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Basidiomycete peroxidases

After the above survey on the general molecular structure of the different types of heme peroxidases, a more detailed analysis on the catalytic sites of some heme peroxidases of particular biotechnological interest produced by fungi is presented in Sects. 3.3-3.5. Previously, a description of the biotechnological interest of these enzymes, followed by a structural classification and evolutionary analysis of all the basidiomycete peroxidases, whose sequence is known to date, is presented in the two subsections included below. For a full evolutionary analysis of heme peroxidases, see Chap. 2. [Pg.43]


Ruiz-Duenas FJ, Morales M, Garcia E et al (2009) Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J Exp Bot 60 441 152... [Pg.34]

Harazono K, Watanabe Y, Nakamura K (2003) Decolorization of azo dye by the white-rot basidiomycete Phanerochaete sordida and by ts manganese peroxidase. J Biosci Bioeng 95(5) 455 195... [Pg.168]

Gold MH, Wariishi H,Valli K (1989) Extracellular peroxidases involved in lignin degradation by the white rot basidiomycete Phanerochaete chrysosporium. In Whitaker JR, Sonnet PE (eds) Biocatalysis in agricultural biotechnology. ACS symposium series 389. American Chemical Society, Washington, D.C., p 127 Thomas JA, Morris DR, Hager LP (1970) J Biol Chem 245 3135... [Pg.104]

Wariishi, H. Valli, K. Gold, M.M. H. Manganese (II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 1992, 267, 23688-23695. [Pg.498]

The purpose of the present paper is to describe the aromatic ring cleavage of lignin substructure model compounds by white-rot basidiomycetes and by lignin peroxidase of P. chrysosporium. The aromatic ring cleavage of synthetic lignin (DHP) by the enzyme will also be described. [Pg.504]

The same authors also investigated the kinetic resolution of racemic hydroperoxides with Coprinus peroxidase (CiP), isolated from the basidiomycete Coprinus cinereus... [Pg.337]

Renganathan V, Miki K, Gold MH (1987) Haloperoxidase Reactions Catalyzed by Lignin Peroxidase, an Extracellular Enzyme from the Basidiomycete Phanerochaete chrysospo-rium. Biochemistry 26 5127... [Pg.488]

Joshi DK, Gold MH. Oxidation of dibenzo-p-dioxin by lignin peroxidase from the Basidiomycete Phanerochaete chrysosporium. Biochem 1994 33 10969-10976. [Pg.473]

At least 87 basidiomycete heme peroxidases have been described to date, whose evolutionary relationships are shown in Fig. 3.3. It also includes putative peroxidases from the genomes of Phanerochaete chrysosporium, Pleurotus ostreatus. and Pycnoporus cinnabarinus, and two reference ascomycete peroxidases. [Pg.44]

Fig. 3.3 Dendrogram of evolutionary relationships between 87 basidiomycete (and two reference ascomycete) peroxidases, including structural-functional classification based on Ruiz-Duenas et al. [10] (GeneBank and P. ostreatus genome references in parentheses). Amino acid sequence comparisons as Poisson distances and clustering based on UPGMA and pair-wise deletion option of MEGA4 [43]... Fig. 3.3 Dendrogram of evolutionary relationships between 87 basidiomycete (and two reference ascomycete) peroxidases, including structural-functional classification based on Ruiz-Duenas et al. [10] (GeneBank and P. ostreatus genome references in parentheses). Amino acid sequence comparisons as Poisson distances and clustering based on UPGMA and pair-wise deletion option of MEGA4 [43]...

See other pages where Basidiomycete peroxidases is mentioned: [Pg.43]    [Pg.44]    [Pg.46]    [Pg.43]    [Pg.44]    [Pg.46]    [Pg.141]    [Pg.282]    [Pg.204]    [Pg.187]    [Pg.180]    [Pg.188]    [Pg.236]    [Pg.263]    [Pg.426]    [Pg.454]    [Pg.504]    [Pg.513]    [Pg.555]    [Pg.368]    [Pg.197]    [Pg.358]    [Pg.52]    [Pg.71]    [Pg.23]    [Pg.28]    [Pg.30]    [Pg.30]    [Pg.34]    [Pg.39]    [Pg.43]    [Pg.44]    [Pg.44]   
See also in sourсe #XX -- [ Pg.43 , Pg.44 , Pg.45 ]




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Evolutionary Relationships of Basidiomycete Peroxidases

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