Sequence of DYP_AURAJ
EC Number:1.11.1.7
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O
Other sequences found for EC No. 1.11.1.7
General information:
Sequence
0 MRLSPVFVAL LSGLLAADLG LARSVAPRVA DSPAAVTGTR KTSLLKNVAG LPPVPSAAQV
60 AATSLNTDDI QGDILVGMHK QKQLFYFFAI NDPATFKTHL ASDIAPVVAS VTQLSNVATQ
120 PLVALNIAFS NTGLLALGVT DNLGDSLFAN GQAKDATSFK ESTSSWVPQF AGTGIHGVII
180 LASDTTDLID QQVASIESTF GSSISKLYSL SASIRPGNEA GHEMFGFLDG IAQPAINGFN
240 TPLPGQNIVD AGVIITGATN DPITRPSWAV GGSFLAFRQL EQLVPEFNKY LLDNAPAGSG
300 SLQARADLLG ARMVGRWKSG APIDLTPTAD DPALGADAQR NNNFTYSHAG FDLGSDQSHC
360 PFSAHIRKTR PRADLGGSLT PPNLSAGANS IMRSGIPYGP EVTSAESASN TTTQERGLAF
420 VAYQAQLSQG FHFLQQTWAD NANFPPGKTP ATVGLDPIIG QNNGQPRVVN GLLPSNSSAS
480 LSIPQFVVSH GGEYFFSPPI SAIGGRLSA
Download this sequence
in fasta formatDownload all sequences for 1.11.1.7
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1180829
Liers C.,Pecyna M.J.,Kellner H.,Worrich A.,Zorn H.,Steffen K.T.,Hofrichter M.,Ullrich R.
Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.
Appl. Microbiol. Biotechnol.
97
5839-5849
2013
1180830
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
1180831
Linde D.,Coscolin C.,Liers C.,Hofrichter M.,Martinez A.T.,Ruiz-Duenas F.J.
Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae.
Protein Expr. Purif.
103
28-37
2014
1180832
Strittmatter E.,Liers C.,Ullrich R.,Wachter S.,Hofrichter M.,Plattner D.A.,Piontek K.
First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: substrate interaction sites and long-range electron transfer.
J. Biol. Chem.
288
4095-4102
2013
1180833
Strittmatter E.,Serrer K.,Liers C.,Ullrich R.,Hofrichter M.,Piontek K.,Schleicher E.,Plattner D.A.
The toolbox of Auricularia auricula-judae dye-decolorizing peroxidase - Identification of three new potential substrate-interaction sites.
Arch. Biochem. Biophys.
574
75-85
2015
1180834
Linde D.,Pogni R.,Canellas M.,Lucas F.,Guallar V.,Baratto M.C.,Sinicropi A.,Saez-Jimenez V.,Coscolin C.,Romero A.,Medrano F.J.,Ruiz-Duenas F.J.,Martinez A.T.
Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.
Biochem. J.
466
253-262
2015
