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  • 1
    Electronic Resource
    Electronic Resource
    A metabolic role of the glyoxylate and tricarboxylic acid cycles for development of the copper-tolerant brown-rot fungus Fomitopsis palustris (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 217 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Fruit bodies of the copper-tolerant brown-rot fungus Fomitopsis palustris were produced in liquid medium for the first time. To induce fruit body formation of this fungus, it was important to inoculate the liquid medium with mycelia grown on potato dextrose agar plates and also to adjust the initial pH of the medium to 5.0. The metabolic role of the glyoxylate and tricarboxylic acid cycles during fungal development in the liquid culture was investigated in relation to oxalate biosynthesis. The enzymes for the glyoxylate cycle and oxalate biosynthesis in mycelium showed greater activities at the vegetative growth stage than at the fruiting stage. The ratios of isocitrate dehydrogenase activity to isocitrate lyase activity in mycelium were 0.3 and 4.0 at the vegetative and fruiting stage, respectively. Thus, isocitrate lyase of the glyoxylate cycle played a more important role in oxalate synthesis at the earlier stage of the cultivation, whereas isocitrate dehydrogenase played a major role in glutamate synthesis during fruit body formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11449.x
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  • 2
    Electronic Resource
    Electronic Resource
    A proposed role of oxalic acid in wood decay systems of wood-rotting basidiomycetes (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 13 (1994), S. 0 
    Details
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: The possible roles of oxalic acid, veratryl alcohol, and manganese were investigated in relation to lignin biodegradation by white-rot basidiomycetes. Oxalate inhibited both lignin peroxidase (LiP) and manganese-peroxidase (MnP). and was decarboxylated by the mediation of veratryl alcohol and Mn. Oxalate was shown to regulate the mineralization of lignin in the in vivo system of Phanerochaete chrysosporium. In the brown-rot wood decay process, oxalic acid may serve as an acid catalyst as well as an electron donor for the Fenton reaction, to breakdown cellulose and hemicellulose. Oxaloacetase and glyoxylate oxidase may play a key role in production of oxalic acid by white-rot and brown-rot basidiomycetes such as Phanerochaete chrysosporium, Coriolus versicolor and Tyromyces palustris. A possible role of oxalate metabolism is discussed in relation to the physiology of wood-rotting fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6976.1994.tb00049.x
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  • 3
    Electronic Resource
    Electronic Resource
    Induction of L-phenylalanine ammonia-lyase and suppression of veratryl alcohol biosynthesis by exogenously added L-phenylalanine in a white-rot fungus Phanerochaete chrysosporium (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 179 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effects of exogenously added L-phenylalanine (L-Phe) on the activities of L-phenylalanine ammonia-lyase (PAL) and 3,4-dimethoxybenzyl alcohol (veratryl alcohol, VA) biosynthesis in ligninolytic cultures of Phanerochaete chrysosporium were investigated. Increasing PAL activity was detected in low nitrogen (LN) culture but not in high nitrogen (HN) culture. The addition of L-Phe into the LN culture caused a 25-fold increase in enzyme activity, which clearly shows that L-Phe, a substrate of the enzyme, served as an inducer of PAL. The increase in activity of PAL triggered by nitrogen starvation was correlated with biosynthesis of VA. However, PAL induced by the added L-Phe did not promote VA biosynthesis but suppressed the biosynthesis probably due to NH4+ released from L-Phe.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08742.x
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  • 4
    Electronic Resource
    Electronic Resource
    Suppressive effect of l-phenylalanine on manganese peroxidase in the white-rot fungus Phanerochaete chrysosporium (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 145 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The effect of added l-amino acids and NH4+ on manganese peroxidase activity in ligninolytic cultures of Phanerochaete chrysosporium were investigated. Among 11 amino acids (0.2 mM) tested, including phenylalanine, glutamate, glutamine, histidine, alanine, iso-leucine, ornithine, glycine, aspartate, proline, and arginine, phenylalanine was the most effective in suppression of manganese peroxidase synthesis. However, all the amino acids tested except proline completely suppressed the enzyme synthesis at 2 mM concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08560.x
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  • 5
    Electronic Resource
    Electronic Resource
    Suppressive effect of l-phenylalanine on lignin peroxidase in the white-rot fungus Phanerochaete chrysosporium (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 131 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The effects of added l-amino acids and on lignin peroxidase activity in ligninolytic cultures of Phanerochaete chrysosporium were investigated. Among 11 arnino acids tested, including phenylalanine, glutamate, glutamine, histidine, alanine, iso-leucine, ornithine, glycine, aspartate, proline, and arginine, phenylalanine was the most effective in suppression of lignin peroxidase synthesis. By contrast, glutamate and NH4+ enhanced the lignin peroxidase synthesis at lower concentrations (below 1 mM), but suppressed it significantly at higher concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07775.x
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  • 6
    Electronic Resource
    Electronic Resource
    Metabolism of a phenylcoumaran substructure lignin model compound in ligninolytic cultures of Phanerochaete chrysosporium (1981)
    Springer
    Archives of microbiology 128 (1981), S. 416-420 
    Details
    ISSN: 1432-072X
    Keywords: Lignin biodegradation ; White-rot fungi ; Fungus physiology ; Wood decay ; Aromatic metabolism ; Phanerochaete chrysosporium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The degradation of the phenylcoumaran substructure model compound methyl dehydrodiconiferyl alcohol by the white-rot wood decay fungus Phanerochaete chrysosporium was investigated using culture conditions optimized for lignin oxidation. Initial attack was in the cinnamyl alcohol side chain, which was oxidized to a glycerol structure. This was subsequently converted by loss of the two terminal carbon atoms, Cβ′ and Cγ′, to yield a Cα′-aldehyde structure, which was further oxidized to the Cα′-acid compound. The next detected intermediate, a phenylcoumarone, was produced by double bond formation between Cα and Cβ, and oxidation of the Cγ-alcohol to an aldehyde group. Further oxidation of Cγ to an acid yielded the next intermediate. The final identified degradation product was veratric acid. No products from the 5-substituted aromatic ring, and no phenolic products, were found. The initial glycerol-containing intermediate was a mixture of the threo and erythro forms, and no optical activity could be found, suggesting that its formation might have involved nonstereospecific Cα′-Cβ′ epoxidation followed by non-enzymatic hydrolysis of the epoxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00405924
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  • 7
    Electronic Resource
    Electronic Resource
    A Phanerochaete chrysosporium mutant defective in lignin degradation as well as several other secondary metabolic functions (1982)
    Springer
    Archives of microbiology 132 (1982), S. 115-122 
    Details
    ISSN: 1432-072X
    Keywords: Phanerochaete chrysosporium ; Lignin degradation ; Veratryl alcohol ; Secondary metabolism ; Mutants ; Phenol oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A pleiotropic mutant of Phanerochaete chrysosporium 104-2 lacking phenol oxidase and unable to form fruit bodies and a revertant strain 424-2 were isolated after UV mutagenesis. Strains 104-2 and 424-2 had no apparent dysfunction in primary metabolism with glucose as a carbon source. Unlike the wild type strain and strain 424-2, strain 104-2 was unable to evolve 14CO2 from 14C ring, side chain and 3-O-14C-methoxy labeled lignin. In addition, strain 104-2 was unable to evolve 14CO2 from a variety of lignin model compounds including 14C-4′-methoxy labeled veratrylglycerol-β-guaiacyl (V) ether, γ-14C-guaiacylglycerol-β-guaiacyl ether (VI), as well as 1-(14C-4′-methoxy, 3′-methoxyphenyl)1,2 propene (III) and 1-(14C-4′-methoxy-3′-methoxyphenyl) 1,2 dihydroxypropane (IV). The addition of peroxidase/H2O2 to cultures of strain 104-2 did not alter its capacity to degrade the labeled lignins. A variety of unlabeled lignin model compounds previously shown to be degraded by the wild type organism including β-aryl ether dimers and diaryl propane dimers were also not degraded by the mutant 104-2. The revertant strain 424-2 regained the capacity to degrade these compounds. The substrates described are degraded by oxygen requiring system(s) expressed during the secondary phase of growth, suggesting this pleiotropic mutant is possibly defective in the onset of postprimary metabolism. The inability of the mutant to produce the secondary metabolite veratryl alcohol and to elaborate enzymes in the veratryl alcohol biosynthetic pathway supports this hypothesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00508715
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  • 8
    Electronic Resource
    Electronic Resource
    Direct cleavage of the vicinal diol linkage of the lignin model compound dihydroanisoin by the basidiomycete Phanerochaete chrysosporium (1983)
    Springer
    Archives of microbiology 134 (1983), S. 299-302 
    Details
    ISSN: 1432-072X
    Keywords: Phanerochaete chrysosporium ; Vicinal diol cleavage ; Lignin model compounds ; Dihydroanisoin ; Anlsyl alcohol ; White rot basidiomycete ; Anisaldehyde ; Cytochrome P-450 ; Activated oxygen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The white rot basidiomycete Phanerochaete chrysosporium metabolized dihydroanisoin (1,2-dianisylethane-1,2 diol) in low nitrogen stationary cultures, conditions under which the ligninolytic system is expressed. Anisyl alcohol was isolated as a metabolic product indicating an initial diol bond cleavage of the substrate. Use of 3H-labeled dihydroanisoin (1,2-dianisylethane-1,2-diol-1,2 3H) indicated that the diol bond was cleaved directly, yielding anisyl aldehyde as the initial product. The metabolically stable ketol anisoin was shown not be an intermediate in the metabolism of dihydroanisoin. The diol cleavage reaction was dependent on the concentration of molecular oxygen but O2 could be replaced by H2O2 under some conditions. The cleavage reaction was inhibited by exogenously-added tyrosine2-Cu2+ complex (TCC). The appearance of the fungal diol cleavage system parallels the appearance of the ligninolytic system under a variety of physiological conditions. In addition, preincubation of ligninolytic cultures with 2.5 mM l-glutamate represses both the ligninolytic and the diol cleavage activities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407806
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  • 9
    Electronic Resource
    Electronic Resource
    Biosynthesis of the secondary metabolite veratryl alcohol in relation to lignin degradation in Phanerochaete chrysosporium (1981)
    Springer
    Archives of microbiology 129 (1981), S. 321-324 
    Details
    ISSN: 1432-072X
    Keywords: White-rot fungi ; Secondary metabolism ; Wood decay ; Mycelial pellets ; Fungus physiology ; l-Glutamic acid repression ; Phenylalanine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The lignin-degrading basidiomycete Phanerochaete chrysosporium synthesizes veratryl alcohol (3,4-dimethoxybenzyl alcohol) via phenylalanine, 3,4-dimethoxycinnamyl alcohol and veratrylglycerol. Study of the conversion of 3,4-dimethoxycinnamyl alcohol to veratrylglycerol and veratryl alcohol showed is to be (a) catalyzed by a secondary metabolic system, (b) markedly suppressed by culture agitation, and (c) strongly inhibited by l-glutamate. The amount of veratryl alcohol synthesized de novo was positively correlated with the O2 concentration after primary growth. Other work has shown that the cinnamyl alcohol terminal residue in a lignin substructure model compound is degraded via arylglycerol and benzyl alcohol structures in ligninolytic cultures of P. chrysosporium, and that the ligninolytic system exhibits traits (a)-(c) above. Ligninolytic activity is also strongly and positively correlated with O2 concentration. The results here suggest, therefore, that the actual biosynthetic secondary metabolic product is 3,4-dimethoxycinnamyl alcohol, but that this is degraded by the ligninolytic system to veratryl alcohol via veratrylglycerol. Veratryl alcohol is only slowly metabolized by the fungus, and accumulates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414706
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  • 10
    Electronic Resource
    Electronic Resource
    The time is ripe for an English journal from Japan on wood science (1998)
    Springer
    Journal of wood science 44 (1998), S. 2-2 
    Details
    ISSN: 1611-4663
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00521866
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