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

Versatile peroxidase
Identifiers
EC no.1.11.1.16
CAS no.42613-30-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
(1) Reactive Black 5 + H2O2 oxidized Reactive Black 5 + 2 H2O
(2) donor + H2O2 oxidized donor + 2 H2O

Versatile peroxidase is a hemoprotein.

References

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  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. hdl:10261/169700. 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 91631. 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 91123. PMID 10049842.
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