Versatile peroxidase

Versatile peroxidase
Identifiers
EC number 1.11.1.16
CAS number 114995-15-2&title= 42613-30-9, 114995-15-2
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

  1. ↑ Martínez, M.J.; Ruiz-Dueñas, F.J.; Guillén, F.; Martínez, A.T. (1996). "Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii". Eur. J. Biochem. 237 (2): 424–432. doi:10.1111/j.1432-1033.1996.0424k.x. PMID 8647081.
  2. ↑ Heinfling, A.; Ruiz-Dueñas, F.J.; Martínez, M.J.; Bergbauer, M.; Szewzyk, U.; Martínez, A.T. (1998). "A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta". FEBS Lett. 428 (3): 141–146. doi:10.1016/s0014-5793(98)00512-2. PMID 9654123.
  3. ↑ Ruiz-Dueñas, F.J.; Martínez, M.J.; Ruiz-Dueñas, F.J.; Martínez, M.J.; Martínez, A.T. (1999). "Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii". Mol. Microbiol. 31 (1): 223–235. doi:10.1046/j.1365-2958.1999.01164.x. PMID 9987124.
  4. ↑ Camarero, S.; Sarkar, S.; Ruiz-Dueñas, F.J.; Martínez, M.J.; Ruiz-Dueñas, F.J.; Martínez, M.J.; Martínez, A.T. (1999). "Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites". J. Biol. Chem. 274 (15): 10324–10330. doi:10.1074/jbc.274.15.10324. PMID 10187820.
  5. ↑ Ruiz-Dueñas, F.J.; Martínez, M.J.; Martínez, A.T. (1999). "Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn2+ and different aromatic substrates". Appl. Environ. Microbiol. 65 (10): 4705–4707. PMC 91631Freely accessible. PMID 10508113.
  6. ↑ Camarero, S.; Ruiz-Dueñas, F.J.; Sarkar, S.; Martínez, M.J.; Martínez, A.T. (2000). "The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases". FEMS Microbiol. Lett. 191 (1): 37–43. doi:10.1016/s0378-1097(00)00367-0. PMID 11004397.
  7. ↑ Ruiz-Dueñas, F.J.; Camarero, S.; Pérez-Boada, M.; Martínez, M.J.; Martínez, A.T. (2001). "A new versatile peroxidase from Pleurotus". Biochem. Soc. Trans. 29 (Pt 2): 116–122. doi:10.1042/0300-5127:0290116. PMID 11356138.
  8. ↑ Banci, L.; Camarero, S.; Martínez, A.T.; Martínez, M.J.; Pérez-Boada, M.; Pierattelli, R.; Ruiz-Dueñas, F.J. (2003). "NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii". J. Biol. Inorg. Chem. 8 (7): 751–760. doi:10.1007/s00775-003-0476-1. PMID 12884090.
  9. ↑ Pérez-Boada, M.; Ruiz-Dueñas, F.J.; Pogni, R.; Basosi, R.; Choinowski, T.; Martínez, M.J.; Piontek, K.; Martínez, A.T. (2005). "Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways". J. Mol. Biol. 354 (2): 385–402. doi:10.1016/j.jmb.2005.09.047. PMID 16246366.
  10. ↑ Caramelo, L.; Martínez, M.J.; Martínez, A.T. (1999). "A search for ligninolytic peroxidases in the fungus Pleurotus eryngii involving α-keto-γ-thiomethylbutyric acid and lignin model dimer". Appl. Environ. Microbiol. 65 (3): 916–922. PMC 91123Freely accessible. PMID 10049842.
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