1.11.1.B2: chloride peroxidase (vanadium-containing)
This is an abbreviated version!
For detailed information about chloride peroxidase (vanadium-containing), go to the full flat file.
Word Map on EC 1.11.1.B2
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1.11.1.B2
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inaequalis
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curvularia
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vanadate
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halide
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bromoperoxidase
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chlorination
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vhpos
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meroterpenoids
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glucose-6-phosphatase
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nodosum
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ascophyllum
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corallina
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prenyltransferase
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peroxo
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vanadiumv
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bipyramidal
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seaweeds
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td-dft
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diagnostics
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synthesis
- 1.11.1.B2
- inaequalis
-
curvularia
- vanadate
- halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
- glucose-6-phosphatase
- nodosum
-
ascophyllum
-
corallina
- prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
- seaweeds
-
td-dft
- diagnostics
- synthesis
Reaction
Synonyms
chloroperoxidase, CPO, Mcl24, More, NapH1, PPHY, V-containing-haloperoxidase, vanadium chloroperoxidase, vanadium haloperoxidase, vanadium-containing chloroperoxidase, vanadium-containing peroxidase, vanadium-dependent chloroperoxidase, vanadium-dependent haloperoxidase, vCPO, VHPO
ECTree
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Engineering
Engineering on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)
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D292A
F397H
12% of the activity of the wild-type enzyme (chlorination of monochlorodimedone), mutant enzyme shows enhancement of bromination activity under certain conditions, inactivation of the mutant enzyme by halide especially at low pH is observed during turnover
H404A
H496A
enzyme loses the ability to bind vanadate covalently, resulting in an inactive enzyme
K353A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase, no clear pH-optimum
P395D/L241V/T343A
P395T/L241V/T343A
20fold increase in brominating activity at pH 8
R360A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
R490A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
S402A
1.8% of the activity of wild-type enzyme (chlorination of monochlorodimedone), mutation decreases activity, mutant enzyme still catalyzes efficiently oxidation of both Cl- and Br-
S427H
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the mutant shows nearly wild type activity at approximately 70% in the monochlorodimedone assay but is unable to catalyze the conversion of 3 into 4 or 5. Instead, the mutant exclusively catalyzes the formation of 3-based bromohydrins
chlorinating activity is drastically reduced to approximately 1%
D292A
strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover
strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover, reduced affinity for vanadium
H404A
chlorinating activity is drastically reduced to approximately 1%
100fold increase in brominating activity at pH 8
P395D/L241V/T343A
100fold increase in brominating activity at pH 8, the brominating activity at pH 5 was increased by a factor of 6
P395D/L241V/T343A
40fold increase in brominating activity at pH 8
P395D/L241V/T343A
the mutant enzyme significantly reduces the levels of all tested microbes. This mutant has a much better potential for surface cleansing formulation at pH 8 than the wild-type enzyme
P395D/L241V/T343A
mutant exhibits 5- to 100fold improved catalytic activity