Regulation of activity of chloroperoxidase from Serratia marcescens.

@article{Burd1998RegulationOA,
  title={Regulation of activity of chloroperoxidase from Serratia marcescens.},
  author={V. N. Burd and O. V. Vasilyeva and Alexander I Voskoboev and Karl-Heinz van P{\'e}e},
  journal={Biochemistry. Biokhimiia},
  year={1998},
  volume={63 11},
  pages={
          1299-301
        }
}
The influence of various factors on the activity of chloroperoxidase from Serratia marcescens was investigated. The enzyme is active only in acetate-containing buffers within the pH range 4.2-5.8. F-, Cu2+, [Fe(CN)6]4+, and [Fe(CN)6]3+ inhibit the enzyme. The chloroperoxidase is thermostable and resistant to the effect of lower alcohols. 

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