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Information on EC 1.11.1.19 - dye decolorizing peroxidase

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.19 dye decolorizing peroxidase
IUBMB Comments
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 phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
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UNIPROT: Q8WZK8
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dye-decolorizing peroxidase, dyp-type peroxidase, dyp1b, tt1485, dye decolorizing peroxidase, lip ba45, mnp ba30, lip-sn, ancdypd-b1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DyP-type peroxidase
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DyP
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-
-
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DyP-type peroxidase
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
Reactive-Blue-5:hydrogen-peroxide oxidoreductase
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 phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Reactive Blue 19 + H2O2 + H+
?
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
Reactive Blue 19
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
980
Reactive Blue 19
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly called Thanatephorus cucumeris Dec 1 and Geotrichum candidum Dec 1
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8WZK8_9APHY
498
0
53307
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of native enzyme, the D171N mutant, the native enzyme complexed with cyanide, and the D171N mutant associated with cyanide, to 1.4 A, 1.42 A, 1.45 and 1.4 A resolution, respectively. Structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. The structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus oryzae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, T.; Tsuge, H.; Konno, H.; Hisabori, T.; Sugano, Y.
The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
FEBS J.
278
2387-2394
2011
Bjerkandera adusta (Q8WZK8)
Manually annotated by BRENDA team
Yoshida, T.; Sugano, Y.
A structural and functional perspective of DyP-type peroxidase family
Arch. Biochem. Biophys.
574
49-55
2015
Bjerkandera adusta (Q8WZK8), Bjerkandera adusta Dec 1 (Q8WZK8), Bjerkandera adusta Dec 1
Manually annotated by BRENDA team
Colpa, D.; Fraaije, M.; Van Bloois, E.
DyP-type peroxidases A promising and versatile class of enzymes
J. Ind. Microbiol. Biotechnol.
41
1-7
2014
Bjerkandera adusta (Q8WZK8), Bjerkandera adusta Dec1 (Q8WZK8)
Manually annotated by BRENDA team