Literature summary 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.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.11.1.B2	Cl-	pH 4.1: mixed type inhibition with respect to H2O2, pH 3.1: competitive inhibition	Curvularia inaequalis
1.11.1.B2	NO3-	pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2	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	-	-

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
1.11.1.B2	80	-	initial decrease of activity, after which the enzyme remains stable for 6.5 h	Curvularia inaequalis

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Release 2023.1 (January 2023)