[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/versatile-peroxidase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/versatile-peroxidase-wikipedia\/","headline":"Versatile peroxidase – Wikipedia","name":"Versatile peroxidase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Versatile peroxidase (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with","datePublished":"2017-06-02","dateModified":"2017-06-02","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/versatile-peroxidase-wikipedia\/","wordCount":4099,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Versatile peroxidase (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive-black-5:hydrogen-peroxide oxidoreductase.[1][2][3][4][5][6][7][8][9][10] This enzyme catalyses the following chemical reaction(1) Reactive Black 5 + H2O2       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4\u21cc{displaystyle rightleftharpoons } oxidized Reactive Black 5 + 2 H2O(2) donor + H2O2\u21cc{displaystyle rightleftharpoons } oxidized donor + 2 H2OVersatile peroxidase is a hemoprotein.References[edit]^ Mart\u00ednez MJ, Ruiz-Due\u00f1as FJ, Guill\u00e9n F, Mart\u00ednez AT (April 1996). “Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii”. European Journal of Biochemistry. 237 (2): 424\u201332. doi:10.1111\/j.1432-1033.1996.0424k.x. PMID\u00a08647081.^ Heinfling A, Ruiz-Due\u00f1as FJ, Mart\u00ednez MJ, Bergbauer M, Szewzyk U, Mart\u00ednez AT (May 1998). “A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta”. FEBS Letters. 428 (3): 141\u20136. doi:10.1016\/s0014-5793(98)00512-2. PMID\u00a09654123.^ Ruiz-Due\u00f1as FJ, Mart\u00ednez MJ, Mart\u00ednez AT (January 1999). “Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii”. Molecular Microbiology. 31 (1): 223\u201335. doi:10.1046\/j.1365-2958.1999.01164.x. PMID\u00a09987124.^ Camarero S, Sarkar S, Ruiz-Due\u00f1as FJ, Mart\u00ednez MJ, Mart\u00ednez AT (April 1999). “Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites”. The Journal of Biological Chemistry. 274 (15): 10324\u201330. doi:10.1074\/jbc.274.15.10324. PMID\u00a010187820.^ Ruiz-Due\u00f1as FJ, Mart\u00ednez MJ, Mart\u00ednez AT (October 1999). “Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates”. Applied and Environmental Microbiology. 65 (10): 4705\u20137. PMC\u00a091631. PMID\u00a010508113.^ Camarero S, Ruiz-Due\u00f1as FJ, Sarkar S, Mart\u00ednez MJ, Mart\u00ednez AT (October 2000). “The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases”. FEMS Microbiology Letters. 191 (1): 37\u201343. doi:10.1016\/s0378-1097(00)00367-0. PMID\u00a011004397.^ Ruiz-Due\u00f1as FJ, Camarero S, P\u00e9rez-Boada M, Mart\u00ednez MJ, Mart\u00ednez AT (May 2001). “A new versatile peroxidase from Pleurotus”. Biochemical Society Transactions. 29 (Pt 2): 116\u201322. doi:10.1042\/0300-5127:0290116. PMID\u00a011356138.^ Banci L, Camarero S, Mart\u00ednez AT, Mart\u00ednez MJ, P\u00e9rez-Boada M, Pierattelli R, Ruiz-Due\u00f1as FJ (September 2003). “NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii”. Journal of Biological Inorganic Chemistry. 8 (7): 751\u201360. doi:10.1007\/s00775-003-0476-1. PMID\u00a012884090.^ P\u00e9rez-Boada M, Ruiz-Due\u00f1as FJ, Pogni R, Basosi R, Choinowski T, Mart\u00ednez MJ, Piontek K, Mart\u00ednez AT (November 2005). “Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways”. Journal of Molecular Biology. 354 (2): 385\u2013402. doi:10.1016\/j.jmb.2005.09.047. PMID\u00a016246366.^ Caramelo L, Martinez MJ, Martinez AT (March 1999). “A search for ligninolytic peroxidases in the fungus pleurotus eryngii involving alpha-keto-gamma-thiomethylbutyric acid and lignin model dimers”. Applied and Environmental Microbiology. 65 (3): 916\u201322. PMC\u00a091123. 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