Asset Details
Do you wish to reserve the book?
A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
Do you wish to request the book?
A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
A conserved strategy of chalcone isomerase-like protein to rectify promiscuous chalcone synthase specificity
2020
Overview
Land plants produce diverse flavonoids for growth, survival, and reproduction. Chalcone synthase is the first committed enzyme of the flavonoid biosynthetic pathway and catalyzes the production of 2′,4,4′,6′-tetrahydroxychalcone (THC). However, it also produces other polyketides, including
p
-coumaroyltriacetic acid lactone (CTAL), because of the derailment of the chalcone-producing pathway. This promiscuity of CHS catalysis adversely affects the efficiency of flavonoid biosynthesis, although it is also believed to have led to the evolution of stilbene synthase and
p
-coumaroyltriacetic acid synthase. In this study, we establish that chalcone isomerase-like proteins (CHILs), which are encoded by genes that are ubiquitous in land plant genomes, bind to CHS to enhance THC production and decrease CTAL formation, thereby rectifying the promiscuous CHS catalysis. This CHIL function has been confirmed in diverse land plant species, and represents a conserved strategy facilitating the efficient influx of substrates from the phenylpropanoid pathway to the flavonoid pathway.
Chalcone synthase is the first committed enzyme in the plant flavonoid biosynthesis pathway, yet shows low product specificity in vitro. Here Waki et al. show that chalcone isomerase-like proteins bind to and reduce the catalytic promiscuity of chalcone synthase, ensuring efficient flavonoid production in planta.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 38
/ 38/35
/ 631/181
/ 631/449
/ 631/45
/ 82/111
/ 82/29
/ 82/58
/ Acyltransferases - metabolism
/ Biosynthetic Pathways - genetics
/ Enzymes
/ Genetic Complementation Test
/ Genomes
/ Humanities and Social Sciences
/ Intramolecular Lyases - genetics
/ Intramolecular Lyases - metabolism
/ Kinetics
/ Plants, Genetically Modified
/ Proteins
/ Science
/ Stilbene
