Information on EC 1.11.1.19 - dye decolorizing peroxidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.11.1.19
-
RECOMMENDED NAME
GeneOntology No.
dye decolorizing peroxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Reactive Blue 5 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O
show the reaction diagram
-
-
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
strain Dec 1
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-diamino-2-sodium anthraquinone sulfonate + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
1-amino-2-sulfonyl-4-aminomethyl-9,10-anthraquinone + H2O2 + H+
?
show the reaction diagram
1-amino-4-(3-amino-4-sodium-sulfonoanilino)-2-sodium anthraquinone sulfonate + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
1-amino-4-methylamino-2-sodium anthraquinone sulfonate + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 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
? + H2O
show the reaction diagram
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
show the reaction diagram
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
show the reaction diagram
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + H+
?
show the reaction diagram
89% activity compared to guaiacol
-
-
?
2,6-dimethoxyphenol + H2O2
?
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
3,3'-diaminobenzidine + H2O2 + H+
?
show the reaction diagram
weak activity
-
-
?
4-aminoantipyrine + H2O2 + H+
?
show the reaction diagram
643% activity compared to guaiacol
-
-
?
Acid Blue 45 + H2O2 + H+
oxidized Acid Blue 45 + H2O
show the reaction diagram
98% decolorization rate compared to Reactive Blue 5
-
-
?
Acid Blue 62 + H2O2 + H+
oxidized Acid Blue 62 + H2O
show the reaction diagram
-
-
-
-
?
Acid Orange 7 + H2O2 + H+
oxidized Acid Orange 7 + H2O
show the reaction diagram
-
100% decolorization rate after 10 days compared to Reactive Blue 114
-
-
?
Acid Red 151 + H2O2 + H+
oxidized Acid Red 151 + H2O
show the reaction diagram
12% decolorization rate compared to Reactive Blue 5
-
-
?
Acid Red 27 + H2O2 + H+
oxidized Acid Red 27 + H2O
show the reaction diagram
-
97.9% decolorization rate after 10 days compared to Reactive Blue 114
-
-
?
Acid Red 73 + H2O2 + H+
oxidized Acid Red 73 + H2O
show the reaction diagram
-
100% decolorization rate after 10 days compared to Reactive Blue 114
-
-
?
adlerol + H2O2
?
show the reaction diagram
adlerol + H2O2 + H+
?
show the reaction diagram
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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
Congo Red + H2O2 + H+
oxidized Congo Red + H2O
show the reaction diagram
12% decolorization rate compared to Reactive Blue 5
-
-
?
D-isoascorbate + H2O2 + H+
?
show the reaction diagram
134% activity compared to guaiacol
-
-
?
Direct Sky Blue 6B + H2O2 + H+
oxidized Direct Sky Blue 6B + H2O
show the reaction diagram
50% decolorization rate compared to Reactive Blue 5
-
-
?
guaiacol + H2O2 + H+
?
show the reaction diagram
guaiacol + H2O2 + H+
oxidized guaiacol + H2O
show the reaction diagram
L-ascorbate + H2O2 + H+
?
show the reaction diagram
126% activity compared to guaiacol
-
-
?
Mordant Black 9 + H2O2 + H+
oxidized Mordant Black 9 + H2O
show the reaction diagram
-
-
-
-
?
o-phenylenediamine + H2O2 + H+
?
show the reaction diagram
0.7%activity compared to Reactive Blue 19
-
-
?
Procion Blue H-ERD + H2O2 + H+
oxidized Procion Blue H-ERD + H2O
show the reaction diagram
90% decolorization rate compared to Reactive Blue 5
-
-
?
Procion Blue H-EXL + H2O2 + H+
oxidized Procion Blue H-EXL + H2O
show the reaction diagram
72% decolorization rate compared to Reactive Blue 5
-
-
?
pyrogallol + H2O2 + H+
?
show the reaction diagram
93% activity compared to guaiacol
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
show the reaction diagram
Reactive Black 5 + H2O2 + H+
oxidized Reactive Black 5 + H2O
show the reaction diagram
Reactive Blue 114 + H2O2 + H+
oxidized Reactive Blue 114 + H2O
show the reaction diagram
Reactive Blue 182 + H2O2 + H+
oxidized Reactive Blue 182 + H2O
show the reaction diagram
Reactive Blue 19 + H2O2
oxidized Reactive Blue 5 + H2O
show the reaction diagram
Reactive Blue 19 + H2O2 + H+
oxidized Reactive Blue 19 + H2O
show the reaction diagram
Reactive Blue 21 + H2O2 + H+
oxidized Reactive Blue 21 + H2O
show the reaction diagram
Reactive Blue 4 + H2O2 + H+
oxidized Reactive Blue 4 + 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
show the reaction diagram
Reactive Blue 5 + H2O2 + H+
4-amino-2-((4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl)amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
show the reaction diagram
Reactive Blue 5 + H2O2 + H+
4-amino-2-([4-chloro-6-[(3-sulfophenyl)amino]-1,3,5-triazin-2-yl]amino)benzenesulfonic acid + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid + 4-amino-2-[(4-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonic acid
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
Reactive Green 19 + H2O2 + H+
oxidized Reactive Green 19 + H2O
show the reaction diagram
35% decolorization rate compared to Reactive Blue 5
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-
?
Reactive Orange 13 + H2O2 + H+
oxidized Reactive Orange 13 + H2O
show the reaction diagram
Reactive Orange 14 + H2O2 + H+
oxidized Reactive Orange 14 + H2O
show the reaction diagram
10% decolorization rate compared to Reactive Blue 5
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-
?
Reactive Red 120 + H2O2 + H+
oxidized Reactive Red 120 + H2O
show the reaction diagram
Reactive Red 120 + H2O2 + H+
oxidized Reactive Violet 23 + H2O
show the reaction diagram
-
slight decolorization
-
-
?
Reactive Red 123 + H2O2 + H+
oxidized Reactive Red 123 + H2O
show the reaction diagram
Reactive Red 187 + H2O2 + H+
oxidized Reactive Red 187 + H2O
show the reaction diagram
-
100% decolorization rate after 10 days compared to Reactive Blue 114
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-
?
Reactive Red 202 + H2O2 + H+
oxidized Reactive Red 202 + H2O
show the reaction diagram
-
98.8% decolorization rate after 10 days compared to Reactive Blue 114
-
-
?
Reactive Red 225 + H2O2 + H+
oxidized Reactive Red 225 + H2O
show the reaction diagram
Reactive Red 33 + H2O2 + H+
oxidized Reactive Red 33 + H2O
show the reaction diagram
Reactive Violet 23 + H2O2 + H+
oxidized Reactive Violet 23 + H2O
show the reaction diagram
-
weak decolorization
-
-
?
Reactive Yellow 2 + H2O2 + H+
oxidized Reactive Yellow 2 + H2O
show the reaction diagram
Reactive Yellow 86 + H2O2 + H+
oxidized Reactive Yellow 86 + H2O
show the reaction diagram
3% decolorization rate compared to Reactive Blue 5
-
-
?
Remazol Brilliant Blue R + H2O2
oxidized Remazol Brilliant Blue R + H2O
show the reaction diagram
-
-
-
-
?
Remazol Brilliant Blue R + H2O2 + H+
oxidized Remazol Brilliant Blue R + H2O
show the reaction diagram
-
-
-
-
?
syringaldehyde + H2O2 + H+
oxidized syringaldehyde + H2O
show the reaction diagram
23% activity compared to guaiacol
-
-
?
Vat Blue 6 + H2O2
oxidized Vat Blue 6 + H2O
show the reaction diagram
veratryl alcohol + H2O2
veratraldehyde + H2O
show the reaction diagram
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
show the reaction diagram
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
10 mM, 117% of initial activity
Co2+
10 mM, 115% of initial activity
Iron
-
DyP contains one heme with an iron at the center of the molecule
Zn2+
10 mM, 122% of initial activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyl dicarbonate
less than 50% inhibition at 50 mM
Fe2+
AnaPX is highly sensitive to Fe2+ (98.8% inhibition at 5 mM)
Fe3+
10 mM, 33% residual activity
KCN
AnaPX shows very low sensitivity to KCN which causes only 9% and 14% inhibition of the activity at 1 and 10 mM, respectively
Mn2+
57.1% inhibition at 5 mM
NaN3
AnaPX is highly sensitive to NaN3 (82% inhibition at 10 mM)
phenylhydrazine
AnaPX is highly sensitive to the suicide substrate phenylhydrazine (complete inhibition at 1 mM)
additional information
the enzyme is not sensitive to the prototypical catalase inhibitor 3-amino-1,2,4,-triazole in the presence of ascorbic acid (1.0 mM), metal chelating and sulfhydryl reagents do not significantly affect activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
syringaldehyde
the presence of syringaldehyde drastically enhances the rate of decolorization of Reactive Black 5, Reactive Orange 14, Reactive Red 120, Reactive Green 19, and Acid Red with 50fold, 9fold, 15fold, 2fold, and 7fold improvements, respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.084
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
-
at pH 3.2 and 30°C
0.02 - 0.166
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.023 - 0.0726
2,6-dimethoxyphenol
0.444
Acid Blue 62
-
pH 4, 25°C
0.499
guaiacol
-
pH 4, 25°C
0.005 - 0.0795
H2O2
0.385
Mordant black 9
-
pH 4, 25°C
0.005 - 0.0112
Reactive Black 5
0.0135 - 0.029
Reactive Blue 19
0.0036 - 0.157
Reactive Blue 5
1.779 - 3.61
veratryl alcohol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
270
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
Geotrichum candidum
-
at pH 3.2 and 30°C
224 - 368
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
70.9 - 90
2,6-dimethoxyphenol
9 - 419
H2O2
3 - 11.9
Reactive Black 5
10 - 79.9
Reactive Blue 19
0.0235 - 384
Reactive Blue 5
0.62 - 2.7
veratryl alcohol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3200
1-amino-4-methylamino-2-sodium anthraquinone sulfonate
Geotrichum candidum
-
at pH 3.2 and 30°C
41297
970 - 3900
2,6-dimethoxyphenol
306
20
Acid Blue 62
Bacillus subtilis
-
pH 4, 25°C
42603
0.3
guaiacol
Bacillus subtilis
-
pH 4, 25°C
359
333 - 66000
H2O2
22
10
Mordant black 9
Bacillus subtilis
-
pH 4, 25°C
23397
410 - 1100
Reactive Black 5
1338
345 - 5900
Reactive Blue 19
15122
0.219 - 120000
Reactive Blue 5
3424
0.22 - 0.83
veratryl alcohol
471
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.058
-
recombinant enzyme from crude extract, at 30°C, pH 3.2
0.2
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mutant enzyme D171N, at 30°C, pH not specified in the publication
0.28
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crude enzyme, in 25 mM citrate buffer (pH 3.2), at 30°C
1.8
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DyP, using Reactive Black 5 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
4.2
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DyP, using Reactive Red 33 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
5.6
recombinant enzyme from crude extract, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
7.5
-
DyP, using Reactive Blue 114 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
17.1
-
unpurified supernatant, at pH 3.5 and 30°C
22.4
-
culture supernatant, at 30°C, pH not specified in the publication
28.4
-
culture liquid, at pH 3.0 and 20°C
34
-
DyP, using guaiacol as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
37.8
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substrate 2,2'-azino-bis(3-ethylthiazoline)-6-sulfonate, pH 5.0, temperature not specified in the publication
54
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using syringaldehyde as substrate
57
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after 210fold purification, in 25 mM citrate buffer (pH 3.2), at 30°C
71
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,6-dimethoxyphenol as substrate
204
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid as substrate
216
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using pyrogallol as substrate
230
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using guaiacol as substrate
261
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15.3fold purified isozyme Dyp2, at pH 3.5 and 30°C
270
-
DyP, using Reactive Blue 19 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
283
recombinant enzyme after 50.5fold purification, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
290
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using L-ascorbate as substrate
308
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using D-isoascorbate as substrate; recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADPH as substrate
331
-
after 14.8fold purification, at 30°C, pH not specified in the publication
340
-
DyP, using Reactive Blue 5 as substrate, in 0.1 M sodium tartrate buffer (pH 3.0), at 30°C
347.8
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manganese-independent peroxidase II after 12.2fold purification, at pH 3.0 and 20°C
374
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADH as substrate
469
-
manganese-independent peroxidase I after 16.5fold purification, at pH 3.0 and 20°C
600
-
wild type enzyme, at 30°C, pH not specified in the publication
732
-
42.8fold purified isozyme Dyp3, at pH 3.5 and 30°C
834
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recombinant enzyme after 14385fold purification, at 30°C, pH 3.2
1478
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 4-aminoantipyrine as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.2
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recombinant enzyme
3
-
using 1-amino-4-methylamino-2-sodium anthraquinone sulfonate as substrate
3.6
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isozyme Dyp3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
for Reactive Blue 19-decolorizing activity in 25 mM citrate buffer pH 3.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
isoelectric focusing
4.1
-
manganese-independent peroxidase II, isoelectric focusing
4.2
-
isoelectric focusing
4.3
-
manganese-independent peroxidase I, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermobifida fusca (strain YX)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
2 * 32000, SDS-PAGE
36000
3 * 36000, SDs-PAGE
40000
-
manganese-independent peroxidase II, SDS-PAGE
45000
gel filtration
46000
1 * 46000, molecular mass of the unprocessed precursor calculated from amino acid sequence
47460
-
recombinant enzyme expressed in Escherichia coli, deduced from amino acid sequence
50000
-
recombinant enzyme expressed in Escherichia coli, gel filtration
51000
-
manganese-independent peroxidase I, SDS-PAGE
53280
4 * 53280, native enzyme, MALDI-TOF spectrometry
53368
4 * 53368, deduced from amino acid sequence
54000
4 * 54000, native enzyme, SDS-PAGE
55000
-
1 * 55000, gel filtration
57260
-
calculated from amino acid sequence
64000
gel filtration
209000
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 000, SDS-PAGE
homotetramer
4 * 53280, native enzyme, MALDI-TOF spectrometry; 4 * 53368, deduced from amino acid sequence; 4 * 54000, native enzyme, SDS-PAGE
monomer
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the six-coordinated low-spin state being the most populated. The poor catalytic activity of BsDyP is ascribed to the presence of a catalytically incompetent six-coordinated low-spin population. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -40 mV at pH 7.6, which is substantially more positive than those reported for the majority of other peroxidases
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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
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
batch method, using 0.89 M ammonium sulfate, 0.92 M sodium chloride, at 10°C
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deglycosylated DyP is crystallized by the batch method, using 0.92 M NaCl and 0.89 M ammonium sulfate as precipitant
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deglycosylated DyP is crystallized by the sitting drop vapor diffusion method, using 25.3% (w/v) PEG 8000 at 5.5 K (pH 6.2)
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 5
-
isozymes DyP1, DyP2 and DyP3 are completely inactivated at pH 2.5. Isozymes DyP1, DyP2 and DyP3 exhibit approximately 20% activity at pH 3.0. Isozymes DyP1 and Dyp2 show almost 100% activity at pH 3.5, isozyme DyP3 shows about 95% activity at pH 3.5. Isozyme DyP1 shows less than 50% activity at pH 4.0, isozymes DyP2 and Dyp3 show about 50% activity at pH 4.0. Isozymes Dyp1, DyP2 and Dyp3 show about 30% activity at pH 4.5 and about 20% activity at pH 5.0
712519
3.5 - 9.5
when maintained at 40°C for 20 min, the enzyme is stable at pH values between 3.5 and 9.5. The enzyme shows 20% relative activity at pH 3.0 and 10.0, 40% relative activity at pH 4.0, about 65% relative activity at pH 4.5 and 9.0, about 80% relative activity at pH 5.0, more than 90% relative activity at pH 6.0-8.0
695785
4
rapid loss of activity below
723971
6.5 - 7
30 min, stable
723971
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
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the activity of isozyme DyP3 is less than that of isozymes DyP2 and DyP1 at 35°C and 40°C. Isozymes DyP1, DyP2 and DyP3 exhibit approximately 75% activity at 20°C and about 90% activity at 30°C. Isozyme DyP1 shows about 75% activity at 40°C, isozyme DyP2 shows about 85% activity at 40°C, and isozyme DyP3 shows about 50% activity at 40°C. Isozymes DyP1, DyP2 and DyP3 show about 10% activity at 50°C and are completely inactivated at 60°C
30 - 60
30 - 70
30 - 60
after incubation for 2 h at 60°C the enzyme loses 50% of its original activity, while at 30°C and 40°C DyP retains its activity after this period. Upon incubation at 60°C, an almost 2fold increase in activity is observed within 10 min
60
4 h, 83% residual activity
70
1 h, more than 70% residual activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant DyP is partially inactivated during successive batches even by continuous fed-batch supply of H2O2, initial recombinant DyP activity is inactivated by 15% over the first 10 min during dye decolorization and remains stable thereafter at 85% of the initial activity from 10 to 40 min
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the activity of recombinant DyP immobilized in synthesized silica-based mesocellular foam drops by 6% and 12% at pH 3.0 andpH 4.0, respectively, while the activity decreases by 35% and 70% at pH 5.0 and pH 6.0 after daily leaching treatment
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized recombinant DyP has higher stability to H2O2 compared to free recombinant DyP. The stability of recombinant DyP immobilized on FSM-16 at pH 4.0 and on AlSBA-15 at pH 3.0 and 4 are similar to that of free recombinant DyP
-
712777
the enzyme retains more than 50% of its activity at 2.5 mM H2O2
695785
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
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20°C, manganese-independent peroxidase II in 50 mM sodium tartrate buffer pH 2.5, 24 h, 75% loss of activity
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4°C, 50 mM potassium phosphate buffer (pH 7.0), 40 days, 10% loss of activity
deglycosylated DyP exhibits enzymatic activity and is stable for more than 26 d either in MES buffer at pH 6.0 or in 45% (v/v) methanol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
-
ammonium sulfate precipitation and butyl-Toyopearl column chromatography
-
ammonium sulfate precipitation, QAE-Toyopearl column chromatography, Mono Q column chromatography, Poros PE column chromatography, and Superdex 75 gel filtration
-
butyl-Toyopearl column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
Ni2+-NTA agarose column chromatography
Q Sepharose column chromatography, Mono Q column chromatography, Mono S column chromatography, and Mono P column chromatography
-
quaternary aminoethyl-Toyopearl column chromatography and Mono-Q column chromatography
-
recombinant protein
Super Q 650M column chromatography and butyl Toyopearl column chromatography
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Toyopearl DEAE-650M column chromatography, Toyopearl butyl-650M column chromatography, and hydroxylapatite column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus oryzae
-
expressed in Aspergillus oryzae and in Escherichia coli
-
expressed in Aspergillus oryzae strain M-2-3, no exogenous heme is necessary for the expression of DyP
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expressed in Aspergillus oryzae strain RD005
-
expressed in Escherichia coli and in Aspergillus oryzae
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells and in Aspergillus oryzae strain RD005
-
expressed in Escherichia coli strain MC1061
expression in Aspergillus oryzae
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
biofilm formation is not essential for DyP activity
-
complete inhibition of DyP activity by molasses molasses (containing approximately 33% sucrose (w/w), 6.5% glucose (w/w), 7.5% fructose (w/w) and 0.57 g/kg nitrogen) is observed at the concentration of 20 g /l
-
dye decolorizing peroxidase activity is 233fold higher in air-membrane surface bioreactor culture than in submerged culture
-
high-level recombinant DyP activity in limitation of carbon and nitrogen sources is maintained stably for 26 cycles of repeated 1-day batches of Aspergillus oryzae pellets without any additional pH control
-
molasses (containing approximately 33% sucrose (w/w), 6.5% glucose (w/w), 7.5% fructose (w/w) and 0.57 g/kg nitrogen) at concentrations greater than 10 g/l increase the decolorization activity of the culture broth toward Reactive Blue 5 mainly because the amount of enzyme produced is enhanced. When the culture broth is diluted 25times, the dye-decolorizing activity is 7times as much as that of non-diluted culture broth
-
similar average recombinant DyP productivities are observed in repeated-batch cultures using wheat bran powder and rice bran powder. Average recombinant DyP productivities in fed-batch cultures are slightly lower than those in repeated-batch cultures. The recombinant DyP production is affected by the addition of K2HPO4 in the repeated-batch and fed-batch cultures using wheat bran powder. Increase in phosphate does not enhance recombinant DyP production, rather rDyP activity decreases by the repeated-batch culture
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M401F
-
heme cavity mutant with significantly increased H2O2 stability of 8.2fold, the mutant retains 16% activity at 100 mM H2O2
M401I
-
heme cavity mutant with significantly increased H2O2 stability of 3.7fold
M401L
-
heme cavity mutant with significantly increased H2O2 stability of 2.4fold
M451I
-
heme cavity mutant with significantly increased H2O2 stability of 5.2fold, the mutant retains 5% activity at 100 mM H2O2
H164A
-
DyP activity and heme binding are lost in the H164A mutant
D171N
-
the mutant displays 3000fold less enzymatic activity compared to the wild type DyP
H164A
-
the specific activity of the purified mutant is 99.8% lower than that of recombinant DyP expressed in Escherichia coli
H166A
-
the specific activity of the purified mutant is 95% lower than that of recombinant DyP expressed in Escherichia coli
D242A
the mutant shows 0.7% of the Reactive Blue 19-decolorizing activity of the wild type protein
H338A
the mutant lacks the heme cofactor and shows 3% of the Reactive Blue 19-decolorizing activity of the wild type protein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
-
DyP is a promising enzyme for the decolorizing treatment of dye-contaminated water
additional information
Show AA Sequence (143 entries)
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