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Enzymology and Protein Engineering

Haloalkylphosphorus Hydrolases Purified from Sphingomonas sp. Strain TDK1 and Sphingobium sp. Strain TCM1

Katsumasa Abe, Satoshi Yoshida, Yuto Suzuki, Junichi Mori, Yuka Doi, Shouji Takahashi, Yoshio Kera
R. E. Parales, Editor
Katsumasa Abe
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Satoshi Yoshida
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Yuto Suzuki
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Junichi Mori
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Yuka Doi
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Shouji Takahashi
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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Yoshio Kera
Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan
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R. E. Parales
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DOI: 10.1128/AEM.01845-14
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ABSTRACT

Phosphotriesterases catalyze the first step of organophosphorus triester degradation. The bacterial phosphotriesterases purified and characterized to date hydrolyze mainly aryl dialkyl phosphates, such as parathion, paraoxon, and chlorpyrifos. In this study, we purified and cloned two novel phosphotriesterases from Sphingomonas sp. strain TDK1 and Sphingobium sp. strain TCM1 that hydrolyze tri(haloalkyl)phosphates, and we named these enzymes haloalkylphosphorus hydrolases (TDK-HAD and TCM-HAD, respectively). Both HADs are monomeric proteins with molecular masses of 59.6 (TDK-HAD) and 58.4 kDa (TCM-HAD). The enzyme activities were affected by the addition of divalent cations, and inductively coupled plasma mass spectrometry analysis suggested that zinc is a native cofactor for HADs. These enzymes hydrolyzed not only chlorinated organophosphates but also a brominated organophosphate [tris(2,3-dibromopropyl) phosphate], as well as triaryl phosphates (tricresyl and triphenyl phosphates). Paraoxon-methyl and paraoxon were efficiently degraded by TCM-HAD, whereas TDK-HAD showed weak activity toward these substrates. Dichlorvos was degraded only by TCM-HAD. The enzymes displayed weak or no activity against trialkyl phosphates and organophosphorothioates. The TCM-HAD and TDK-HAD genes were cloned and found to encode proteins of 583 and 574 amino acid residues, respectively. The primary structures of TCM-HAD and TDK-HAD were very similar, and the enzymes also shared sequence similarity with fenitrothion hydrolase (FedA) of Burkholderia sp. strain NF100 and organophosphorus hydrolase (OphB) of Burkholderia sp. strain JBA3. However, the substrate specificities and quaternary structures of the HADs were largely different from those of FedA and OphB. These results show that HADs from sphingomonads are novel members of the bacterial phosphotriesterase family.

FOOTNOTES

    • Received 4 June 2014.
    • Accepted 10 July 2014.
    • Accepted manuscript posted online 18 July 2014.
  • Supplemental material for this article may be found at http://dx.doi.org/10.1128/AEM.01845-14.

  • Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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Haloalkylphosphorus Hydrolases Purified from Sphingomonas sp. Strain TDK1 and Sphingobium sp. Strain TCM1
Katsumasa Abe, Satoshi Yoshida, Yuto Suzuki, Junichi Mori, Yuka Doi, Shouji Takahashi, Yoshio Kera
Appl. Environ. Microbiol. Aug 2014, 80 (18) 5866-5873; DOI: 10.1128/AEM.01845-14

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Haloalkylphosphorus Hydrolases Purified from Sphingomonas sp. Strain TDK1 and Sphingobium sp. Strain TCM1
Katsumasa Abe, Satoshi Yoshida, Yuto Suzuki, Junichi Mori, Yuka Doi, Shouji Takahashi, Yoshio Kera
Appl. Environ. Microbiol. Aug 2014, 80 (18) 5866-5873; DOI: 10.1128/AEM.01845-14
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