SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase

BMC Research Notes

Eric Chabriere²  Mikael Elias¹  Charlotte Champion²  Guillaume Gotthard²  Julien Hiblot²  Janek Bzdrenga² 

[1] Weizmann Institute of Science, Biological Chemistry, Rehovot, Israel;URMITE UMR CNRS-IRD 6236, IFR48, Faculté de Médecine et de Pharmacie, Université de la Méditerranée, Marseille, France

关键词: Thermoacidophile;    Extremophile;    Phosphotriesterase;    Quorum sensing;    PLL;    Lactonase;   

Others  :  1132590
DOI  :  10.1186/1756-0500-7-333

 received in 2014-02-04, accepted in 2014-05-27,  发布年份 2014

【 摘 要 】

Background

SacPox, an enzyme from the extremophilic crenarchaeal Sulfolobus acidocaldarius (Sac), was isolated by virtue of its phosphotriesterase (or paraoxonase; Pox) activity, i.e. its ability to hydrolyze the neurotoxic organophosphorus insecticides. Later on, SacPox was shown to belong to the Phosphotriesterase-Like Lactonase family that comprises natural lactonases, possibly involved in quorum sensing, and endowed with promiscuous, phosphotriesterase activity.

Results

Here, we present a comprehensive and broad enzymatic characterization of the natural lactonase and promiscuous organophosphorus hydrolase activities of SacPox, as well as a structural analysis using a model.

Conclusion

Kinetic experiments show that SacPox is a proficient lactonase, including at room temperature. Moreover, we discuss the observed differences in substrate specificity between SacPox and its closest homologues SsoPox and SisLac together with the possible structural causes for these observations.

【 授权许可】

   
2014 Bzdrenga et al.; licensee BioMed Central Ltd.

【 图 表 】

Figure 1.

Figure 2.

Figure 3.

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