A comparative study of the inactivation of wild-type, recombinant and two mutant horseradish peroxidase isoenzymes C by hydrogen peroxide and m-chloroperoxybenzoic acid.

Abstract excerpt

The mechanism-based inactivation of four horseradish peroxidase (HRP-C) enzyme variants has been studied kinetically with either hydrogen peroxide or the xenobiotic m-chloroperoxybenzoic acid (mClO2-BzOH) as sole substrate. The concentration and time dependence of inactivation was investigated for the wild-type plant enzyme (HRP-C), the unglycosylated recombinant enzyme (HRP-C*), and two site-directed mutants...

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