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Literature summary for 1.11.1.B2 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.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D292A strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover Curvularia inaequalis
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

Metals/Ions Comment Organism Structure
Vanadium vanadium enzyme Curvularia inaequalis

Organism

Organism UniProt Comment Textmining
Curvularia inaequalis P49053
-
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
brominating activity of mutant enzyme H404A Curvularia inaequalis

Cofactor

Cofactor Comment Organism Structure
additional information non-heme chloroperoxidase Curvularia inaequalis