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)

The fungi Pleurotus ostreatus and Trametes pubescens were grown in a mineral medium containing 1% of glucose and 0.9% of lignosulfonates introduced into the culture medium in the form of yeast waste liquor. Chromatography of extracts of the medium and determinations of sulphur and lignosulfonates have revealed that the fungi studied utilized the constituents of the yeast waste liquor (lignosulfonates) as carbon source. This was manifested in an increase of dry mass of the mycelium and protein as compared with the control. The constituents of the yeast waste liquor were also found to have a stimulating effect on the formation of both exo-and endoenzymes, laccase and peroxidase. This may indicate that these oxidases take part in the decomposition of lignosulfonates.
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PMID:Studies on the decomposition of lignosulfonates by the fungi Pleurotus ostreatus and Trametes pubescens. 117 50

The ascomycete Aspergillus nidulans produces green conidia (asexual spores). Recessive mutants which produce yellow conidia have been previously isolated from haploid strains and have been shown to be deficient in laccase (diphenol oxidase), an enzyme that requires copper for activity. Using a diploid parent strain, we isolated dominant yellow conidial mutants which, in the haploid state, produced even less laccase activity than a recessive mutant. Three isolates of such mutants behaved similarly and define a single complementation group (yB) on chromosome VIII distinct from the yA locus on chromosome I defined by recessive mutants. Unlike yA mutants, whose only discernable phenotype is their conidial color, yB mutants are pleiotropic: conidial germination was delayed relative to the wild type, and sexual development was blocked at an early stage. The three phenotypes of yB mutants were expressed on yeast extract-glucose medium containing 1.6 microM of added copper. When copper was added to above 5 microM, all three phenotypes were remediated, and near wild-type levels of laccase were produced. We conclude that yB mutants have a reduced availability of copper. The dominance of yB mutants could result, for example, from an alteration in transport or storage of copper. Using an immunological assay, we detected no laccase antigenic cross-reacting material in yB mutants grown on medium of low copper content. We conclude that either the synthesis or the stability of laccase is copper dependent.
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PMID:Dominant spore color mutants of Aspergillus nidulans defective in germination and sexual development. 702 22

A biosensor was used for the analysis of catecholamines in media and lysates of cultured bovine adrenal chromaffin cells. The sensor is composed of coimmobilised laccase and glucose dehydrogenase coupled with an oxygen electrode, using the catalytic effect of cate cholamines for glucose oxidation in this system. The analysis time is almost 5 min. The correlation between the biosensor and HPLC determination is 0.99.
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PMID:A new sensitive and simple method for detection of catecholamines from adrenal chromaffin cells. 748 95

This method was proposed earlier for measuring glucose in a peroxidase-glucose oxidase system but has not been studied for determination of manganese peroxidase (MnP) activity. The assay is based on the oxidative coupling of 3-methyl-2-benzothiazolinone hydrazone (MBTH) and 3-(dimethylamino)benzoic acid (DMAB). The reaction of MBTH and DMAB in the presence of H2O2, Mn2+, and MnP gives a deep purple-blue color with a broad absorption band with a peak at 590 nm. The extinction coefficient is high (53,000 M-1 cm-1), so low MnP activities can be detected. Lignin peroxidase and laccase, usually present in cultures of white rot fungi, gave little or no interference at the concentrations tested. However, slight interference from very high LiP activity may occur at very low MnP activity.
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PMID:Determination of manganese peroxidase activity with 3-methyl-2-benzothiazolinone hydrazone and 3-(dimethylamino)benzoic acid. 807 99

Melanin production is a major virulence factor for Cryptococcus neoformans, an organism causing life-threatening infections in an estimated 10% of AIDS patients. In order to characterize the events involved in melanin synthesis, an enzyme having diphenol oxidase activity was purified and its gene was cloned. The enzyme was purified as a glycosylated 75-kDa protein which migrated at 66 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis after deglycosylation by endoglycosidase F. Substrate specificity resembled that of a laccase in that it oxidized multiple diphenolic and diamino compounds. Dopamine was shown by mass spectroscopy to be oxidized to decarboxy dopachrome, an intermediate of melanin synthesis. The enzyme contained 4.1 +/- 0.1 mol of copper per mol. It resembled a laccase in its absorbance spectrum, containing a peak of 610 nm and the shoulder at 320 nm, corresponding to the absorbance of a type I and type III copper, respectively. The cloned gene of C. neoformans laccase (CNLAC1) contained a single open reading frame encoding a polypeptide 624 amino acids in length. The encoded polypeptide contained a presumptive leader sequence, on the basis of its relative hydrophobicity and by comparison of the sequence to that of the N-terminal sequence of the purified enzyme. CNLAC1 also contained 14 introns ranging from 52 to 340 bases long. Transcriptional activity of CNLAC1 was found to be derepressed in the absence of glucose and to correspond to an increase in enzymatic activity.
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PMID:Biochemical and molecular characterization of the diphenol oxidase of Cryptococcus neoformans: identification as a laccase. 830 May 20

Two protein bands with laccase activity were found after PAGE of culture liquid or mycelium extract of Pleurotus eryngii, grown on glucose-ammonium tartrate-yeast extract medium with and without inducers. A major and a minor laccase band were observed in the basal medium. The intensity of the major band (laccase I) did not change after the addition of inducers. However, the minor band (laccase II), characterized by higher electrophoretic mobility, was strongly induced by wheat-straw alkalilignin and vanillic and veratric acids. Laccase activity in the basal medium had an optimum pH of 4.5 and was stable from pH 3 to 10 during 24 h at room temperature. This enzyme had wide substrate specificity on hydroquinones, methoxy-substituted monophenols, and aromatic amines. In general, laccase activity was found only with compounds having a redox potential lower than 0.5 mV. The highest activity was obtained with methoxy- and methyl-substituted p-hydroquinones and aromatic diamines. Some activity also occurred with the aliphatic compound 3,5-cyclohexadiene-1,2-diol.
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PMID:Induction and Characterization of Laccase in the Ligninolytic Fungus Pleurotus eryngii 893 93

Effect of various cultivation conditions and lignin preparations on the enzymes of ligninolytic enzyme complex of white-rot fungus Pleurotus floridae has been studied. The maximal Mn-peroxidase activity was revealed in the medium with low nitrogen content (1.2 mM); maximal values of cellobiose quinone oxidoreductase activity were observed in the media with high nitrogen content (7.2 mM); maximal values of laccase activity in the media with low content of glucose (2 g/l) during Pleurotus floridae cultivation in Kirk's stationary cultures have been shown. Employment of submerged cultivation under conditions of mycelium immobilization on polyurethane carriers allowed us to increase laccase activity twice as compared with cultivation in small stationary cultures, while had the crucial effect on the Mn-peroxidase activity. The selective effect of the studied lignin preparations on the components of ligninolytic complex and their isoenzymes has been stated. The dependence of laccase and Mn-peroxidase activities on high and low-molecular weight fractions balance in lignin preparations has been established.
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PMID:[Effect of lignin preparations and cultivation conditions on the ligninolytic complex of the fungus Pleurotus floridae, the wood white-rot pathogen]. 945 73

When glucose is the carbon source, the white rot fungus Pycnoporus cinnabarinus produces a characteristic red pigment, cinnabarinic acid, which is formed by laccase-catalyzed oxidation of the precursor 3-hydroxyanthranilic acid. When P. cinnabarinus was grown on media containing cellobiose or cellulose as the carbon source, the amount of cinnabarinic acid that accumulated was reduced or, in the case of cellulose, no cinnabarinic acid accumulated. Cellobiose-dependent quinone reducing enzymes, the cellobiose dehydrogenases (CDHs), inhibited the redox interaction between laccase and 3-hydroxyanthranilic acid. Two distinct proteins were purified from cellulose-grown cultures of P. cinnabarinus; these proteins were designated CDH I and CDH II. CDH I and CDH II were both monomeric proteins and had apparent molecular weights of about 81,000 and 101,000, respectively, as determined by both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The pI values were approximately 5.9 for CDH I and 3.8 for CDH II. Both CDHs used several known CDH substrates as electron acceptors and specifically adsorbed to cellulose. Only CDH II could reduce cytochrome c. The optimum pH values for CDH I and CDH II were 5.5 and 4.5, respectively. In in vitro experiments, both enzymes inhibited laccase-mediated formation of cinnabarinic acid. Oxidation intermediates of 3-hydroxyanthranilic acid served as endogenous electron acceptors for the two CDHs from P. cinnabarinus. These results demonstrated that in the presence of a suitable cellulose-derived electron donor, CDHs can regenerate fungal metabolites oxidized by laccase, and they also supported the hypothesis that CDHs act as links between cellulolytic and ligninolytic pathways.
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PMID:Novel interaction between laccase and cellobiose dehydrogenase during pigment synthesis in the white rot fungus Pycnoporus cinnabarinus. 992 58

Germlings of Botrytis cinerea, an important fungal pathogen of plants, produce an extracellular matrix (ECM), or ensheathing film, that serves, in part, in their attachment (R. P. Doss, et al., Appl. Environ. Microbiol. 61:260-265, 1995). The composition of this film has been ascertained by using samples obtained by growing germlings on a glass surface, removing the fungal mycelium by vigorous washing, and collecting the tightly attached film by scraping the substratum with a razor blade. Slightly over half of the dry weight of the ECM was found to be carbohydrates (about 20%), proteins (about 28%), and lipids (about 6%). Hydrolysis of the carbohydrate portion of the ECM revealed that glucose was the most prominent monosaccharide present, comprising about 60% of the total monosaccharides. Also present were mannose (about 35%) and myo-inositol (about 5%). The proteinaceous fraction of the ECM was made up of a number of polypeptides separable by polyacrylamide gel electrophoresis. The lipid fraction of the ECM, analyzed by thin-layer chromatography, was made up of several simple lipid components, including free fatty acid, mono- and triacylglycerol, wax ester, fatty alcohol, and several unidentified components. No complex lipids were detected. Isolated ECM exhibited polygalacturonase and laccase activity and was able to catalyze the hydrolysis of p-nitrophenyl butyrate, a model substrate for assessing cutinase activity. Cellulase, pectin lyase, and pectin methyl esterase activities were noted with both heated and unheated ECM preparations. Proteinase activity was not detected.
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PMID:Composition and enzymatic activity of the extracellular matrix secreted by germlings of botrytis cinerea. 992 60

The gene lcc3-2 encoding a second laccase of the white-rot fungus Pycnoporus cinnabarinus has been cloned, sequenced, and characterized. The isolated gene consists of 2840bp, with the coding region interrupted by ten introns and flanked by an upstream region in which putative CAAT and TATA boxes were identified. The cDNA of lcc3-2 contains an open reading frame of 1563bp. The deduced mature laccase protein consisted of 498 amino acids and was preceded by a signal peptide of 23 amino acids. The sequence of lcc3-2 reveals 73% similarity on the protein level to the previously characterized lcc3-1. The new laccase gene shares highest similarity to lcc1 from Trametes villosa (75%), and lcc2 from the unidentified basidiomycete CECT 20197 (75%). The calculated isoelectric point (pI) of 6.1 for the gene product LCC3-2 was in good agreement with the experimentally determined pI of a laccase secreted by P. cinnabarinus grown on cellulose. Transcription analysis using competitive reverse transcription (RT)-PCR showed that lcc3-2 was expressed in glucose and cellulose containing cultures. However, in contrast to lcc3-1, lcc3-2 transcription was not increased in response to 2,5-xylidine.
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PMID:Cloning and characterization of a second laccase gene from the lignin-degrading basidiomycete Pycnoporus cinnabarinus. 1043 78


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