KOPRI Repository

Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum

Cited 17 time in wos
Cited 16 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorT. Doohun Kim-
dc.contributor.authorPark, Hyun-
dc.contributor.authorSunghwan Kim-
dc.contributor.authorShin, Seung Chul-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorBum Han Ryu-
dc.contributor.authorWanki Yoo-
dc.contributor.authorBoo-Young Kim-
dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorSena Kwon-
dc.description.abstractA novel microbial esterase, EaEST, from a psychrophilic bacterium Exiguobacterium antarcticum B7, was identified and characterized. To our knowledge, this is the first report describing structural analysis and biochemical characterization of an esterase isolated from the genus Exiguobacterium. Crystal structure of EaEST, determined at a resolution of 1.9 A, showed that the enzyme has a canonical α/β hydrolase fold with an α-helical cap domain and a catalytic triad consisting of Ser96, Asp220, and His248. Interestingly, the active site of the structure of EaEST is occupied by a peracetate molecule, which is the product of perhydrolysis of acetate. This result suggests that EaEST may have perhydrolase activity. The activity assay showed that EaEST has significant perhydrolase and esterase activity with respect to short-chain p-nitrophenyl esters (≤C8), naphthyl derivatives, phenyl acetate, and glyceryl tributyrate. However, the S96A single mutant had low esterase and perhydrolase activity. Moreover, the L27A mutant showed low levels of protein expression and solubility as well as preference for different substrates. On conducting an enantioselectivity analysis using R- and S-methyl-3-hydroxy-2-methylpropionate, a preference for R-enantiomers was observed. Surprisingly, immobilized EaEST was found to not only retain 200% of its initial activity after incubation for 1 h at 80°C, but also retained more than 60% of its initial activity after 20 cycles of reutilization. This research will serve as basis for future engineering of this esterase for biotechnological and industrial applications.-
dc.subjectScience & Technology - Other Topics-
dc.titleCrystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum-
dc.title.alternative극지 호냉성 박테리아 (Exiguobacterium antarcticum) 유래 EaEST 효소의 구조-기능연구-
dc.identifier.bibliographicCitationLee, Chang Woo, et al. 2017. "Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum". <em>PLOS ONE</em>, 12(1): 169540-0.-
dc.citation.titlePLOS ONE-
dc.description.jcrRateJCR 2015:17.46-
dc.subject.keywordExiguobacterium antarcticum-
dc.subject.keywordX-ray crystallography-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun
2017-2018, Polar Genomics 101 Project: Genome analysis of polar organisms and establishment of application platform (17-18) / Park, Hyun
2016-2017, Developing analytical techniques for investigating changing permafrost ecosystems in the Arctic (16-17) / Kim, Mincheol
Files in This Item
General Conditions
      ROMEO Green
    Can archive pre-print and post-print or publisher's version/PDF
      ROMEO Blue
    Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
      ROMEO Yellow
    Can archive pre-print (ie pre-refereeing)
      ROMEO White
    Archiving not formally supported

    Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.