title: Regulation of activity of chloroperoxidase from Serratia marcescens.
abstract: 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.
authors.affiliation: Grodno State University, Grodno, 230012, Belarus. burd@univer.belpak. grodno.by.
authors.forename: V N
authors.initials: VN
authors.lastname: Burd
authors.forename: O V
authors.initials: OV
authors.lastname: Vasilyeva
authors.forename: A I
authors.initials: AI
authors.lastname: Voskoboev
authors.forename: K H
authors.initials: KH
authors.lastname: van Pee
mesh_terms: D002021:Buffers; D002711:Chloride Peroxidase / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012706:Serratia marcescens / Q000201:enzymology*; D013816:Thermodynamics
chemical_list: D002021:Buffers; D004791:Enzyme Inhibitors; D002711:Chloride Peroxidase