<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7</volume><submitter>Bzdrenga J</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>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.&lt;h4>Results&lt;/h4>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.&lt;h4>Conclusion&lt;/h4>Kinetic experiments show that SacPox is a proficient lactonase, including at roo</pubmed_abstract><journal>BMC research notes</journal><pagination>333</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4068969</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.</pubmed_title><pmcid>PMC4068969</pmcid><pubmed_authors>Gotthard G</pubmed_authors><pubmed_authors>Champion C</pubmed_authors><pubmed_authors>Hiblot J</pubmed_authors><pubmed_authors>Chabriere E</pubmed_authors><pubmed_authors>Bzdrenga J</pubmed_authors><pubmed_authors>Elias M</pubmed_authors></additional><is_claimable>false</is_claimable><name>SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase.</name><description>&lt;h4>Background&lt;/h4>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.&lt;h4>Results&lt;/h4>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.&lt;h4>Conclusion&lt;/h4>Kinetic experiments show that SacPox is a proficient lactonase, including at roo</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Jun</publication><modification>2026-05-04T07:48:34.53Z</modification><creation>2019-03-27T01:30:46Z</creation></dates><accession>S-EPMC4068969</accession><cross_references><pubmed>24894602</pubmed><doi>10.1186/1756-0500-7-333</doi></cross_references></HashMap>