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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

Reaction

RH
+
Cl-
+
H2O2
+
H+
=
RCl
+ 2 H2O

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

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.B2 chloride peroxidase (vanadium-containing)

Engineering

Engineering on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
10fold increase in brominating activity at pH 8
P395D/L241V/T343A
P395E
10fold increase in brominating activity at pH 8
P395H/A399S
5fold increase in brominating activity at pH 8
P395T
6fold increase in brominating activity at pH 8
P395T/L241V
19fold increase in brominating activity at pH 8
P395T/L241V/T343A
20fold increase in brominating activity at pH 8
P395T/T343A
14fold increase in brominating activity at pH 8
R360A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
R360C/I391V
5fold increase in brominating activity at pH 8
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-
H420F
-
inactive
S427H
-
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