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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: Q8EIU4
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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
dye-decolorizing peroxidase
-
DyP
-
-
-
-
DyP-type peroxidase
-
-
-
-
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 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.084
Reactive Blue 5
in 25 mM citrate buffer, pH 3.2, at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.9
Reactive Blue 5
in 25 mM citrate buffer, pH 3.2, at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8EIU4_SHEON
Shewanella oneidensis (strain MR-1)
311
0
35760
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TyrA in complex with iron protoporphyrin (IX), hanging drop vapor diffusion method, using 0.1 M Tris pH 8.0, 5% (v/v) 2-propanol, 20% (w/v) polyethylene glycol 4000, and 1 mM hemin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zubieta, C.; Joseph, R.; Krishna, S.S.; McMullan, D.; Kapoor, M.; Axelrod, H.L.; Miller, M.D.; Abdubek, P.; Acosta, C.; Astakhova, T.; et al
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA
Proteins Struct. Funct. Bioinform.
69
234-243
2007
Shewanella oneidensis MR-1 (Q8EIU4)
Manually annotated by BRENDA team