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Crystal structure of chalcone synthase, a key enzyme for isoflavonoid biosynthesis in soybean
  • +8
  • Riki Imaizumi,
  • Ryo Mameda,
  • Kohei Takeshita,
  • Toshiyuki Waki,
  • Hiroki Kubo,
  • Shun Nakata,
  • Seiji Takahashi,
  • Kunishige Kataoka,
  • Masaki Yamamoto,
  • Satoshi Yamashita,
  • Toru Nakayama
Riki Imaizumi
Kanazawa University
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Ryo Mameda
Tohoku University
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Kohei Takeshita
SPring-8
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Toshiyuki Waki
Tohoku University
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Hiroki Kubo
Kanazawa University
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Shun Nakata
Kanazawa University
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Seiji Takahashi
Tohoku University
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Kunishige Kataoka
Kanazawa University
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Masaki Yamamoto
SPring-8
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Satoshi Yamashita
Kanazawa University
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Toru Nakayama
Tohoku University
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Peer review status:ACCEPTED

15 Apr 2020Submitted to PROTEINS: Structure, Function, and Bioinformatics
16 Apr 2020Submission Checks Completed
16 Apr 2020Assigned to Editor
18 May 2020Reviewer(s) Assigned
08 Jun 2020Review(s) Completed, Editorial Evaluation Pending
14 Jun 2020Editorial Decision: Revise Minor
10 Jul 20201st Revision Received
13 Jul 2020Submission Checks Completed
13 Jul 2020Assigned to Editor
16 Jul 2020Review(s) Completed, Editorial Evaluation Pending
26 Jul 2020Editorial Decision: Accept

Abstract

Isoflavonoid is one of the groups of flavonoids that play pivotal roles in the survival of land plants. Chalcone synthase (CHS), the first enzyme of the isoflavonoid biosynthetic pathway, catalyzes the formation of a common isoflavonoid precursor. We have previously reported that an isozyme of soybean CHS (termed GmCHS1) is a key component of the isoflavonoid metabolon, a protein complex to enhance efficiency of isoflavonoid production. Here, we determined the crystal structure of GmCHS1 as a first step of understanding the metabolon structure, as well as to better understand the catalytic mechanism of GmCHS1.