ID: | 1.11.1.19 |
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Description: | Dye decolorizing peroxidase. |
Alternative Name: |
DyP-type peroxidase. DyP. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.11.1.19 |
BRENDA Enzyme Link: | BRENDA 1.11.1.19 |
KEGG Enzyme Link: | KEGG1.11.1.19 |
BioCyc Enzyme Link: | BioCyc 1.11.1.19 |
ExPASy Enzyme Link: | ExPASy1.11.1.19 |
EC2PDB Enzyme Link: | EC2PDB 1.11.1.19 |
ExplorEnz Enzyme Link: | ExplorEnz 1.11.1.19 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.11.1.19 |
IntEnz Enzyme Link: | IntEnz 1.11.1.19 |
MEDLINE Enzyme Link: | MEDLINE 1.11.1.19 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:28086 | 2 H2O2 + Reactive Blue 5 = 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H(+) + 2 H2O + phthalate |
RULE(radius=1) | [*:1]-[NH;+0:2]-[c;H0;+0:3](:[*:4]):[*:5]:[c;H0;+0:6](:[*:7])-[NH;+0:8]-[c;H0;+0:9](:[*:10]):[c;H0;+0:11]1:[c;H0;+0:12](:[*:13]-[NH2;+0:14])-[CH;+0:15](-[OH;+0:16])-[*:17]:[*:18]-[CH;+0:19]-1-[OH;+0:20].[OH;+0:21]-[OH;+0:22].[OH;+0:23]-[OH;+0:24]>>[*:1]-[NH2;+0:2].[*:7]:[cH;+0:6]:[*:5]:[c;H0;+0:3](:[*:4])-[N;H0;+0:8]=[N;H0;+0:14]-[*:13]:[cH;+0:12]:[cH;+0:11]:[cH;+0:9]:[*:10].[O;H0;+0:20]=[C;H0;+0:19](-[OH;+0:23])-[*:18]:[*:17]-[C;H0;+0:15](=[O;H0;+0:16])-[OH;+0:24].[OH2;+0:21].[OH2;+0:22] |
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Title | Authors | Date | PubMed ID |
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New and classic families of secreted fungal heme peroxidases. | Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T | 2010 Jul | 20495915 |
Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. | Ogola HJ, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y | 2009 Dec | 19801472 |
DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. | Liers C, Bobeth C, Pecyna M, Ullrich R, Hofrichter M | 2010 Feb | 19756587 |
Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1. | Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M | 2009 Jun | 19009358 |
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. | 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 Nov 1 | 17654547 |
Identification and characterization of a multifunctional dye peroxidase from a lignin-reactive bacterium. | Brown ME, Barros T, Chang MC | 2012 Dec 21 | 23054399 |