01909nas a2200217   4500008004100000022001400041245016500055210006900220260007900289300001200368490000800380520103200388653001601420653002401436653001001460653002101470653003101491100002201522700002101544856012601565       2015                        eng d  a0273-228900aPossible correlation between bile salt hydrolysis and ahl deamidation: staphylococcus epidermidis RM1, a potent quorum quencher and bile salt hydrolase producer0 aPossible correlation between bile salt hydrolysis and ahl deamid  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcMAY  a140-1500 v1763 a<p>The aim of the present work was to isolate a bile salt hydrolase (BSH) producer from fermented soy curd and explore the ability of the BSH produced to cleave bacterial quorum sensing signals. Bacterial isolates with possible ability to deconjugate bile salts were enriched and isolated on De Man, Rogosa and Sharpe (MRS) medium containing 0.2 % bile salts. BSH-producing positive isolate with orange-pink-pigmented colonies was isolated and was identified as a strain of Staphylococcus epidermidis using biochemical and phylogenetic tools. S. epidermidis RM1 was shown to possess both potent BSH and N-acyl homoserine lactone (AHL) cleavage activity. Genetic basis of this dual-enzyme activity was explored by means of specific primers designed using S. epidermidis ATCC 12228 genome as template. It was observed that a single enzyme was not responsible for both the activity. Two different genetic elements corresponding to each of the enzymatic activity were successfully amplified from the genomic DNA of the isolate.</p>10aAHL acylase10aBile salt hydrolase10aCV02610aQuorum quenching10aStaphylococcus epidermidis1 aMukherji, Ruchira1 aPrabhune, Asmita  uhttps://library.ncl.res.in/content/possible-correlation-between-bile-salt-hydrolysis-and-ahl-deamidation-staphylococcus-002161nas 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