New and classic families of secreted fungal heme peroxidases
Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant comp...
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Veröffentlicht in: | Applied microbiology and biotechnology 2010-07, Vol.87 (3), p.871-897 |
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description | Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments. |
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Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-010-2633-0</identifier><identifier>PMID: 20495915</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Amino Acid Sequence ; Basidiomycota ; Biocatalysts ; Biodegradation ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Catalysis ; Classification ; Enzymes ; Fundamental and applied biological sciences. 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For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</description><subject>Amino Acid Sequence</subject><subject>Basidiomycota</subject><subject>Biocatalysts</subject><subject>Biodegradation</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Catalysis</subject><subject>Classification</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. 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For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>20495915</pmid><doi>10.1007/s00253-010-2633-0</doi><tpages>27</tpages></addata></record> |
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subjects | Amino Acid Sequence Basidiomycota Biocatalysts Biodegradation Biological and medical sciences Biomedical and Life Sciences Biotechnology Catalysis Classification Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fungi Fungi - chemistry Fungi - classification Fungi - enzymology Fungi - genetics Heme - metabolism Life Sciences Lignin Manganese Microbial Genetics and Genomics Microbiology Mini-Review Molecular Sequence Data Multigene Family Oxidation Oxygen transfer P450 peroxidases Peroxidases - chemistry Peroxidases - genetics Peroxidases - metabolism Peroxygenases Phenols Phylogeny Physiology Protein Transport Proteins Sequence Alignment Thyroid gland |
title | New and classic families of secreted fungal heme peroxidases |
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