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
| Dye-decolorizing peroxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
- 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
edit- ^ Kim SJ, Shoda M (March 1999). "Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes". Applied and Environmental Microbiology. 65 (3): 1029–35. Bibcode:1999ApEnM..65.1029K. doi:10.1128/AEM.65.3.1029-1035.1999. PMC 91140. PMID 10049859.
- ^ Sugano Y, Ishii Y, Shoda M (September 2004). "Role of H164 in a unique dye-decolorizing heme peroxidase DyP". Biochemical and Biophysical Research Communications. 322 (1): 126–32. doi:10.1016/j.bbrc.2004.07.090. PMID 15313183.
- ^ 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 (November 2007). "Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA". Proteins. 69 (2): 234–43. doi:10.1002/prot.21673. PMID 17654547. S2CID 24489389.
- ^ Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M (June 2009). "Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1". Biodegradation. 20 (3): 433–40. doi:10.1007/s10532-008-9234-y. PMID 19009358. S2CID 24911119.
- ^ Sugano Y (April 2009). "DyP-type peroxidases comprise a novel heme peroxidase family". Cellular and Molecular Life Sciences. 66 (8): 1387–403. doi:10.1007/s00018-008-8651-8. PMC 11131544. PMID 19099183. S2CID 19739157.
- ^ Ogola HJ, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y (December 2009). "Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120". Applied and Environmental Microbiology. 75 (23): 7509–18. Bibcode:2009ApEnM..75.7509O. doi:10.1128/AEM.01121-09. PMC 2786418. PMID 19801472.
- ^ van Bloois E, Torres Pazmiño DE, Winter RT, Fraaije MW (May 2010). "A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily". Applied Microbiology and Biotechnology. 86 (5): 1419–30. doi:10.1007/s00253-009-2369-x. PMC 2854361. PMID 19967355.
- ^ Liers C, Bobeth C, Pecyna M, Ullrich R, Hofrichter M (February 2010). "DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes". Applied Microbiology and Biotechnology. 85 (6): 1869–79. doi:10.1007/s00253-009-2173-7. PMID 19756587.
- ^ Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T (July 2010). "New and classic families of secreted fungal heme peroxidases". Applied Microbiology and Biotechnology. 87 (3): 871–97. doi:10.1007/s00253-010-2633-0. PMID 20495915. S2CID 24417282.
External links
edit- Dye+decolorizing+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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