[Hydrolysis of phosphoether bonds of heme-independent chloride peroxidase from Serratia marcescens].
Heme- and metal-independent chloroperoxidase from Serratia marcescens W 250 is shown to be capable of catalyzing the p-nitrophenyl phosphate hydrolysis. The parameters of the phosphatase reaction are determined and inhibitors and activators of the process are found. A hypothetical mechanism of the hydrolysis of phosphoesters by heme- and metal-independent haloperoxidases is suggested. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2003, vol. 29, no. 6; see also http://www.maik.ru.
Preobrazhenskaia
Iu V
IuV
Kupala State University, per. Dovatora 3/1, Grodno, 230012 Belarus. burd@mail.grsu.grodno.by
Voskoboev
A I
AI
Burd'
V N
VN
D002711:Chloride Peroxidase / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004952:Esters / Q000378:metabolism*; D006418:Heme / Q000378:metabolism; D006868:Hydrolysis; D009943:Organophosphorus Compounds / Q000378:metabolism*; D012706:Serratia marcescens / Q000201:enzymology*
D004952:Esters; D009943:Organophosphorus Compounds; D006418:Heme; D002711:Chloride Peroxidase