Phosphatase activity of non‐heme chloroperoxidase from the bacterium Serratia marcescens

FEBS Letters

Burd, Vasilii N¹  Preobrazhenskaya, Yuliya V¹  Voskoboev, Alexander I¹ 

[1] Grodno State University, Department of Biology and Ecology, per. Dovatora 3/1, 230015 Grodno, Belarus

关键词: Chloroperoxidase;    Serratia marcescens;    p-nitrophenylphosphate;    CPO;    chloroperoxidase;    pNPP;    p-nitrophenylphosphate;   

DOI  :  10.1016/S0014-5793(03)00008-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Mg²⁺ and F⁻, and is inhibited by WO₄ ²⁻, tartrate, acetate and phosphate anions. The irreversible inhibition by phenylmethanesulfonyl fluoride, modificator of serine residue in active site, decreases in the presence of phosphate ions. A mechanism of phosphoesters hydrolysis by non-heme haloperoxidases is proposed.

【 授权许可】

Unknown