The peroxidase database
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Classes

Dye-decolorizing peroxidase (Dyp-type peroxidase)

  Contact author: Marcel Zamocky

  Last update: 2017-03-15 (Marcel Zamocky)

DyP type peroxidase (A)
DyP-type peroxidase (B)
DyP-type peroxidase (C)
DyP-type peroxidase (D)
Profiles

Pfam : PF04261, Dyp-type peroxidase family.
InterPro : IPR006314, Dyp-type peroxidase and IPR006311, Twin-arginine translocation pathway signal

a part of a larger superfamily: peroxidase-chlorite dismutase (ABB 2015 574:108-119
Description Dyp-type peroxidase sequences can be detected in fungi, mycetozoa, bacteria and archaea. A distinct branch of this family has a typical twin-arginine dependent signal sequence (TAT domain) characteristic of exported proteins with bound redox cofactors.
DyP from fungus show no homology to other fungal peroxidases such as LiP and MnP, and lacks the typical heme-binding region conserved among plant peroxidase superfamily (Sugano et al. 1999). DyP differs from MnP because of its ability to oxidize phenolic compounds, such as 2,6-dimethoxyphenol and guaiacol, in the absence of Mn2+. Moreover, DyP does not degrade non-phenolic compounds, thus differing from LiP. Another singular characteristic of DyP is its ability to degrade several synthetic dyes (Kim and Shoda 1999), mainly anthraquinone dyes, which are not oxidized by most of the other peroxidases. As a fact LiP, versatile peroxidase (Ruiz-Duenas et al. 2001) and manganese-independent peroxidase (Ruiz-Duenas et al. 1999) have been reported to mainly degrade azo dyes.
Bacterial DyP sequences are not detected neither in Archeaebacteria nor in Chlamydiae/Verrucomicrobia nor in Cyanobacteria; they are poorly represented in Bacteroidetes/Chlorobi. Together with chlorite dismutases and EfeB known also as Heme Q they constitute a large CDE superfamily (Goblirsch et al. 2011) known also as the peroxidase-chlorite dismutase superfamily.
Literature Faraco V, Piscitelli A, Sannia G and Giardina P Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus. 23, 6:2007 889-893
Goblirsch B, Kurker RC, Streit BR, Wilmot CM, DuBois JL J. Mol. Biol. 408 (2011) 379-398.
Sugano Y, Ishii Y, Shoda M. Role of H164 in a unique dye-decolorizing heme peroxidase DyP. Biochem Biophys Res Commun. 2004 Sep 10;322(1):126-32. PMID: 15313183

Sato T, Hara S, Matsui T, Sazaki G, Saijo S, Ganbe T, Tanaka N, Sugano Y, Shoda M. A unique dye-decolorizing peroxidase, DyP, from Thanatephorus cucumeris Dec 1: heterologous expression, crystallization and preliminary X-ray analysis. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):149-52. Epub 2003 Dec 18. PMID: 14684913

Vyas BR, Molitoris HP. Involvement of an extracellular H2O2-dependent ligninolytic activity of the white rot fungus Pleurotus ostreatus in the decolorization of Remazol brilliant blue R. Appl Environ Microbiol. 1995 Nov;61(11):3919-27. PMID: 8526504
Zámocký M, Hofbauer S, Schaffner I, Gasselhuber B, Nicolussi A, Soudi M, Pirker KF, Furtmüller PG, Obinger C. Independent evolution of four heme peroxidase superfamilies. ABB 574:108-119 (2015).
Zubieta C, et al., Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Proteins. 2007 Nov 1;69(2):234-43. PMID: 17654547

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