EC 1.11.1.19 - Dye decolorizing peroxidase

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IntEnz Enzyme Nomenclature
EC 1.11.1.19

Names

Accepted name:
dye decolorizing peroxidase
Other names:
DyP
DyP-type peroxidase
Systematic name:
Reactive-Blue-5:hydrogen-peroxide oxidoreductase

Reaction

Comments:

Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Kim, S. J., Shoda, M.
    Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes.
    Appl. Environ. Microbiol. 65 : 1029-1035 (1999). [PMID: 10049859]
  2. Sugano, Y., Ishii, Y., Shoda, M.
    Role of H164 in a unique dye-decolorizing heme peroxidase DyP.
    Biochem. Biophys. Res. Commun. 322 : 126-132 (2004). [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.
    Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.
    Proteins 69 : 234-243 (2007). [PMID: 17654547]
  4. Sugano, Y., Matsushima, Y., Tsuchiya, K., Aoki, H., Hirai, M., Shoda, M.
    Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1.
    Biodegradation 20 : 433-440 (2009). [PMID: 19009358]
  5. Sugano, Y.
    DyP-type peroxidases comprise a novel heme peroxidase family.
    Cell. Mol. Life Sci. 66 : 1387-1403 (2009). [PMID: 19099183]
  6. Ogola, H. J., Kamiike, T., Hashimoto, N., Ashida, H., Ishikawa, T., Shibata, H., Sawa, Y.
    Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120.
    Appl. Environ. Microbiol. 75 : 7509-7518 (2009). [PMID: 19801472]
  7. van Bloois, E., Torres Pazmino, D. E., Winter, R. T., Fraaije, M. W.
    A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily.
    Appl. Microbiol. Biotechnol. 86 : 1419-1430 (2010). [PMID: 19967355]
  8. Liers, C., Bobeth, C., Pecyna, M., Ullrich, R., Hofrichter, M.
    DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes.
    Appl. Microbiol. Biotechnol. 85 : 1869-1879 (2010). [PMID: 19756587]
  9. Hofrichter, M., Ullrich, R., Pecyna, M. J., Liers, C., Lundell, T.
    New and classic families of secreted fungal heme peroxidases.
    Appl. Microbiol. Biotechnol. 87 : 871-897 (2010). [PMID: 20495915]

[EC 1.11.1.19 created 2010, modified 2015]