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show all sequences of 1.11.1.19

Molecular characterization of a novel DyP-type peroxidase from the cyanobacterium Anabaena sp. PCC 7120

Ogola, H.J.; Kamiike, T.; Hashimoto, N.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.; Appl. Environ. Microbiol. 75, 7509-7518 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
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
Anabaena sp.
Application
Application
Commentary
Organism
additional information
AnaPX is a useful alternative of horseradish peroxidase or fungal DyPs
Anabaena sp.
Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Anabaena sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
less than 50% inhibition at 50 mM
Anabaena sp.
Fe2+
AnaPX is highly sensitive to Fe2+ (98.8% inhibition at 5 mM)
Anabaena sp.
KCN
AnaPX shows very low sensitivity to KCN which causes only 9% and 14% inhibition of the activity at 1 and 10 mM, respectively
Anabaena sp.
Mn2+
57.1% inhibition at 5 mM
Anabaena sp.
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
Anabaena sp.
NaN3
AnaPX is highly sensitive to NaN3 (82% inhibition at 10 mM)
Anabaena sp.
phenylhydrazine
AnaPX is highly sensitive to the suicide substrate phenylhydrazine (complete inhibition at 1 mM)
Anabaena sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0036
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
0.0058
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53280
-
4 * 53280, native enzyme, MALDI-TOF spectrometry
Anabaena sp.
53368
-
4 * 53368, deduced from amino acid sequence
Anabaena sp.
54000
-
4 * 54000, native enzyme, SDS-PAGE
Anabaena sp.
209000
-
native enzyme, gel filtration
Anabaena sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Anabaena sp.
Q8YWM0
strain PCC7120 (ATCC 27893)
-
Oxidation Stability
Oxidation Stability
Organism
the enzyme retains more than 50% of its activity at 2.5 mM H2O2
Anabaena sp.
Purification (Commentary)
Commentary
Organism
Toyopearl DEAE-650M column chromatography, Toyopearl butyl-650M column chromatography, and hydroxylapatite column chromatography
Anabaena sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.6
-
recombinant enzyme from crude extract, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
Anabaena sp.
54
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using syringaldehyde as substrate
Anabaena sp.
71
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,6-dimethoxyphenol as substrate
Anabaena sp.
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
Anabaena sp.
216
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using pyrogallol as substrate
Anabaena sp.
230
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using guaiacol as substrate
Anabaena sp.
283
-
recombinant enzyme after 50.5fold purification, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
Anabaena sp.
290
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using L-ascorbate as substrate
Anabaena sp.
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
Anabaena sp.
374
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADH as substrate
Anabaena sp.
1478
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 4-aminoantipyrine as substrate
Anabaena sp.
Storage Stability
Storage Stability
Organism
4°C, 50 mM potassium phosphate buffer (pH 7.0), 40 days, 10% loss of activity
Anabaena sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + H+
89% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
2,6-dimethoxyphenol + H2O2 + H+
31% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
4-aminoantipyrine + H2O2 + H+
643% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Acid Blue 45 + H2O2 + H+
98% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Acid Blue 45 + H2O
-
-
-
?
Acid Red 151 + H2O2 + H+
12% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Acid Red 151 + H2O
-
-
-
?
Congo Red + H2O2 + H+
12% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Congo Red + H2O
-
-
-
?
D-isoascorbate + H2O2 + H+
134% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Direct Sky Blue 6B + H2O2 + H+
50% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Direct Sky Blue 6B + H2O
-
-
-
?
guaiacol + H2O2 + H+
100% activity
695785
Anabaena sp.
?
-
-
-
?
L-ascorbate + H2O2 + H+
126% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
additional information
the decolorization activity of AnaPX toward azo dyes is relatively low. No decolorization of Toluidine Blue O, Reactive Red 33, and Reactive Yellow 2 is observed
695785
Anabaena sp.
?
-
-
-
-
Procion Blue H-ERD + H2O2 + H+
90% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Procion Blue H-ERD + H2O
-
-
-
?
Procion Blue H-EXL + H2O2 + H+
72% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Procion Blue H-EXL + H2O
-
-
-
?
pyrogallol + H2O2 + H+
93% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Reactive Black 5 + H2O2 + H+
8% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Blue 114 + H2O2 + H+
187% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 114 + H2O
-
-
-
?
Reactive Blue 19 + H2O2 + H+
153% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 19 + H2O
-
-
-
?
Reactive Blue 4 + H2O2 + H+
64% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 4 + H2O
-
-
-
?
Reactive Blue 5 + H2O2 + H+
123% activity compared to guaiacol, the apparent optimum concentration of H2O2 required for the decolorization of Reactive Blue 5 by AnaPX is 0.4 mM
695785
Anabaena sp.
oxidized Reactive Blue 5 + H2O
-
-
-
?
Reactive Green 19 + H2O2 + H+
35% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Green 19 + H2O
-
-
-
?
Reactive Orange 14 + H2O2 + H+
10% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Orange 14 + H2O
-
-
-
?
Reactive Red 120 + H2O2 + H+
5% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Red 120 + H2O
-
-
-
?
Reactive Yellow 86 + H2O2 + H+
3% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Yellow 86 + H2O
-
-
-
?
syringaldehyde + H2O2 + H+
23% activity compared to guaiacol
695785
Anabaena sp.
oxidized syringaldehyde + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 53280, native enzyme, MALDI-TOF spectrometry; 4 * 53368, deduced from amino acid sequence; 4 * 54000, native enzyme, SDS-PAGE
Anabaena sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Anabaena sp.
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
60
the enzyme is considerably stable at 30°C and 40°C where it retains more than 90% of its activity, while the enzyme loses more than 90% of its activity after incubation at 50°C and 60°C for 3 h
Anabaena sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
384
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
384
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
4.4
-
Anabaena sp.
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
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
Anabaena sp.
Cofactor
Cofactor
Commentary
Organism
Structure
heme
iron protoporphyrin-containing heme peroxidase, the heme content is estimated to be 0.91 mol per mole of protein
Anabaena sp.
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Anabaena sp.
isoelectric focusing
-
3.7
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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
Anabaena sp.
Application (protein specific)
Application
Commentary
Organism
additional information
AnaPX is a useful alternative of horseradish peroxidase or fungal DyPs
Anabaena sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Anabaena sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
iron protoporphyrin-containing heme peroxidase, the heme content is estimated to be 0.91 mol per mole of protein
Anabaena sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
less than 50% inhibition at 50 mM
Anabaena sp.
Fe2+
AnaPX is highly sensitive to Fe2+ (98.8% inhibition at 5 mM)
Anabaena sp.
KCN
AnaPX shows very low sensitivity to KCN which causes only 9% and 14% inhibition of the activity at 1 and 10 mM, respectively
Anabaena sp.
Mn2+
57.1% inhibition at 5 mM
Anabaena sp.
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
Anabaena sp.
NaN3
AnaPX is highly sensitive to NaN3 (82% inhibition at 10 mM)
Anabaena sp.
phenylhydrazine
AnaPX is highly sensitive to the suicide substrate phenylhydrazine (complete inhibition at 1 mM)
Anabaena sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0036
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
0.0058
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53280
-
4 * 53280, native enzyme, MALDI-TOF spectrometry
Anabaena sp.
53368
-
4 * 53368, deduced from amino acid sequence
Anabaena sp.
54000
-
4 * 54000, native enzyme, SDS-PAGE
Anabaena sp.
209000
-
native enzyme, gel filtration
Anabaena sp.
Oxidation Stability (protein specific)
Oxidation Stability
Organism
the enzyme retains more than 50% of its activity at 2.5 mM H2O2
Anabaena sp.
Purification (Commentary) (protein specific)
Commentary
Organism
Toyopearl DEAE-650M column chromatography, Toyopearl butyl-650M column chromatography, and hydroxylapatite column chromatography
Anabaena sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
5.6
-
recombinant enzyme from crude extract, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
Anabaena sp.
54
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using syringaldehyde as substrate
Anabaena sp.
71
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 2,6-dimethoxyphenol as substrate
Anabaena sp.
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
Anabaena sp.
216
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using pyrogallol as substrate
Anabaena sp.
230
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using guaiacol as substrate
Anabaena sp.
283
-
recombinant enzyme after 50.5fold purification, using Reactive Blue 5 as substrate, pH 4.0-4.4, at 37°C
Anabaena sp.
290
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using L-ascorbate as substrate
Anabaena sp.
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
Anabaena sp.
374
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using NADH as substrate
Anabaena sp.
1478
-
recombinant enzyme, in 50 mM citrate buffer (pH 4.0-4.4), at 37°C, using 4-aminoantipyrine as substrate
Anabaena sp.
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 50 mM potassium phosphate buffer (pH 7.0), 40 days, 10% loss of activity
Anabaena sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + H+
89% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
2,6-dimethoxyphenol + H2O2 + H+
31% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
4-aminoantipyrine + H2O2 + H+
643% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Acid Blue 45 + H2O2 + H+
98% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Acid Blue 45 + H2O
-
-
-
?
Acid Red 151 + H2O2 + H+
12% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Acid Red 151 + H2O
-
-
-
?
Congo Red + H2O2 + H+
12% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Congo Red + H2O
-
-
-
?
D-isoascorbate + H2O2 + H+
134% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Direct Sky Blue 6B + H2O2 + H+
50% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Direct Sky Blue 6B + H2O
-
-
-
?
guaiacol + H2O2 + H+
100% activity
695785
Anabaena sp.
?
-
-
-
?
L-ascorbate + H2O2 + H+
126% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
additional information
the decolorization activity of AnaPX toward azo dyes is relatively low. No decolorization of Toluidine Blue O, Reactive Red 33, and Reactive Yellow 2 is observed
695785
Anabaena sp.
?
-
-
-
-
Procion Blue H-ERD + H2O2 + H+
90% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Procion Blue H-ERD + H2O
-
-
-
?
Procion Blue H-EXL + H2O2 + H+
72% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Procion Blue H-EXL + H2O
-
-
-
?
pyrogallol + H2O2 + H+
93% activity compared to guaiacol
695785
Anabaena sp.
?
-
-
-
?
Reactive Black 5 + H2O2 + H+
8% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Blue 114 + H2O2 + H+
187% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 114 + H2O
-
-
-
?
Reactive Blue 19 + H2O2 + H+
153% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 19 + H2O
-
-
-
?
Reactive Blue 4 + H2O2 + H+
64% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Blue 4 + H2O
-
-
-
?
Reactive Blue 5 + H2O2 + H+
123% activity compared to guaiacol, the apparent optimum concentration of H2O2 required for the decolorization of Reactive Blue 5 by AnaPX is 0.4 mM
695785
Anabaena sp.
oxidized Reactive Blue 5 + H2O
-
-
-
?
Reactive Green 19 + H2O2 + H+
35% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Green 19 + H2O
-
-
-
?
Reactive Orange 14 + H2O2 + H+
10% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Orange 14 + H2O
-
-
-
?
Reactive Red 120 + H2O2 + H+
5% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Red 120 + H2O
-
-
-
?
Reactive Yellow 86 + H2O2 + H+
3% decolorization rate compared to Reactive Blue 5
695785
Anabaena sp.
oxidized Reactive Yellow 86 + H2O
-
-
-
?
syringaldehyde + H2O2 + H+
23% activity compared to guaiacol
695785
Anabaena sp.
oxidized syringaldehyde + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 53280, native enzyme, MALDI-TOF spectrometry; 4 * 53368, deduced from amino acid sequence; 4 * 54000, native enzyme, SDS-PAGE
Anabaena sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Anabaena sp.
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
60
the enzyme is considerably stable at 30°C and 40°C where it retains more than 90% of its activity, while the enzyme loses more than 90% of its activity after incubation at 50°C and 60°C for 3 h
Anabaena sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
384
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
384
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4
4.4
-
Anabaena sp.
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
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
Anabaena sp.
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Anabaena sp.
isoelectric focusing
-
3.7
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
66000
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
120000
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
66000
-
H2O2
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
120000
-
Reactive Blue 5
in 50 mM citrate buffer (pH 4.0-4.4), at 37°C
Anabaena sp.
Other publictions for EC 1.11.1.19
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
724099
Santos
New dye-decolorizing peroxidas ...
Bacillus subtilis
Appl. Microbiol. Biotechnol.
98
253-2065
2014
-
-
1
-
-
-
-
6
-
-
1
-
-
1
-
-
-
-
-
-
-
-
6
1
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
6
-
-
1
-
-
-
-
-
-
-
-
-
6
1
1
-
-
-
-
-
-
-
-
-
-
-
5
5
724033
Salvachua
Characterization of a novel dy ...
Irpex lacteus
Appl. Environ. Microbiol.
79
4316-4324
2013
-
-
-
-
-
-
1
6
-
-
-
-
-
4
-
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-
-
-
1
-
5
-
-
-
-
6
-
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-
-
-
-
-
-
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1
-
6
-
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-
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-
1
-
5
-
-
-
-
6
-
-
-
-
-
-
-
-
5
5
724379
Sezer
Distinct structural and redox ...
Bacillus subtilis
Biochemistry
52
3074-3084
2013
-
-
-
1
-
-
-
-
-
-
-
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-
1
-
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1
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-
-
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-
-
-
-
-
-
-
-
-
-
-
724776
Wang
Recombinant expression, purifi ...
Zymomonas mobilis, Zymomonas mobilis ATXX 31821
Chin. J. Biotechnol.
29
772-784
2013
-
-
1
-
-
-
-
-
-
-
2
-
-
6
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725543
Strittmatter
First crystal structure of a f ...
Auricularia auricula-judae
J. Biol. Chem.
288
4095-4102
2013
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
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-
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-
-
-
1
-
-
-
-
-
-
1
1
-
-
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-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723971
Li
Identification and molecular c ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa PKE117
Appl. Biochem. Biotechnol.
166
774-785
2012
-
-
1
-
-
-
1
1
-
3
2
-
-
4
-
-
-
-
-
-
-
-
10
1
-
-
2
1
1
-
2
1
-
1
-
-
-
1
1
-
-
-
-
1
-
1
-
3
2
-
-
-
-
-
-
-
-
-
10
1
-
-
2
1
1
-
2
1
-
-
-
-
1
1
724963
Yoshida
The catalytic mechanism of dye ...
Bjerkandera adusta
FEBS J.
278
2387-2394
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710965
Liers
DyP-like peroxidases of the je ...
Auricularia auricula-judae
Appl. Microbiol. Biotechnol.
85
1869-1879
2010
-
-
-
-
-
-
-
11
-
1
2
-
-
1
-
-
1
-
-
-
3
2
7
1
-
-
-
11
1
-
1
1
-
2
-
-
-
-
1
-
-
-
-
-
-
11
-
1
2
-
-
-
-
1
-
-
3
2
7
1
-
-
-
11
1
-
1
2
-
-
-
-
10
10
710967
van Bloois
A robust and extracellular hem ...
Thermobifida fusca YX
Appl. Microbiol. Biotechnol.
86
1419-1430
2010
-
-
1
-
2
-
-
2
2
-
2
-
-
2
-
-
1
-
-
-
-
-
9
1
1
-
1
2
1
1
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
2
2
-
2
-
-
-
-
1
-
-
-
-
9
1
1
-
1
2
1
1
-
-
-
-
-
-
2
2
710971
Ogola
Enhancement of hydrogen peroxi ...
Anabaena sp.
Appl. Microbiol. Biotechnol.
87
1727-1736
2010
-
1
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710977
Hofrichter
New and classic families of se ...
Anabaena sp., Auricularia auricula-judae, Bacillus subtilis, Bacteroides thetaiotaomicron, Escherichia coli, Mycetinis scorodonius, Shewanella oneidensis, Termitomyces albuminosus, Thanatephorus cucumeris, Thermobifida fusca
Appl. Microbiol. Biotechnol.
87
871-897
2010
-
10
1
-
-
-
-
-
-
-
1
-
-
10
-
10
-
-
-
-
-
-
51
-
-
-
-
-
1
-
1
10
-
1
-
-
10
1
10
-
-
-
-
-
-
-
-
-
1
-
-
-
10
-
-
-
-
-
51
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
712788
Shakeri
-
Efficient decolorization of an ...
Thanatephorus cucumeris
J. Mol. Catal. B
62
277-281
2010
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
695785
Ogola
Molecular characterization of ...
Anabaena sp.
Appl. Environ. Microbiol.
75
7509-7518
2009
1
1
1
-
-
-
7
2
-
-
4
-
-
5
1
-
1
-
-
-
11
1
24
1
1
-
1
2
1
-
1
1
-
1
-
1
1
1
1
-
-
-
-
7
-
2
-
-
4
-
-
1
-
1
-
-
11
1
24
1
1
-
1
2
1
-
1
1
-
-
-
-
2
2
711333
Sugano
Degradation pathway of an anth ...
Thanatephorus cucumeris
Biodegradation
20
433-440
2009
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
711709
Sugano
DyP-type peroxidases comprise ...
Bacteroides thetaiotaomicron, Escherichia coli, Mycetinis scorodonius, Pleurotus ostreatus, Shewanella oneidensis, Thanatephorus cucumeris, Thermus thermophilus HB8
Cell. Mol. Life Sci.
66
1387-1403
2009
-
-
1
-
1
-
-
-
2
-
2
-
-
8
-
7
1
-
-
-
-
-
21
5
-
-
-
-
-
-
-
7
-
-
-
-
-
1
7
-
1
-
-
-
-
-
2
-
2
-
-
-
7
1
-
-
-
-
21
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712519
Shimokawa
Purification and characterizat ...
Thanatephorus cucumeris
J. Biosci. Bioeng.
107
113-115
2009
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
1
1
-
-
-
3
-
9
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
1
1
-
-
3
-
9
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
712517
Shakeri
Stable repeated-batch producti ...
Thanatephorus cucumeris
J. Biosci. Bioeng.
105
683-686
2008
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
1
-
1
-
-
1
-
-
712518
Shimokawa
Efficient dye decolorization a ...
Thanatephorus cucumeris
J. Biosci. Bioeng.
106
481-487
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
16
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
712777
Shakeri
-
Decolorization of an anthraqui ...
Thanatephorus cucumeris
J. Mol. Catal. B
54
42-49
2008
-
-
1
-
-
-
-
-
-
-
1
-
-
1
1
-
1
-
-
-
-
-
2
-
-
-
-
-
2
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
2
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
710956
Shakeri
Change in turnover capacity of ...
Thanatephorus cucumeris
Appl. Microbiol. Biotechnol.
76
919-926
2007
-
1
1
-
-
1
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712362
Sugano
DyP, a unique dye-decolorizing ...
Thanatephorus cucumeris
J. Biol. Chem.
282
36652-36658
2007
-
1
-
1
1
-
-
-
-
1
1
-
-
3
-
1
1
-
-
-
2
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
1
-
-
-
-
-
-
1
1
-
-
-
1
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
712516
Shakeri
Production of dye-decolorizing ...
Thanatephorus cucumeris
J. Biosci. Bioeng.
103
129-134
2007
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
713479
Zubieta
Identification and structural ...
Shewanella oneidensis MR-1
Proteins Struct. Funct. Bioinform.
69
234-243
2007
-
-
-
1
-
-
-
1
-
-
-
-
-
5
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
713587
Faraco
Identification of a new member ...
Pleurotus ostreatus
World J. Microbiol. Biotechnol.
23
889-893
2007
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710954
Sugano
Complete decolorization of the ...
Thanatephorus cucumeris
Appl. Microbiol. Biotechnol.
73
862-871
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
6
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710722
Saijo
Precipitation diagram and opti ...
Thanatephorus cucumeris
Acta Crystallogr. Sect. F
61
729-732
2005
-
-
1
1
-
-
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
1
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
710721
Sato
A unique dye-decolorizing pero ...
Thanatephorus cucumeris
Acta Crystallogr. Sect. D
D60
149-152
2004
-
-
1
1
-
-
-
-
-
-
1
-
-
3
-
1
1
-
-
-
-
-
1
1
-
-
-
-
1
-
-
1
-
1
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
-
1
1
-
-
-
-
1
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
711063
Sugano
Role of H164 in a unique dye-d ...
Thanatephorus cucumeris
Biochem. Biophys. Res. Commun.
322
126-132
2004
-
-
1
-
2
-
-
-
-
-
5
-
-
4
-
1
1
-
-
-
2
-
11
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
5
-
-
-
1
1
-
-
2
-
11
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
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Sugano
Efficient heterologous express ...
Geotrichum candidum
Appl. Environ. Microbiol.
66
1754-1758
2000
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1
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1
2
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3
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1
-
-
1
2
-
10
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-
1
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
2
-
-
-
-
1
-
1
2
-
10
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1
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2
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712525
Lee
Effect of molasses on the prod ...
Thanatephorus cucumeris
J. Biosci. Bioeng.
89
545-549
2000
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2
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1
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1
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1
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1
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2
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2
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710921
Kim
Purification and characterizat ...
Geotrichum candidum
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65
1029-1035
1999
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-
-
-
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1
4
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1
2
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1
-
1
1
-
-
-
2
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13
1
1
1
1
4
3
-
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1
-
1
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-
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-
1
-
-
-
-
1
-
4
-
1
2
-
-
-
1
1
-
-
2
-
13
1
1
1
1
4
3
-
-
1
-
-
-
-
4
4