{"refrec":{"BRefID":257180,"RR":"<b>Tang, K.; Su, Y.; Brackman, G.; Cui, F.; Zhang, Y.; Shi, X.; Coenye, T.; Zhang, X.</b> (2015). MomL, a novel marine-derived <i>N</i>-Acyl homoserine lactonase from <i>Muricauda olearia</i>. <i>Appl. Environ. Microbiol. 81(2)</i>: 774-782. <a href=\"https://dx.doi.org/10.1128/AEM.02805-14\" target=\"_blank\">https://dx.doi.org/10.1128/AEM.02805-14</a>","BEntID":249189,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Appl. Environ. Microbiol. 81(2)</i>: 774-782. <a href=\"https://dx.doi.org/10.1128/AEM.02805-14\" target=\"_blank\">https://dx.doi.org/10.1128/AEM.02805-14</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Tang, K.; Su, Y.; Brackman, G.; Cui, F.; Zhang, Y.; Shi, X.; Coenye, T.; Zhang, X.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Tang, K. <i>et al.</i>","Englishabstract":"Gram-negative bacteria use <i>N</i>-acyl homoserine lactones (AHLs) as quorum sensing (QS) signaling molecules for interspecies communication, and AHL-dependent QS is related with virulence factor production in many bacterial pathogens. Quorum quenching, the enzymatic degradation of                      the signaling molecule, would attenuate virulence rather than kill the pathogens, and thereby reduce the potential for evolution of drug resistance. In a previous study, we showed that <i>Muricauda olearia</i> Th120, belonging to the class <i>Flavobacteriia</i>, has strong AHL degradative activity. In this study, an AHL lactonase (designated MomL), which could degrade both short- and long-chain AHLs with or without a substitution of <i>oxo</i>-group at the C-3 position, was identified from Th120. Liquid chromatography-mass spectrometry analysis demonstrated that MomL functions as an AHL lactonase catalyzing AHL degradation through lactone hydrolysis. MomL is an AHL lactonase belonging to the metallo-ß-lactamase superfamily that harbors an N-terminal signal peptide. The overall catalytic efficiency of MomL for C<sub>6</sub>-HSL is ~2.9 × 10<sup>5</sup> s<sup>-1</sup> M<sup>-1</sup>. Metal analysis and site-directed mutagenesis showed that, compared to AiiA, MomL has a different metal-binding capability and requires the histidine and aspartic acid residues for activity, while it shares the “HXHXDH” motif with other AHL lactonases belonging to the metallo-ß-lactamase superfamily. This suggests that MomL is a representative of a novel type of secretory AHL lactonase. Furthermore, MomL significantly attenuated the virulence of <i>Pseudomonas aeruginosa</i> in a <i>Caenorhabditis elegans</i> infection model, which suggests that MomL has the potential to be used as a therapeutic agent.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"MomL, a novel marine-derived <i>N</i>-Acyl homoserine lactonase from <i>Muricauda olearia</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-25 01:32:15.375099","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2015,"MonPub":null,"DateUpdate":"2020-06-25","DateCreate":"2016-05-29","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000347377500033","VABBcode":null,"OpenAcc":1,"DOI":"10.1128/AEM.02805-14"},"refs":null,"anarec":{"AnaID":257180,"PubliDate":2015,"Pagination":"774-782","XtraPublOfAnaID":null,"ISBN":null,"Volume":"81","Issue":"2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42360,"SerRR":"Applied and Environmental Microbiology. American Society for Microbiology: Washington.  ISSN 0099-2240; e-ISSN 1098-5336","StandardTitleSer":"Applied and Environmental Microbiology","ISSN":"0099-2240","AbbrevSer":"Appl. Environ. 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