Literature summary extracted from

Renirie, R.; Hemrika, W.; Wever, R.
Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms (2000), J. Biol. Chem., 275, 11650-11657.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.11.1.B2	D292A	strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover	Curvularia inaequalis
1.11.1.B2	H404A	strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover, reduced affinity for vanadium	Curvularia inaequalis

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.11.1.B2	Vanadium	vanadium enzyme	Curvularia inaequalis

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.11.1.B2	Curvularia inaequalis	P49053	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.11.1.B2	monochlorodimedon + Cl- + H2O2	-	Curvularia inaequalis	dichlorodimedon + H2O	-	?
1.11.1.B2	monochlorodimedone + Br- + H2O2	-	Curvularia inaequalis	?	-	?

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.11.1.B2	7	-	brominating activity of mutant enzyme H404A	Curvularia inaequalis

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.11.1.B2	additional information	non-heme chloroperoxidase	Curvularia inaequalis

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Release 2023.1 (January 2023)