Versatile peroxidase

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Versatile peroxidase
Identifiers
EC number 1.11.1.16
CAS number 42613-30-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Versatile 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 oxidized Reactive Black 5 + 2 H2O
(2) donor + H2O2 oxidized donor + 2 H2O

Versatile peroxidase is a hemoprotein.

References[edit]

  1. ^ Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez AT (April 1996). "Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii". European Journal of Biochemistry. 237 (2): 424–32. doi:10.1111/j.1432-1033.1996.0424k.x. PMID 8647081. 
  2. ^ Heinfling A, Ruiz-Dueñas FJ, Martínez MJ, Bergbauer M, Szewzyk U, Martínez AT (May 1998). "A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta". FEBS Letters. 428 (3): 141–6. doi:10.1016/s0014-5793(98)00512-2. PMID 9654123. 
  3. ^ Ruiz-Dueñas FJ, Martínez MJ, Martínez AT (January 1999). "Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii". Molecular Microbiology. 31 (1): 223–35. doi:10.1046/j.1365-2958.1999.01164.x. PMID 9987124. 
  4. ^ Camarero S, Sarkar S, Ruiz-Dueñas FJ, Martínez MJ, Martínez 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): 10324–30. doi:10.1074/jbc.274.15.10324. PMID 10187820. 
  5. ^ Ruiz-Dueñas FJ, Martínez MJ, Martínez 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): 4705–7. PMC 91631Freely accessible. PMID 10508113. 
  6. ^ Camarero S, Ruiz-Dueñas FJ, Sarkar S, Martínez MJ, Martínez 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): 37–43. doi:10.1016/s0378-1097(00)00367-0. PMID 11004397. 
  7. ^ Ruiz-Dueñas FJ, Camarero S, Pérez-Boada M, Martínez MJ, Martínez AT (May 2001). "A new versatile peroxidase from Pleurotus". Biochemical Society Transactions. 29 (Pt 2): 116–22. doi:10.1042/0300-5127:0290116. PMID 11356138. 
  8. ^ Banci L, Camarero S, Martínez AT, Martínez MJ, Pérez-Boada M, Pierattelli R, Ruiz-Dueñas 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): 751–60. doi:10.1007/s00775-003-0476-1. PMID 12884090. 
  9. ^ Pérez-Boada M, Ruiz-Dueñas FJ, Pogni R, Basosi R, Choinowski T, Martínez MJ, Piontek K, Martínez 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): 385–402. doi:10.1016/j.jmb.2005.09.047. PMID 16246366. 
  10. ^ 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): 916–22. PMC 91123Freely accessible. PMID 10049842. 

External links[edit]