Disease relevance of Chrysosporium

• Pathways for the degradation of 3,5-dimethyl-4-hydroxy-azobenzene-4'-sulfonic acid (I) and 3-methoxy-4-hydroxyazobenzene-4'-sulfonamide (II) by the manganese peroxidase and ligninase of Phanerochaete chrysosporium and by the peroxidase of Streptomyces chromofuscus have been proposed [1].
• For both P. chrysosporium and P. putida, all ketones showed a higher toxicity than their corresponding alcohol derivatives [2].
• Enhanced production of manganese peroxidase from immobilized Phanerochaete chrysosporium due to the increased autolysis of chlamydospore-like cells [3].

High impact information on Chrysosporium

• Phanerochaete chrysosporium and other fungi mineralize TNT under ligninolytic conditions by converting it into reduced TNT intermediates, which are excreted to the external milieu, where they are substrates for ligninolytic enzymes [4].
• Binding properties of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium against a synthetic lignin (dehydrogenated polymerizate, DHP) were studied with a resonant mirror biosensor [5].
• Our studies here show that the white-rot fungus Phanerochaete chrysosporium produces extracellular oxalate under conditions that induce synthesis of the ligninolytic system [6].
• The H2O2-requiring ligninase of the basidiomycete Phanerochaete chrysosporium oxidatively cleaves both lignin and lignin model compounds between C alpha and C beta (C-1 and C-2) of their aliphatic side chains [7].
• One is similar to Phanerochaete chrysosporium manganese-dependent peroxidase [8].

Chemical compound and disease context of Chrysosporium

• Mineralization of sulfonated azo dyes and sulfanilic acid by Phanerochaete chrysosporium and Streptomyces chromofuscus [9].
• Homologous expression of recombinant MnP isozyme 1 (rMnP1) in P. chrysosporium was achieved using a novel transformation system for this fungus, which utilizes the Streptomyces hygroscopicus bialaphos-resistant gene, bar, as the selectable marker [10].

Biological context of Chrysosporium

• Manganese peroxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Transient state kinetics and reaction mechanism [11].
• The biotransformation of 2,4,6-trinitrotoluene (TNT) (175 microM) by Phanerochaete chrysosporium with molasses and citric acid at pH 4.5 was studied [12].
• Exonuclease III and dam methylation analyses, respectively, indicated that pG12-I undergoes replication in P. chrysosporium and that it is maintained extrachromosomally in a circular form [13].
• Previously, we reported that Arg177 is involved in MnII binding at the MnII binding site of manganese peroxidase isozyme 1 (MnP1) of Phanerochaete chrysosporium by examining two mutants: R177A and R177K [14].
• Mycelia of the lignin-degrading fungus Phanerochaete chrysosporium consume O2 and produce extracellular H2O2 when incubated with fatty acyl-CoA substrates, even in the presence of mitochondrial respiratory chain inhibitors such as antimycin A and cyanide [15].

Anatomical context of Chrysosporium

• Therefore, we conclude that the extracellular BGL from P. chrysosporium is primarily a glucan 1,3-beta-glucosidase (EC 3.2.1.58), which might play a role on fungal cell wall metabolism, rather than a beta-glucosidase (EC 3.2.1.21), which might be involved in the hydrolysis of beta-1,4-glucosidic compounds during cellulose degradation [16].

Associations of Chrysosporium with chemical compounds

• Manganese peroxidase from the lignin-degrading fungus Phanerochaete chrysosporium catalyzes the H2O2-dependent oxidation of Mn2+ to Mn3+ [17].
• Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds [18].
• Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators [19].
• The possible involvement of hydrogen peroxide (H2O2)-derived hydroxyl radical (.OH) in lignin degradation ([14C]lignin leads to 14CO2) by Phanerochaete chrysosporium was investigated [20].
• Diarylpropane oxygenase, an H2O2-dependent lignin-degrading enzyme from the basidiomycete fungus Phanerochaete chrysosporium, catalyzes the oxygenation of various lignin model compounds with incorporation of a single atom of dioxygen (O2) [21].

Gene context of Chrysosporium

• The genomic clone (gleu2) was subsequently isolated and was used successfully as a selectable marker to transform P. chrysosporium auxotrophs for LEU2 [22].
• N0300 is 76% identical to YCR107w, a hypothetical protein of yeast chromosome III, and 55% identical to a ligninolytic aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium [23].
• The coding sequence of the TRP1 gene was interrupted by a single intron of 48 bases, the position and flanking sequences of which were highly homologous to those of basidiomycete Phanerochaete chrysosporium trpC [24].
• The P. chrysosporium trpC gene encodes a single protein containing three enzyme activities involved in tryptophan biosynthesis arranged in the order: NH2-GAT-IGPS-PRAI-COOH [25].
• The glyceraldehyde-3-phosphate dehydrogenase (gpd) promoter was used to drive expression of lip2, the gene encoding lignin peroxidase (LiP) isozyme H8, in primary metabolic cultures of Phanerochaete chrysosporium [26].

Analytical, diagnostic and therapeutic context of Chrysosporium

• Circular dichroism spectra of the phenanthrene trans-9,10-dihydrodiol indicated that the absolute configuration of the predominant enantiomer was 9R,10R, which is different from that of the principal enantiomer produced by Phanerochaete chrysosporium [27].
• Southern blot analysis suggests the presence of only a single gene for CDH in P. chrysosporium OGC101 [28].
• Pyranose 2-oxidase (P2O) was purified 43-fold to apparent homogeneity from the basidiomycete Phanerochaete chrysosporium using liquid chromatography on phenyl Sepharose, Mono Q (twice) and phenyl Superose [29].
• Cultures of a bronchoalveolar lavage and protected brush specimen revealed the presence of fungal elements that were identified as Emmonsia parva var. parva [30].
• Production of manganese-dependent peroxidase in a new solid-state bioreactor by Phanerochaete chrysosporium grown on wood shavings. Application to the decolorization of synthetic dyes [31].

References