Document Detail

Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium.
MedLine Citation:
PMID:  11985594     Owner:  NLM     Status:  MEDLINE    
Vanadium haloperoxidases and the bacterial class A nonspecific acid phosphatases have a conserved active site. It is shown that vanadate-substituted recombinant acid phosphatase from Shigella flexneri (PhoN-Sf) and Salmonella enterica ser. typhimurium (PhoN-Se) in the presence of H2O2 are able to oxidize bromide to hypobromous acid. Vanadate is essential for this activity. The kinetic parameters for the artificial bromoperoxidases have been determined. The Km value for H2O2 is about the same as that for the vanadium bromoperoxidases from the seaweed Ascophyllum nodosum. However, the Km value for Br- is about 10-20 times higher, and the turnover values of about 3.4 min-1 and 33 min-1 for PhoN-Sf and PhoN-Se, respectively, are much slower, than those of the native bromoperoxidase. Thus, despite the striking similarity in the active-site structures of the vanadium haloperoxidases and the acid phosphatase, the turnover frequency is low, and clearly the active site of acid phosphatases is not optimized for haloperoxidase activity. Like the native vanadium bromoperoxidase, the vanadate-substituted PhoN-Sf and PhoN-Se catalyse the enantioselective sulfoxidation of thioanisole.
Naoko Tanaka; Valérie Dumay; Qianning Liao; Alex J Lange; Ron Wever
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  269     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  2002 Apr 
Date Detail:
Created Date:  2002-05-02     Completed Date:  2002-06-21     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  2162-7     Citation Subset:  IM    
Institute for Molecular Chemistry, University of Amsterdam, The Netherlands.
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MeSH Terms
Acid Phosphatase / genetics,  metabolism*
Binding Sites
Peroxidases / genetics,  metabolism*
Recombinant Proteins / genetics,  metabolism
Salmonella typhimurium / enzymology*
Shigella flexneri / enzymology*
Substrate Specificity / genetics
Vanadates / metabolism
Grant Support
Reg. No./Substance:
0/Recombinant Proteins; 0/Vanadates; EC 1.11.1.-/Peroxidases; EC 1.11.1.-/bromide peroxidase; EC Phosphatase

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