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)

Syringaldazine did not turn purple on cross sections of tree branches or saplings or on cambial tissue cultures unless hydrogen peroxide was added; this indicated the absence of laccase but presence of peroxidase in lignifying cells. Peroxidase, therefore, apparently is the only en enzyme that polymerizes p-coumaryl alcohols to lignin in trees.
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PMID:Lignification in trees: indication of exclusive peroxidase participation. 1781 89

Research was conducted to evaluate the potential use of laccase and its susceptibility to inactivation in an alternative enzyme-based treatment technology to remove parent phenol from buffered distilled water. Enzymatic oxidative polymerization of phenol with laccase was carried out in continuously stirred batch reactors. The reaction products were insoluble polymers, which precipitated out of the solution once their solubility limits were exceeded. The findings demonstrated that the polymeric products had significant effects on enzyme activity consumption and subsequent phenol removal. Enzyme species present in the reaction vessel were classified into enzyme remaining in the solution (type 1) and enzyme adhering to the precipitate polymers (type 2). Type 1 enzyme was more efficient in removal of phenol from solution compared with type 2. Subsequent filtration enhanced the phenol removal by removing type 2 enzyme adhering to the polymer particles and decelerating enzyme inactivation. The study also investigated the effects of available dissolved oxygen, provided through aeration and hydrogen peroxide addition, on phenol removal. Aeration and hydrogen peroxide addition increased the dissolved oxygen concentration, but had no effect on the progress curve for phenol removal.
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PMID:Inactivation of enzyme laccase and role of cosubstrate oxygen in enzymatic removal of phenol from water. 1782 32

Fungal laccases are remarkable green catalysts that have a broad substrate specificity and many potential applications in bioremediation, lignocellulose processing, organic synthesis, and more. However, most of these transformations must be carried out at high concentrations of organic cosolvents in which laccases undergo unfolding, thereby losing their activity. We have tailored a thermostable laccase that tolerates high concentrations of cosolvents, the genetic product of five rounds of directed evolution expressed in Saccharomyces cerevisiae. This evolved laccase--R2 variant--was capable of resisting a wide array of cosolvents at concentrations as high as 50% (v/v). Intrinsic laccase features such as the redox potential and the geometry of catalytic copper varied slightly during the course of the molecular evolution. Some mutations at the protein surface stabilized the laccase by allowing additional electrostatic and hydrogen bonding to occur.
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PMID:In vitro evolution of a fungal laccase in high concentrations of organic cosolvents. 1788 37

Intramolecular M(II)...H-C interactions (M(II)=Cu(II), Pd(II)) involving a side chain alkyl group of planar d8 and d9 metal complexes of the N-alkyl (R) derivatives of N,N-bis(2-pyridylmethyl)amine with an N3Cl donor set were established by structural and spectroscopic methods. The methyl group from the branched alkyl group (R=2,2-dimethylpropyl and 2-methylbutyl) axially interacts with the metal ion with the M...C and M...H distances of 3.056(3)-3.352(9) and 2.317(1)-2.606(1) A, respectively, and the M-H-C angles of 122.4-162.3 degrees . The Cu(II) complexes showing the interaction have a higher redox potential as compared with those without it, and the (1)H NMR signals of the interacting methyl group in Pd(II) complexes shifted downfield relative to the ligand signals. Dependence of the downshift values on the dielectric constants of the solvents used indicated that the M(II)...H-C interaction is mainly electrostatic in nature and may be regarded as a weak hydrogen bond. Implications for possible environmental effects of the leucine alkyl group at the type 1 Cu site of fungal laccase are also discussed.
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PMID:CH...Metal(II) axial interaction in planar complexes (metal=Cu, Pd) and implications for possible environmental effects of alkyl groups at biological copper sites. 1823 44

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

Different operating conditions (viz. pulp consistency, oxygen pressure and treatment time) in the biobleaching of eucalyptus kraft pulp with the laccase-HBT system was tested in order to describe their effect and normalize a biobleaching protocol. A high O(2) pressure (0.6MPa) was found to result in improved laccase-assisted delignification of the pulp. Also, a high pulp consistency (10%) and a short treatment time (2h) proved the best choices with a view to obtaining good pulp properties (kappa number and ISO brightness) under essentially mild conditions. The laccase-HBT treatment was found to result in slight delignification (in the form of a 20-27% decrease in kappa number); however, an alkaline extraction stage raised delignification to 41-45%, a much higher level than those obtained in the control tests (16-23%). Also, the use of hydrogen peroxide in the extraction stage resulted in improved brightness (14-19%), but in scarcely improved delignification (4-7%). Treating the pulp with the laccase-HBT system reduced the amount of hydrogen peroxide required for subsequent alkaline bleaching by a factor of 3-4 relative to control tests.
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PMID:Laccase-HBT bleaching of eucalyptus kraft pulp: influence of the operating conditions. 1849 77

Oxygen-reducing enzyme electrodes are prepared from laccase of Trametes versicolor and a series of osmium-based redox polymer mediators covering a range of redox potentials from 0.11 to 0.85 V. Experimentally obtained current density generated by the film electrodes is analyzed using a one-dimensional numerical model to obtain kinetic parameters. The bimolecular rate constant for mediation is found to vary with mediator redox potential from 250 s(-1) M(-1) when mediator and enzyme are close in redox potential to 9.4 x 10(4) s(-1) M(-1) when the redox potential difference is large. The value of the bimolecular rate constant for the simultaneously occurring laccase-oxygen reaction is found to be 2.4 x 10(5) s(-1) M(-1). The relationship between mediator-enzyme overpotential and bimolecular rate constant is used to determine the optimum mediator redox potential for maximum power output of a hypothetical biofuel cell with a planar cathode and a reversible hydrogen anode. For laccase of T. versicolor (E(e)(0) = 0.82), the optimum mediator potential is 0.66 V (SHE), and a molecular structure is presented to achieve this result.
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PMID:Kinetics of redox polymer-mediated enzyme electrodes. 1854 May 77

A novel bacterial species identified as Exiguobacterium sp. RD3 degraded the diazo dye reactive yellow 84A (50 mg l(-1)) within 48 h at static condition, at 30 degrees C and pH 7. Lower salinity conditions were found to be favorable for growth and decolorization. Enzymatic activities of an H(2)O(2) independent oxidase along with laccase and an azoreductase suggest their prominent role during the decolorization of reactive yellow 84A. Presence of an H(2)O(2) independent oxidase in Exiguobacterium sp. RD3 was confirmed and hydrogen peroxide produced was detected by a coupled iodometric assay. Azoreductase activity was prominent in presence of cofactors NADH and NADP in mineral salt medium. Considerable depletion of COD of the dye solution during degradation of dye was indicative of conversion of complex dye into simple oxidizable products. Products of degradation were analyzed by HPLC, FTIR and GCMS. A possible product of the degradation was identified by GCMS. Degradation of dye resulted with significant reduction of phytotoxicity, confirming the environmentally safe nature of the degradation metabolites.
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PMID:Coordinate action of exiguobacterial oxidoreductive enzymes in biodegradation of reactive yellow 84A dye. 1880

Melanocarpus albomyces laccase crystals were soaked with 2,6-dimethoxyphenol, a common laccase substrate. Three complex structures from different soaking times were solved. Crystal structures revealed the binding of the original substrate and adducts formed by enzymatic oxidation of the substrate. The dimeric oxidation products were identified by mass spectrometry. In the crystals, a 2,6-dimethoxy-p-benzoquinone and a C-O dimer were observed, whereas a C-C dimer was the main product identified by mass spectrometry. Crystal structures demonstrated that the substrate and/or its oxidation products were bound in the pocket formed by residues Ala191, Pro192, Glu235, Leu363, Phe371, Trp373, Phe427, Leu429, Trp507 and His508. Substrate and adducts were hydrogen-bonded to His508, one of the ligands of type 1 copper. Therefore, this surface-exposed histidine most likely has a role in electron transfer by laccases. Based on our mutagenesis studies, the carboxylic acid residue Glu235 at the bottom of the binding site pocket is also crucial in the oxidation of phenolics. Glu235 may be responsible for the abstraction of a proton from the OH group of the substrate and His508 may extract an electron. In addition, crystal structures revealed a secondary binding site formed through weak dimerization in M. albomyces laccase molecules. This binding site most likely exists only in crystals, when the Phe427 residues are packed against each other.
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PMID:Structure-function studies of a Melanocarpus albomyces laccase suggest a pathway for oxidation of phenolic compounds. 1956 11


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