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ABSTRACT: 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 roo
SUBMITTER: Bzdrenga J
PROVIDER: S-EPMC4068969 | biostudies-literature | 2014 Jun
REPOSITORIES: biostudies-literature