Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.11.1.19 - dye decolorizing peroxidase and Organism(s) Auricularia auricula-judae and UniProt Accession I2DBY1

for references in articles please use BRENDA:EC1.11.1.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Auricularia auricula-judae
UNIPROT: I2DBY1
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Auricularia auricula-judae
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-type peroxidase
-
dye-decolorizing peroxidase
-
-
DyP-type peroxidase
manganese-independent peroxidase I
-
-
manganese-independent peroxidase II
-
-
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
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
?
2,6-dimethoxyphenol + H2O2 + H+
?
show the reaction diagram
2,6-dimethoxyphenol + H2O2 + H+
oxidized 2,6-dimethoxyphenol + H2O
show the reaction diagram
-
-
-
?
4-bromophenol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-chlorophenol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-hydroxyacetophenone + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-hydroxybenzoic acid + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-hydroxybenzonitrile + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-methoxyphenol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
4-nitrophenol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
guaiacol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
guaiacylglycerol-beta-guaiacyl ether + H2O2 + H+
oxidized guaiacylglycerol-beta-guaiacyl ether + H2O
show the reaction diagram
-
-
-
?
phenol + H2O2 + H+
?
show the reaction diagram
-
-
-
?
Reactive Black 5 + H2O2 + H+
?
show the reaction diagram
-
-
-
?
Reactive Blue 19 + H2O2 + H+
?
show the reaction diagram
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
show the reaction diagram
-
-
-
?
Reactive Blue 5 + H2O2
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
show the reaction diagram
-
-
-
?
Reactive Blue 5 + H2O2 + H+
?
show the reaction diagram
-
-
-
?
veratryl alcohol + H2O2 + H+
?
show the reaction diagram
veratrylglycerol-beta-guaiacyl ether + H2O2 + H+
oxidized veratrylglycerol-beta-guaiacyl ether + H2O
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
show the reaction diagram
-
-
-
-
?
2,6-dimethoxyphenol + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
adlerol + H2O2
?
show the reaction diagram
-
-
-
-
?
adlerol + H2O2 + H+
?
show the reaction diagram
-
i.e 1-(3,4-dimethoxyphenyl)-1-oxo-2-(2-methoxyphenoxy)-1,3-dihydroxy-propane, maximum oxidation activity at pH 2.5
-
-
?
beta,beta-carotene + H2O2 + H+
beta-ionone + beta-apo-10'-carotenal + H2O
show the reaction diagram
-
-
-
-
?
norbixin + H2O2
?
show the reaction diagram
-
-
-
-
?
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
show the reaction diagram
-
-
-
-
?
Reactive Blue 5 + H2O2 + H+
? + phthalic acid + H2O
show the reaction diagram
-
-
-
-
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
show the reaction diagram
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme shows manganese-independent peroxidase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.121 - 2.75
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.703 - 1.32
2,6-dimethoxyphenol
0.137
H2O2
at pH 3.0 and 25°C
0.03
Reactive Black 5
wild type enzyme, at pH 3.0 and 30°C
0.09 - 0.12
Reactive Blue 19
0.0106 - 0.0156
Reactive Blue 5
7.36
veratryl alcohol
mutant enzyme W377S, at pH 2.5 and 25°C
0.448
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
-
0.02 - 0.1875
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.023 - 0.027
2,6-dimethoxyphenol
0.005 - 0.01
H2O2
0.005 - 0.007
Reactive Black 5
0.015 - 0.023
Reactive Blue 5
1.779 - 2.89
veratryl alcohol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
171 - 654
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
120 - 420
2,6-dimethoxyphenol
223
H2O2
at pH 3.0 and 25°C
10.6
Reactive Black 5
wild type enzyme, at pH 3.0 and 30°C
224 - 422
Reactive Blue 19
0.7 - 4.8
Reactive Blue 5
0.23
veratryl alcohol
mutant enzyme W377S, at pH 2.5 and 25°C
0.3
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
-
1.15 - 368
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
89 - 90
2,6-dimethoxyphenol
238 - 268
H2O2
3
Reactive Black 5
114 - 256
Reactive Blue 5
0.62 - 0.86
veratryl alcohol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
62 - 2300
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
173 - 320
2,6-dimethoxyphenol
1600
H2O2
at pH 3.0 and 25°C
400
Reactive Black 5
wild type enzyme, at pH 3.0 and 30°C
2400 - 3600
Reactive Blue 19
68 - 310
Reactive Blue 5
0.032 - 0.11
veratryl alcohol
0.7
veratrylglycerol-beta-guaiacyl ether
at pH 3.0 and 25°C
-
6.12
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
at pH 4.0 and 30°C
3300 - 3900
2,6-dimethoxyphenol
27000 - 48000
H2O2
410 - 570
Reactive Black 5
5000 - 17000
Reactive Blue 5
0.22 - 0.48
veratryl alcohol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28.4
-
culture liquid, at pH 3.0 and 20°C
347.8
-
manganese-independent peroxidase II after 12.2fold purification, at pH 3.0 and 20°C
469
-
manganese-independent peroxidase I after 16.5fold purification, at pH 3.0 and 20°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
isoelectric focusing
4.1
-
manganese-independent peroxidase II, isoelectric focusing
4.3
-
manganese-independent peroxidase I, isoelectric focusing
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?
DYP_AURAJ
509
0
52992
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
manganese-independent peroxidase II, SDS-PAGE
51000
-
manganese-independent peroxidase I, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52900, calculated from SDS-PAGE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 32.5% (w/v) PEG 4000 as precipitant
to 2.1 A resolution. At the distal side of the heme molecule, flexible aspartate residue Asp168 plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. A transient radical on the surface-exposed residue Tyr337 is the oxidation site for bulky substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G169L
the mutant shows strongly increased activity compared to the wild type enzyme
Y147F/Y337F
the mutant shows reduced activity compared to the wild type enzyme
Y147S
the mutant shows reduced activity compared to the wild type enzyme
Y337S
the mutant shows about wild type activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
the enzyme shows more than 80% activity after 24 h at pH 4.0-9.0
743731
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 65
the wild type enzyme remains stable after 24 h at 30-55°C and shows 50% activity after 24 h at 65.5°C
50
-
the enzyme shows a residual activity of ca. 80% after incubation at 50°C for 1 h. The enzyme shows almost no activity at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, manganese-independent peroxidase I in 50 mM sodium tartrate buffer pH 2.5, 24 h, 20% loss of activity
-
20°C, manganese-independent peroxidase II in 50 mM sodium tartrate buffer pH 2.5, 24 h, 75% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q Sepharose column chromatography, Mono Q column chromatography, and Mono P column chromatography
Ni-NTA bead chromatography
-
Q Sepharose column chromatography, Mono Q column chromatography, Mono S column chromatography, and Mono P column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLyS cells
expressed in Escherichia coli BL21(DE3)Star cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
with oxidized glutathione (1.5 mM), hemin (0.03 mM) and urea (0.8 M)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
DyP-type peroxidases are interesting for applications in the waste treatment sector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Auricularia auricula-judae
Manually annotated by BRENDA team
Hofrichter, M.; Ullrich, R.; Pecyna, M.J.; Liers, C.; Lundell, T.
New and classic families of secreted fungal heme peroxidases
Appl. Microbiol. Biotechnol.
87
871-897
2010
Anabaena sp., Auricularia auricula-judae, Bacillus subtilis, Bacteroides thetaiotaomicron, Escherichia coli, Mycetinis scorodonius, Shewanella oneidensis, Termitomyces albuminosus, Thanatephorus cucumeris, Thermobifida fusca
Manually annotated by BRENDA team
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
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
Manually annotated by BRENDA team
Behrens, C.J.; Zelena, K.; Berger, R.G.
Comparative cold shock expression and characterization of fungal dye-decolorizing peroxidases
Appl. Biochem. Biotechnol.
179
1404-1417
2016
Bjerkandera adusta, Pleurotus ostreatus, Auricularia auricula-judae, Mycetinis scorodonius, Pleurotus ostreatus 1020, Auricularia auricula-judae 11326
Manually annotated by BRENDA team
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
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
Manually annotated by BRENDA team
Liers, C.; Aranda, E.; Strittmatter, E.; Piontek, K.; Plattner, D.; Zorn, H.; Ullrich, R.; Hofrichter, M.
Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases
J. Mol. Catal. B
103
41-46
2014
Mycetinis scorodonius, Mycena epipterygia, Auricularia auricula-judae (I2DBY1), Exidia glandulosa (I2DBY2)
-
Manually annotated by BRENDA team
Baratto, M.C.; Sinicropi, A.; Linde, D.; Saez-Jimenez, V.; Sorace, L.; Ruiz-Duenas, F.J.; Martinez, A.T.; Basosi, R.; Pogni, R.
Redox-active sites in Auricularia auricula-judae dye-decolorizing peroxidase and several directed variants a multifrequency EPR study
J. Phys. Chem. B
119
13583-13592
2015
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
Manually annotated by BRENDA team
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
Auricularia auricula-judae (I2DBY1), Auricularia auricula-judae
Manually annotated by BRENDA team
Linde, D.; Ayuso-Fernandez, I.; Laloux, M.; Aguiar-Cervera, J.E.; de Lacey, A.L.; Ruiz-Duenas, F.J.; Martinez, A.T.
Comparing ligninolytic capabilities of bacterial and fungal dye-decolorizing peroxidases and class-II peroxidase-catalases
Int. J. Mol. Sci.
22
2629
2021
Amycolatopsis sp. ATCC 39116 (K7N5M8), Auricularia auricula-judae (I2DBY1), Thermomonospora curvata (D1A807), Thermomonospora curvata ATCC 19995 (D1A807)
Manually annotated by BRENDA team