Phosphatase activity of non-heme chloroperoxidase from the bacterium Serratia marcescens
| Autor: | Vasilii N Burd, Alexander I. Voskoboev, Yuliya V. Preobrazhenskaya |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Chloroperoxidase
Stereochemistry Phosphatase Biophysics Heme Biochemistry Nitrophenols chemistry.chemical_compound Hydrolysis Organophosphorus Compounds Structural Biology p-nitrophenylphosphate Genetics Hydrogen peroxide Molecular Biology Serratia marcescens chemistry.chemical_classification biology Halogenation Active site Cell Biology biology.organism_classification Phosphoric Monoester Hydrolases Enzyme chemistry Models Chemical biology.protein Chloride Peroxidase |
| Zdroj: | FEBS letters. 536(1-3) |
| ISSN: | 0014-5793 |
| Popis: | Haloperoxidases are enzymes capable of formation of carbon-halogen bonds in the presence of hydrogen peroxide and halide ions. A mechanism of halogenation catalyzed by heme- and metal-independent bacterial haloperoxidases differs from other representatives of this group of enzymes. Here we report for the first time that bacterial non-heme haloperoxidases possess a phosphatase activity. Chloroperoxidase from Serratia marcescens W 250 purified up to homogeneity is shown to catalyze p-nitrophenylphosphate hydrolysis (K(m) value, 1.8+/-0.1 mM at pH 5.7). The reaction is activated by Mg(2+) and F(-), and is inhibited by WO(4)(2-), tartrate, acetate and phosphate anions. The irreversible inhibition by phenylmethanesulfonyl fluoride, modifier of serine residue in active site, decreases in the presence of phosphate ions. A mechanism of phosphoesters hydrolysis by non-heme haloperoxidases is proposed. |
| Databáze: | OpenAIRE |
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