Authors of the article assert that isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. They emphasize that understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids.
The College of Science provides students with the high-demand skills and knowledge to succeed as researchers and professionals. The College includes four departments: Biology, Chemistry, Math, and Physics, and is also home to a number of interdisciplinary programs, centers, institutes, intercollegiate programs, labs, and services.
Authors of the article assert that isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. They emphasize that understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids.
Physical Description
10 p.
Notes
Abstract: Isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. Their biosynthesis is initiated by two enzymes with unusual catalytic activities; 2-hydroxyisoflavanone synthase (2-HIS), a membrane-bound cytochrome P450 catalyzing a coupled aryl-ring migration and hydroxylation, and 2-hydroxyisoflavanone dehydratase (2-HID), a member of a large carboxylesterase family that paradoxically catalyzes dehydration of 2-hydroxyisoflavanones to isoflavone. Here we report the crystal structures of 2-HIS from Medicago truncatula and 2-HID from Pueraria lobata. The 2-HIS structure reveals a unique cytochrome P450 conformation and heme and substrate binding mode that facilitate the coupled aryl-ring migration and hydroxylation reactions. The 2-HID structure reveals the active site architecture and putative catalytic residues for the dual dehydratase and carboxylesterase activities. Mutagenesis studies revealed key residues involved in substrate binding and specificity. Understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids.
This article is part of the following collection of related materials.
UNT Scholarly Works
Materials from the UNT community's research, creative, and scholarly activities and UNT's Open Access Repository. Access to some items in this collection may be restricted.
Wang, Xiaoqiang; Pan, Haiyun; Sagurthi, Someswar; Paris, Vincent; Zhuo, Chunliu & Dixon, R. A.The protein conformational basis of isoflavone biosynthesis,
article,
November 15, 2022;
(https://digital.library.unt.edu/ark:/67531/metadc2179468/:
accessed June 28, 2024),
University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu;
crediting UNT College of Science.