Asset Details
Do you wish to reserve the book?
Functional characterization of CYP96T1-like cytochrome P450 from Lycoris aurea catalyzing para-para′ and para-ortho′ oxidative coupling in Amaryllidaceae alkaloids biosynthesis
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?
Functional characterization of CYP96T1-like cytochrome P450 from Lycoris aurea catalyzing para-para′ and para-ortho′ oxidative coupling in Amaryllidaceae alkaloids biosynthesis
Do you wish to request the book?
Functional characterization of CYP96T1-like cytochrome P450 from Lycoris aurea catalyzing para-para′ and para-ortho′ oxidative coupling in Amaryllidaceae alkaloids biosynthesis
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
Functional characterization of CYP96T1-like cytochrome P450 from Lycoris aurea catalyzing para-para′ and para-ortho′ oxidative coupling in Amaryllidaceae alkaloids biosynthesis
2024
Overview
Amaryllidaceae alkaloids (AAs) are complex plant secondary metabolites possessing a wide range of biological activities. 4′-O-methylnorbelladine (4OMN) is the branchpoint intermediate for the entire AAs, and was the last common intermediate before AA pathway branches diverge. The cyclization of 4OMN by C-C oxidative coupling, which can afford
para-para
′,
ortho-para
′, and
para-ortho
′ scaffold, was catalyzed by cytochrome P450 96T (CYP96T) family enzymes. To clarify the mechanisms involved in this controversial step, four CYP96T homologs (LauCYP96T1, LauCYP96T1-like-1, LauCYP96T1-like-2 and LauCYP96T1-like-3) were cloned from the full-length transcriptome of
Lycoris aurea
. All the four LauCYP96T are localized to endoplasmic reticulum. Functional analysis reveals that LauCYP96T1 and LauCYP96T1-like proteins display inverted regioselectivity for oxidative coupling of 4OMN, in which LauCYP96T1 and LauCYP96T1-like-2 dominantly afford
para-para
′ scaffold, and LauCYP96T1-like-1 and LauCYP96T1-like-3 are responsible for
para-ortho
′ scaffold formation. Using molecular homology modeling and docking studies, we predicted models for the binding of 4OMN to LauCYP96T, and identified two amino acid residues that might be responsible for the dominant changes in generated products of
para-ortho
′ and
para-para
′ oxidative coupling. Our results highlight the functional diversity and promiscuity of LauCYP96T enzymes and might provide valuable information for Amaryllidaceae alkaloid production.
We currently cannot retrieve any items related to this title. Kindly check back at a later time.