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)

Horseradish peroxidase (HRP; EC 1.11.1.7) catalyzed the H(2)O(2)-dependent oxidative coupling of (+)-catechin 1 to form three different biphenyl C-C dimers 2-4, whereas Rhus vernicifera laccase catalyzed the formation of two new catechin-hydroquinone adducts 5 and 6. Spectroscopic evidence showed that HRP dimers were linked through position 8 of the A-ring of one catechin moiety to C-5' of ring B in 2 and 4 and to C-2 of ring C in 3. The unusual catechin dicarboxylic acid dimer 4 was obtained by ortho cleavage of the E-ring. Hydroquinone served as both a shuttle oxidant and a reactant by coupling at C-2' and C-5' of the catechin B-ring during laccase oxidations. HRP and laccase oxidation products were compared to D,L-alpha-tocopherol and (+)-catechin for their abilities to inhibit iron-induced lipid peroxidation in rat brain homogenates and Fe(3+)-ADP/NADPH in rat liver microsomes, as measured by the intensity of thiobarbituric acid reactive substance. All metabolites exhibited anti-lipid peroxidation with IC(50) values approximately 2-8 times higher than those of standard compounds. Characteristic reaction products may prove to be novel markers for (+)-catechin antioxidant reactions in living systems.
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PMID:Novel oxidations of (+)-catechin by horseradish peroxidase and laccase. 1223 76

In this study, cDNA and genomic clones encoding a homologue of the yeast gene anti-oxidant 1 (ATX1) from the white-rot fungus Trametes versicolor, a basidiomycete known to produce several laccase isoenzymes involved in lignin degradation, were identified. This gene, named Trametes ATX homologue (tahA), encodes a protein of 7.9 kDa with 56% identity to the yeast Atx1p sequence. Two different alleles of tahA were obtained that differed mainly in their intervening sequences and in a 425 nt insertion located 183 nt upstream of the transcription start site. tahA is present as one copy per haploid nucleus in T. versicolor, as shown by Southern analysis. Expression of tahA cDNA restored high-affinity iron uptake in a deltaatx1 yeast strain and oxygen sensitivity in a deltasod1 deltasod2 yeast strain, showing that tahA is also a functional homologue of ATX1. The inability of tahA to rescue the deltasod1 phenotype on copper-deficient medium indicated that tahA function is copper-dependent. Sequence analysis of the tahA promoter revealed several motifs that were similar to the conserved motifs found in the copper-regulated metallothionein and Cu, Zn superoxide dismutase genes, CUP1 and SOD1, of Saccharomyces cerevisiae, Neurospora crassa and Candida glabrata. In contrast to its yeast homologue ATX1, tahA is induced under elevated copper concentrations in the medium (>0.25 micro M CuSO(4)) and repressed under copper starvation. The transcription of tahA was analysed in response to copper and iron, and after adding xenobiotica. The results are discussed in relevance to laccase expression.
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PMID:Identification and functional expression of tahA, a filamentous fungal gene involved in copper trafficking to the secretory pathway in Trametes versicolor. 1248 Sep 8

Various physiological parameters of Lentinula edodes (Shiitake) in the presence of nine heavy metal salts were investigated. The mycelial growth was highly sensitive to cadmium and mercury, but less sensitive to zinc, copper, and lead. This resistance can be particularly dangerous to humans in the case of edible fungi such as Shiitake because of the possible heavy metal accumulation during growth and fruiting body production. All of the tested heavy metals inhibited decolorization of the dye Poly R-478 and the production of manganese peroxidase to a greater extent than they inhibited growth. Interestingly, with the exception of iron, the addition of all heavy metal salts investigated led to the increase of laccase production. Apart from cadmium and iron, none of the heavy metals inhibited the in vitro enzyme activities in concentrations up to 3mM. The results of this study indicated the applicability of L. edodes in biosorption technologies used in the removal of toxic metals from contaminated effluents and in bioremediation technologies designed to treat complex wastes contaminated with heavy metals in addition to other xenobiotics.
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PMID:Effects of certain heavy metals on the growth, dye decolorization, and enzyme activity of Lentinula edodes. 1274 69

Cryptococcus neoformans secretes 3-hydroxyanthranilate (3HAA), but the utility is unknown. Exogenous 3HAA promoted growth of cultures starved for iron with transferrin, presumably by releasing Fe(III) reductively. Exogenous 3HAA protected C. neoformans from strong oxidants, suggesting a role in resistance to killing by immune cells. 3HAA represents an endogenous laccase substrate, in that crude laccase preparations convert 3HAA to cinnabarinic acid, whereas 3HAA concentrations are higher in Lac- mutants. We isolated hypersecreting mutants as highly fluorescent clones. Because C. neoformans has been isolated from rotting wood, we looked for a role in degradation of lignin. Using cyclic voltammetry, we found no electrochemical evidence that organic oxidation products of 3HAA are capable of oxidizing lignin. We found neither cellulose dehydrogenase nor lignin peroxidase enzymic activity, nor did C. neoformans grow on cellulose as carbon source. We found no evidence for production of Fenton reagent by cultures, even in the presence of transition metal ions or of those and 3HAA. The biological utility of 3HAA may be related to its functions as reducing agent and, conceivably, as laccase substrate. It does not appear to attack wood, nor does C. neoformans appear to have a mechanism to rot wood.
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PMID:3-Hydroxyanthranilate in Cryptococcus neoformans: a secreted reductant that does not enable wood rot. 1296 24

The Fet3 protein in Saccharomyces cerevisiae and mammalian ceruloplasmin are multicopper oxidases (MCO) that are required for iron homeostasis via their catalysis of the ferroxidase reaction, 4Fe(2+)+O(2)+4H(+)-->4Fe(3+)+2H(2)O. The enzymes may play an essential role in copper homeostasis since they exhibit a strikingly similar kinetic activity towards Cu(1+) as substrate. In contrast, laccase, an MCO that exhibits weak activity towards Fe(2+), exhibits a similarly weak activity towards Cu(1+). Kinetic analyses of the Fet3p reaction demonstrate that the ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme. These two ferroxidases are fully competent kinetically to play a major role in maintaining the cuprous-cupric redox balance in aerobic organisms.
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PMID:Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function. 1462 5

Ferroxidase activity was detected in a laccase-like multicopper oxidase (LMCO) produced in transgenic tobacco cells expressing an LMCO cDNA (Ltlacc2.2) cloned from yellow-poplar (Liriodendron tulipifera). This marks the first report of ferroxidase activity associated with a plant laccase and suggests that some members of this plant enzyme family may have physiological functions based on activities other than their more widely recognized phenoloxidase activity. Recent work with LMCOs from bacteria, yeast and mammals has shown that metal oxidase activities in these enzymes can be important for their primary physiological functions, With respect to ferroxidase activity in certain plant LMCOs, it is proposed that the high levels of LMCO expression in plant vascular tissues may reflect the need for high-efficiency iron uptake pumps in tissues that undergo lignification during normal development. Such iron uptake pumps would function to minimize levels of free iron so that reactive oxygen species do not reach toxic levels when H2O2 is generated for peroxidase-mediated monolignol coupling during lignin deposition.
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PMID:Ferroxidase activity in a laccase-like multicopper oxidase from Liriodendron tulipifera. 1506 Oct 81

This report represents the conclusions of a Joint FAO/WHO Expert Committee convened to evaluate the safety of various food additives, with a view to recommending acceptable daily intakes (ADIs) and to prepare specifications for the identity and purity of food additives. The first part of the report contains a general discussion of the principles governing the toxicological evaluation of food additives (including flavouring agents) and contaminants, assessments of intake, and the establishment and revision of specifications for food additives. A summary follows of the Committee's evaluations of toxicological and intake data on various specific food additives (alpha-amylase from Bacillus lichenformis containing a genetically engineered alpha-amylase gene from B. licheniformis, annatto extracts, curcumin, diacetyl and fatty acid esters of glycerol, D-tagatose, laccase from Myceliophthora thermophila expressed in Aspergillus oryzae, mixed xylanase, beta-glucanase enzyme preparation produced by a strain of Humicola insolens, neotame, polyvinyl alcohol, quillaia extracts and xylanase from Thermomyces lanuginosus expressed in Fusarium venenatum), flavouring agents, a nutritional source of iron (ferrous glycinate, processed with citric acid), a disinfectant for drinking-water (sodium dichloroisocyanurate) and contaminants (cadmium and methylmercury). Annexed to the report are tables summarizing the Committee's recommendations for ADIs of the food additives, recommendations on the flavouring agents considered, and tolerable intakes of the contaminants considered, changes in the status of specifications and further information requested or desired.
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PMID:Evaluation of certain food additives and contaminants. 1535 33

Completed genome sequences have made it clear that multicopper oxidases related to laccase are widely distributed as multigene families in higher plants. Laccase-like multicopper oxidase (LMCO) sequences culled from GenBank and the Arabidopsis thaliana genome, as well as those from several newly cloned genes, were used to construct a gene phylogeny that clearly divided plant LMCOs into six distinct classes, at least three of which predate the evolutionary divergence of angiosperms and gymnosperms. Alignments of the predicted amino acid sequences highlighted regions of variable sequence flanked by the highly conserved copper-binding domains that characterize members of this enzyme family. All of the predicted proteins contained apparent signal sequences. The expression of 13 of the 17 LMCO genes in A. thaliana was assessed in different tissues at various stages of development using RT-PCR. A diversity of expression patterns was demonstrated with some genes being expressed in a constitutive fashion, while others were only expressed in specific tissues at a particular stage of development. Only a few of the LMCO genes were expressed in a pattern that could be considered consistent with a major role for these enzymes in lignin deposition. These results are discussed in the context of other potential physiological functions for plant LMCOs, such as iron metabolism and wound healing.
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PMID:Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana. 1594 Apr 65

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

Previous studies have demonstrated an important role for the vacuole in the virulence of the fungus Cryptococcus and studies in yeast have implicated the vacuolar protein Vps41 in copper loading of proteins such as iron transporters. However, our studies found that a cryptococcal vps41Delta strain displayed wild-type growth on media containing iron and copper chelators and normal activity of the copper-containing virulence factor laccase as well as almost normal growth at 37 degrees C and wild-type production of the virulence factor capsule. Despite these attributes, the vps41Delta mutant strain showed a dramatic attenuation of virulence in mice and co-incubation of mutant cells with the macrophage cell line, J774.16, resulted in a dramatic loss in viability of the vps41Delta mutant strain at 10 h compared with wild-type and complemented strains. Closer examination revealed that the vps41Delta mutant displayed a dramatic loss in viability after nutrient starvation which was traced to a failure to undergo G2 arrest, but there was no defect in the formation of autophagic or proteolytic vesicles. Our results indicate that VPS41 plays a key role in regulating starvation response in this pathogenic organism and that defects in cell cycle arrest are associated with attenuated pathogenic fitness in mammalian hosts.
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PMID:Role of a VPS41 homologue in starvation response, intracellular survival and virulence of Cryptococcus neoformans. 1687 14


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