Phosphatase activity of non-heme chloroperoxidase from the bacterium Serratia marcescens.
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.
Preobrazhenskaya
Yuliya V
YV
Grodno State University, Department of Biology and Ecology, per. Dovatora 3/1, 230015 Grodno, Belarus. dima555552002@yahoo.com
Voskoboev
Alexander I
AI
Burd
Vasilii N
VN
D002711:Chloride Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D006418:Heme; D008956:Models, Chemical; D009596:Nitrophenols / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D012706:Serratia marcescens / Q000201:enzymology*
D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D006418:Heme; D002711:Chloride Peroxidase; D010744:Phosphoric Monoester Hydrolases