Structural highlights
Function
CHS1_SOYBN The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Publication Abstract from PubMed
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. This article is protected by copyright. All rights reserved.
Crystal structure of chalcone synthase, a key enzyme for isoflavonoid biosynthesis in soybean.,Imaizumi R, Mameda R, Takeshita K, Kubo H, Sakai N, Nakata S, Takahashi S, Kataoka K, Yamamoto M, Nakayama T, Yamashita S, Waki T Proteins. 2020 Jul 29. doi: 10.1002/prot.25988. PMID:32725893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Imaizumi R, Mameda R, Takeshita K, Kubo H, Sakai N, Nakata S, Takahashi S, Kataoka K, Yamamoto M, Nakayama T, Yamashita S, Waki T. Crystal structure of chalcone synthase, a key enzyme for isoflavonoid biosynthesis in soybean. Proteins. 2020 Jul 29. PMID:32725893 doi:10.1002/prot.25988
