Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium

Naoko Tanaka, Valérie Dumay, Qianning Liao, Alex J Lange, Ron Wever

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Vanadium haloperoxidases and the bacterial class A non-specific 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 phophatase, 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.

Original languageEnglish (US)
Pages (from-to)2162-2167
Number of pages6
JournalEuropean Journal of Biochemistry
Volume269
Issue number8
DOIs
StatePublished - May 6 2002

Fingerprint

Shigella flexneri
Salmonella
Salmonella enterica
Vanadates
Acid Phosphatase
Catalytic Domain
Vanadium
Ascophyllum
Seaweed
Bromides
Kinetic parameters
Acids
bromide peroxidase

Keywords

  • Acid phosphatase
  • Brominating activity
  • Enantioselective sulfoxidation
  • Vanadium bromoperoxidase
  • Vanadium chloroperoxidase

Cite this

Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium. / Tanaka, Naoko; Dumay, Valérie; Liao, Qianning; Lange, Alex J; Wever, Ron.

In: European Journal of Biochemistry, Vol. 269, No. 8, 06.05.2002, p. 2162-2167.

Research output: Contribution to journalArticle

Tanaka, Naoko ; Dumay, Valérie ; Liao, Qianning ; Lange, Alex J ; Wever, Ron. / Bromoperoxidase activity of vanadate-substituted acid phosphatases from Shigella flexneri and Salmonella enterica ser. typhimurium. In: European Journal of Biochemistry. 2002 ; Vol. 269, No. 8. pp. 2162-2167.
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AB - Vanadium haloperoxidases and the bacterial class A non-specific 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 phophatase, 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.

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