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Literature summary for 1.11.1.B2 extracted from

  • Van Schijndel, J.W.; Barnett, P.; Roelse, J.; Vollenbroek, E.G.; Wever, R.
    The stability and steady-state kinetics of vanadium chloroperoxidase from the fungus Curvularia inaequalis (1994), Eur. J. Biochem., 225, 151-157.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cl- pH 4.1: mixed type inhibition with respect to H2O2, pH 3.1: competitive inhibition Curvularia inaequalis
NO3- pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2 Curvularia inaequalis

Metals/Ions

Metals/Ions Comment Organism Structure
Vanadium vanadium enzyme Curvularia inaequalis

Organism

Organism UniProt Comment Textmining
Curvularia inaequalis P49053
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
initial decrease of activity, after which the enzyme remains stable for 6.5 h Curvularia inaequalis