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Literature summary for 1.11.1.B2 extracted from

  • Hemrika, W.; Renirie, R.; Macedo-Ribeiro, S.; Messerschmidt, A.; Wever, R.
    Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, and Arg490 (1999), J. Biol. Chem., 274, 23820-23827.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae Curvularia inaequalis

Protein Variants

Protein Variants Comment Organism
H496A enzyme loses the ability to bind vanadate covalently, resulting in an inactive enzyme Curvularia inaequalis
K353A enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase, no clear pH-optimum Curvularia inaequalis
R360A enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase Curvularia inaequalis
R490A enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase Curvularia inaequalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
H2O2
-
Curvularia inaequalis
0.9
-
Cl-
-
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
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Curvularia inaequalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
chlorination of monochlorodimedone Curvularia inaequalis