02161nas a2200265   4500008004100000022001400041245012500055210006900180260000800249300001200257490000800269520124900277653001601526653002901542653001401571653001301585653002701598100002701625700001901652700002901671700002101700700002101721700002601742856012701768       2020                        eng d  a0300-908400aStructural and enzymatic analysis of a dimeric cholylglycine hydrolase like acylase active on N-acyl homoserine lactones0 aStructural and enzymatic analysis of a dimeric cholylglycine hyd  cOCT  a108-1160 v1773 a<p>The prevalence of substrate cross-reactivity between AHL acylases and beta-lactam acylases provides a glimpse of probable links between quorum sensing and antibiotic resistance in bacteria. Both these enzyme classes belong to the N-terminal nucleophile (Ntn)-hydrolase superfamily. Penicillin V acylases alongside bile salt hydrolases constitute the cholylglycine hydrolase (CGH) group of the Ntn-hydrolase superfamily. Here we report the ability of two acylases, Slac1 and Slac2, from the marine bacterium Shewanella loihica PV4 to hydrolyze AHLs. Three-dimensional structure of Slac1 reveals the conservation of the Ntn hydrolase fold and CGH active site, making it a unique CGH exclusively active on AHLs. Slac1homologs phylogenetically cluster separate from reported CGHs and AHL acylases, thereby representing a functionally distinct sub-class of CGH that might have evolved as an adaptation to the marine environment. We hypothesize that Slac1 could provide the structural framework for understanding this subclass, and further our understanding of the evolutionary link between AHL acylases and beta-lactam acylases. (C) 2020 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.</p>
10aAHL acylase10aCholyolglycine hydrolase10aHomodimer10aNtn-fold10aShewanella loihica-PV41 aPhilem, Pushparani, D.1 aYadav, Yashpal1 aSunder, Avinash, Vellore1 aGhosh, Deepanjan1 aPrabhune, Asmita1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/structural-and-enzymatic-analysis-dimeric-cholylglycine-hydrolase-acylase-active-n-acyl