00607nas a2200181   4500008004100000022001400041245007300055210006900128260000800197300000900205490000700214653001400221653002400235653001800259100001900277700002600296856010300322       2014                        eng d  a2053-273300aAllostery mapping in enterococcus faecalis Bile Salt Hydrolase (BSH)0 aAllostery mapping in enterococcus faecalis Bile Salt Hydrolase B  cMAY  aC2740 v7010aAllostery10aBile salt hydrolase10aMD Simulation1 aYadav, Yashpal1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/allostery-mapping-enterococcus-faecalis-bile-salt-hydrolase-bsh02696nas a2200301   4500008004100000022001400041245016000055210006900215260010600284300000900390490000700399520155800406653001301964653001801977653002801995653002902023653001502052653002402067100002402091700002002115700001902135700002002154700002202174700002302196700002602219700002002245856012902265       2016                        eng d  a0965-174800aCharacterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose0 aCharacterization of two coleopteran alphaamylases and molecular   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUL  a1-110 v743 a<p>Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran alpha-amylases viz. Callosobruchus chinensis alpha-amylase (CcAmy) and Tribolium castaneum alpha-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous alpha-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran alpha-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin. HPLC analysis detected common amylolytic products like maltose and maltotriose while glucose and malto-tetrose were unique in CcAmy and TcAmy catalyzed reactions respectively. At very low concentrations, wheat alpha-amylase inhibitor was found to be superior over the acarbose as far as complete inhibition of amylolytic activities of CcAmy and TcAmy was concerned. Mechanism underlying differential amylolytic reaction inhibition by acarbose was discussed. (C) 2016 Elsevier Ltd. All rights reserved.</p>10aAcarbose10aalpha-amylase10aalpha-amylase inhibitor10aCallosobruchus chinensis10aColeoptera10aTribolium castaneum1 aChannale, Sonal, M.1 aBhide, Amey, J.1 aYadav, Yashpal1 aKashyap, Garima1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/characterization-two-coleopteran-alpha-amylases-and-molecular-insights-their-differential02629nas a2200229   4500008004100000245012800041210006900169260000800238300001200246490001000258520179900268100002002067700002402087700001902111700002602130700002202156700002302178700002102201700002602222700002002248856013102268       2017                        eng d00aGenomic and functional characterization of coleopteran insect-specific alpha-amylase inhibitor gene from amaranthus species0 aGenomic and functional characterization of coleopteran insectspe  cJUN  a319-3320 v 94  3 aThe smallest 32 amino acid alpha-amylase inhibitor from Amaranthus hypochondriacus (AAI) is reported. The complete gene of pre-protein (AhAI) encoding a 26 amino acid (aa) signal peptide followed by the 43 aa region and the previously identified 32 aa peptide was cloned successfully. Three cysteine residues and one disulfide bond conserved within known alpha-amylase inhibitors were present in AhAI. Identical genomic and open reading frame was found to be present in close relatives of A. hypochondriacus namely Amaranthus paniculatus, Achyranthes aspera and Celosia argentea. Interestingly, the 3'UTR of AhAI varied in these species. The highest expression of AhAI was observed in A. hypochondriacus inflorescence; however, it was not detected in the seed. We hypothesized that the inhibitor expressed in leaves and inflorescence might be transported to the seeds. Sub-cellular localization studies clearly indicated the involvement of AhAI signal peptide in extracellular secretion. Full length rAhAI showed differential inhibition against alpha-amylases from human, insects, fungi and bacteria. Particularly, alpha-amylases from Helicoverpa armigera (Lepidoptera) were not inhibited by AhAI while Tribolium castaneum and Callosobruchus chinensis (Coleoptera) alpha-amylases were completely inhibited. Molecular docking of AhAI revealed tighter interactions with active site residues of T. castaneum alpha-amylase compared to C. chinensis alpha-amylase, which could be the rationale behind the disparity in their IC50. Normal growth, development and adult emergence of C. chinensis were hampered after feeding on rAhAI. Altogether, the ability of AhAI to affect the growth of C. chinensis demonstrated its potential as an efficient bio-control agent, especially against stored grain pests.1 aBhide, Amey, J.1 aChannale, Sonal, M.1 aYadav, Yashpal1 aBhattacharjee, Kabita1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aGupta, Vidya, S.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/genomic-and-functional-characterization-coleopteran-insect-specific-alpha-amylase-inhibitor02161nas 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