MetaCyc EC 1.11.1.19 -- dye decolorizing peroxidase

Parent Class: EC-Numbers1 -- Oxidoreductases1.11 -- Acting on a peroxide as acceptor1.11.1 -- Peroxidases

Synonyms: DyP, DyP-type peroxidase

Systematic Name: Reactive-Blue-5:hydrogen-peroxide oxidoreductase

Unification Links: BRENDA:1.11.1.19, ENZYME:1.11.1.19, IUBMB-ExplorEnz:1.11.1.19

Reaction:
Reactive blue 5 + 2 hydrogen peroxide → phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O + 2 H+

Unofficial Reactions:
2 Fe2+ + hydrogen peroxide + 2 H+ → 2 Fe3+ + 2 H2O,
2 guaiacol + hydrogen peroxide → 2 guaiacol radical + 2 H2O

Enzymes and Genes:
porphyrinogen peroxidase: yfeX ( Escherichia coli K-12 substr. MG1655 )
dye-decolorizing peroxidase: DyP ( Thermobifida fusca YX )

Summary:
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 phthalate. Bacterial TfuDyP catalyses sulfoxidation.

Citations: [Kim99, Sugano04, Zubieta07, Sugano09, Sugano09a, Ogola09, vanBloois10, Liers10, Hofrichter10]


References

Hofrichter10: Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T (2010). "New and classic families of secreted fungal heme peroxidases." Appl Microbiol Biotechnol 87(3);871-97. PMID: 20495915

Kim99: Kim SJ, 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);1029-35. PMID: 10049859

Liers10: 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);1869-79. PMID: 19756587

Ogola09: Ogola HJ, 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);7509-18. PMID: 19801472

Sugano04: Sugano Y, Ishii Y, Shoda M (2004). "Role of H164 in a unique dye-decolorizing heme peroxidase DyP." Biochem Biophys Res Commun 322(1);126-32. PMID: 15313183

Sugano09: 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);433-40. PMID: 19009358

Sugano09a: Sugano Y (2009). "DyP-type peroxidases comprise a novel heme peroxidase family." Cell Mol Life Sci 66(8);1387-403. PMID: 19099183

vanBloois10: van Bloois E, Torres Pazmino DE, Winter RT, Fraaije MW (2010). "A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily." Appl Microbiol Biotechnol 86(5);1419-30. PMID: 19967355

Zubieta07: Zubieta C, Joseph R, Krishna SS, McMullan D, Kapoor M, Axelrod HL, Miller MD, Abdubek P, Acosta C, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Murphy KD, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, Trout CV, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA (2007). "Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA." Proteins 69(2);234-43. PMID: 17654547


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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