Dye decolorizing peroxidase

Dye-decolorizing peroxidase
Identifiers
EC number 1.11.1.19
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Dye-decolorizing peroxidase (EC 1.11.1.19, DyP, DyP-type peroxidase) is an enzyme with systematic name Reactive-Blue-5:hydrogen-peroxide oxidoreductase.[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction

Reactive Blue 5 + H2O2 phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate

These heme proteins are secreted by basidiomycetous fungi and eubacteria.

References

  1. ↑ Kim, S.J.; Shoda, M. (1999). "Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes". Appl. Environ. Microbiol. 65 (3): 1029–1035. PMC 91140. PMID 10049859.
  2. ↑ Sugano, Y.; Ishii, Y.; Shoda, M. (2004). "Role of H164 in a unique dye-decolorizing heme peroxidase DyP". Biochem. Biophys. Res. Commun. 322 (1): 126–132. doi:10.1016/j.bbrc.2004.07.090. PMID 15313183.
  3. ↑ Zubieta, C.; Joseph, R.; Krishna, S.S.; McMullan, D.; Kapoor, M.; Axelrod, H.L.; Miller, M.D.; Abdubek, P.; Acosta, C.; Astakhova, T.; Carlton, D.; Chiu, H.J.; Clayton, T.; Deller, M.C.; Duan, L.; Elias, Y.; Elsliger, M.A.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Kumar, A.; Marciano, D.; Morse, A.T.; Murphy, K.D.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Reyes, R.; Rife, C.L.; Schimmel, P.; Trout, C.V.; van den Bedem, H.; Weekes, D.; White, A.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A. (2007). "Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA". Proteins. 69: 234–243. doi:10.1002/prot.21673. PMID 17654547.
  4. ↑ Sugano, Y.; Matsushima, Y.; Tsuchiya, K.; Aoki, H.; Hirai, M.; Shoda, M. (2009). "Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1". Biodegradation. 20 (3): 433–440. doi:10.1007/s10532-008-9234-y. PMID 19009358.
  5. ↑ Sugano, Y. (2009). "DyP-type peroxidases comprise a novel heme peroxidase family". Cell. Mol. Life Sci. 66 (8): 1387–1403. doi:10.1007/s00018-008-8651-8. PMID 19099183.
  6. ↑ Ogola, H.J.; Kamiike, T.; Hashimoto, N.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y. (2009). "Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120". Appl. Environ. Microbiol. 75 (23): 7509–7518. doi:10.1128/AEM.01121-09. PMC 2786418. PMID 19801472.
  7. ↑ van Bloois, E.; Torres Pazmino, D.E.; Winter, R.T.; Fraaije, M.W. (2010). "A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily". Appl. Microbiol. Biotechnol. 86 (5): 1419–1430. doi:10.1007/s00253-009-2369-x. PMC 2854361. PMID 19967355.
  8. ↑ Liers, C.; Bobeth, C.; Pecyna, M.; Ullrich, R.; Hofrichter, M. (2010). "DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes". Appl. Microbiol. Biotechnol. 85 (6): 1869–1879. doi:10.1007/s00253-009-2173-7. PMID 19756587.
  9. ↑ Hofrichter, M.; Ullrich, R.; Pecyna, M.J.; Liers, C.; Lundell, T. (2010). "New and classic families of secreted fungal heme peroxidases". Appl. Microbiol. Biotechnol. 87 (3): 871–897. doi:10.1007/s00253-010-2633-0. PMID 20495915.


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