity is observed against catechol. No activity is detected against tyrosine and common laccase substrates such as ABTS and syringaldazine with the exception of weak activity with p-hydroquinone. Common catechol oxidase inhibitors, salicylhydroxamic acid and p-coumaric acid, inhibit the oxidase activity. Catechol oxidation activity was also detected in three other catalases tested, from Aspergillus niger, human erythrocyte, and bovine liver, suggesting that this dual catalase-phenol oxidase activity may be a common feature of catalases.
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PMID:Purification, characterization, and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum. 1836 15

The tri-enzyme system pyranose 2-oxidase (P2O), laccase, and catalase was used to study major parameters in the homogeneous and heterogeneous application of a multi-component enzymatic machinery. P2O oxidizes aldoses to 2-ketosugars, which are interesting intermediates in carbohydrate chemistry, and concomitantly reduces oxygen or alternative electron acceptors. The enzyme was immobilized on eleven agarose or acrylic resins using various coupling methods. The binding capacity was determined and an acrylic carrier with the most suitable properties selected for detailed studies. As P2O shows higher turnover numbers with the electron acceptor 1,4-benzoquinone than with oxygen, the use of this alternative electron acceptor was enabled by employing laccase for the continuous reoxidation of hydroquinone. The laccase regeneration system was found to increase the specific productivity up to 3-fold. Catalase was used to disproportionate the formed hydrogen peroxide in close proximity to the oxygen consuming enzymes and applied in different amounts to adjust the hydrogen peroxide concentration, which was found to be the main reason for enzyme deactivation under turnover conditions. In contrast to homogeneous catalysis, the specific productivity of heterogeneous catalysts under the applied experimental conditions was limited primarily by oxygen transfer, an effect significantly reduced by the laccase regeneration system.
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PMID:Comparing soluble and co-immobilized catalysts for 2-ketoaldose production by pyranose 2-oxidase and auxiliary enzymes. 1849 82


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