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1.11.1.19: dye decolorizing peroxidase

This is an abbreviated version!
For detailed information about dye decolorizing peroxidase, go to the full flat file.

Word Map on EC 1.11.1.19

Reaction

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

Synonyms

AnaPX, AncDyPD-b1, DtpA, dye decolorizing peroxidases type B, dye-decolorizing peroxidase, DyP, DyP I, DyP II, DyP-I, DyP-type peroxidase, DyP-V, DyP1, DyP1B, DyP2, DyP3, DyP4, DyPA, EfeB, LiP BA45, LiP-SN, manganese-independent peroxidase I, manganese-independent peroxidase II, MnP BA30, POX, reactiveblue-5: hydrogen-peroxide oxidoreductase, TT1485, tyrA, YcdB, YfeX, YRW2 Mb, YwbN

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.19 dye decolorizing peroxidase

Engineering

Engineering on EC 1.11.1.19 - dye decolorizing peroxidase

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PROTEIN VARIANTS
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
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
D222A
-
the mutant shows reduced catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), Reactive Black 5 and H2O, as compared to the wild type enzyme
D222E
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and reduced activity with Reactive Black 5 and H2O, as compared to the wild type enzyme
D222E/R390K
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and reduced activity with Reactive Black 5 and H2O, as compared to the wild type enzyme
R390A
-
the mutant shows reduced catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), Reactive Black 5 and H2O, as compared to the wild type enzyme
R390K
-
the mutant shows increased catalytic efficiency with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and H2O and reduced activity with Reactive Black 5, as compared to the wild type enzyme
E201D
-
the mutant shows a significantly higher activity on several dyes when compared with the wild type enzyme and the activity of the mutant enzyme is almost 10fold greater than the wild type at pH 4.0
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
L246W
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
S234Y
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
D143A
-
the mutant shows no activity towards 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and guaiacol, but about 20% of wild type activity with Reactive Blue 19 and 10% activity with catechol
-
D143N
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
H215A
-
the mutant shows no activity towards guaiacol, catechol, Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
R232E
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 40% of wild type activity with guaiacol and 35% activity with catechol
-
R232L
-
the mutant shows no activity towards Reactive Blue 19 and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), but about 90% of wild type activity with guaiacol and 50% activity with catechol
-
W109F
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W147F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W212F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W264F
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
W264H
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W264Y
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380F
the mutant shows severely decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380G
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
W380Y
the mutation does not weaken the first step of the catalytic cycles (oxidation of the resting state Fe3+ by H2O2) significantly, but it weakens the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and other reducing substrates which has a larger size than H2O2
W109F
-
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
-
W147F
-
the mutant shows decreased oxidative activity and increased decolorizing ability compared to the wild type enzyme
-
W264D
-
inactive
-
W264G
-
inactive
-
W264Y
-
the mutant shows decreased oxidative activity and decolorizing ability compared to the wild type enzyme
-
D143A
active site mutant
D143A/R232A
active site mutant
R232A
active site mutant
H164A
DyP activity and heme binding are lost in the H164A mutant
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
E188K
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V
-
the mutant shows 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/A142V/H125Y
-
the mutant shows a 100fold enhanced catalytic efficiency (kcat/Km) for 2,6-dimethoxyphenol and 2fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
E188K/H125R
-
the mutant shows 6fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
H125R
-
the mutant shows 3-4fold higher activity for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in comparison to the wild type enzyme
-
Y288F
-
kcat is least affected by the mutation whereas Km shows significant increase compared to the wild type enzyme
Y374F
-
the mutation results in an overall 5.5fold decrease in catalytic efficiency as compared to the wild type enzyme
Y437F
-
kcat is least affected by the mutation whereas Km shows significant increase compared to the wild type enzyme
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
D220A
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
D220F
the mutant shows reduced activity compared to the wild type enzyme
D220G
the mutant shows reduced activity compared to the wild type enzyme
D220H
the mutant shows reduced activity compared to the wild type enzyme
D220K
the mutant shows reduced activity compared to the wild type enzyme
D220N
the mutant shows reduced activity compared to the wild type enzyme
H312C
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
D220A
-
the catalytic efficiency of the mutant toward H2O2 drops by 22fold compared to the wild type enzyme
-
D220N
-
the mutant shows reduced activity compared to the wild type enzyme
-
H312C
-
the catalytic efficiency of the mutant toward H2O2 drops by 88fold compared to the wild type enzyme
-
D138V
-
the mutant displays significantly increased activity at pH 6.5 as compared to the wild type enzyme
D144H
-
almost completely inactive
H178F
-
the mutant exhibits about 35% of wild type activity
H178W
-
inactive
H178Y
-
inactive
T278V
-
the mutant shows wild type activity