KOPRI Repository

Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.

Cited 0 time in scopus
Metadata Downloads
Title
Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.
Other Titles
남극 좀새풀유래 Chalcone isomerase 효소의 삼차구조 와 생화학적 특성연구
Authors
Park, Sun-Ha
Lee, Jun Hyuck
Lee, Jong Eun
Park, Hyun
Lee, Hyoungseok
Cho, Sung-Mi
Lee, Chang Woo
Subject
Science & Technology - Other Topics
Keywords
Chalcone isomerase; Crystal structure; Deschampsia antarctica; X-ray crystallography
Issue Date
2018
Citation
Park, Sun-Ha, et al. 2018. "Crystal structure and enzymatic properties of chalcone isomerase from the Antarctic vascular plant Deschampsia antarctica Desv.". PLOS ONE, 13: 1-17.
Abstract
Chalcone isomerase (CHI) is an important enzyme for flavonoid biosynthesis that catalyzes the intramolecular cyclization of chalcones into (S)-flavanones. CHIs have been classified into two types based on their substrate specificity. Type I CHIs use naringenin chalcone as a substrate and are found in most of plants besides legumes, whereas type II CHIs in leguminous plants can also utilize isoliquiritigenin. In this study, we found that the CHI from the Antarctic plant Deschampsia antarctica (DaCHI1) is of type I based on sequence homology but can use type II CHI substrates. To clarify the enzymatic mechanism of DaCHI1 at the molecular level, the crystal structures of unliganded DaCHI1 and isoliquiritigenin-bound DaCHI1 were determined at 2.7 and 2.1 A resolutions, respectively. The structures revealed that isoliquiritigenin binds to the active site of DaCHI1 and induces conformational changes. Additionally, the activity assay showed that while DaCHI1 exhibits substrate preference for naringenin chalcone, it can also utilize isoliquiritigenin although the catalytic activity was relatively low. Based on these results, we propose that DaCHI1 uses various substrates to produce antioxidant flavonoids as an adaptation to oxidative stresses associated with harsh environmental conditions.
URI
http://repository.kopri.re.kr/handle/201206/6470
DOI
http://dx.doi.org/10.1371/journal.pone.0192415
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

    qrcode

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

    Browse