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Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin
Rhodoxanthin is a vibrant red carotenoid found across the plant kingdom and in certain birds and fish. It is a member of the atypical retro class of carotenoids, which contain an additional double bond and a concerted shift of the conjugated double bonds relative to the more widely occurring caroten...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7176425/ https://www.ncbi.nlm.nih.gov/pubmed/32426461 http://dx.doi.org/10.1126/sciadv.aay9226 |
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author | Royer, John Shanklin, John Balch-Kenney, Nathalie Mayorga, Maria Houston, Peter de Jong, René M. McMahon, Jenna Laprade, Lisa Blomquist, Paul Berry, Timothy Cai, Yuanheng LoBuglio, Katherine Trueheart, Joshua Chevreux, Bastien |
author_facet | Royer, John Shanklin, John Balch-Kenney, Nathalie Mayorga, Maria Houston, Peter de Jong, René M. McMahon, Jenna Laprade, Lisa Blomquist, Paul Berry, Timothy Cai, Yuanheng LoBuglio, Katherine Trueheart, Joshua Chevreux, Bastien |
author_sort | Royer, John |
collection | PubMed |
description | Rhodoxanthin is a vibrant red carotenoid found across the plant kingdom and in certain birds and fish. It is a member of the atypical retro class of carotenoids, which contain an additional double bond and a concerted shift of the conjugated double bonds relative to the more widely occurring carotenoid pigments, and whose biosynthetic origins have long remained elusive. Here, we identify LHRS (Lonicera hydroxylase rhodoxanthin synthase), a variant β-carotene hydroxylase (BCH)–type integral membrane diiron enzyme that mediates the conversion of β-carotene into rhodoxanthin. We identify residues that are critical to rhodoxanthin formation by LHRS. Substitution of only three residues converts a typical BCH into a multifunctional enzyme that mediates a multistep pathway from β-carotene to rhodoxanthin via a series of distinct oxidation steps in which the product of each step becomes the substrate for the next catalytic cycle. We propose a biosynthetic pathway from β-carotene to rhodoxanthin. |
format | Online Article Text |
id | pubmed-7176425 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-71764252020-05-18 Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin Royer, John Shanklin, John Balch-Kenney, Nathalie Mayorga, Maria Houston, Peter de Jong, René M. McMahon, Jenna Laprade, Lisa Blomquist, Paul Berry, Timothy Cai, Yuanheng LoBuglio, Katherine Trueheart, Joshua Chevreux, Bastien Sci Adv Research Articles Rhodoxanthin is a vibrant red carotenoid found across the plant kingdom and in certain birds and fish. It is a member of the atypical retro class of carotenoids, which contain an additional double bond and a concerted shift of the conjugated double bonds relative to the more widely occurring carotenoid pigments, and whose biosynthetic origins have long remained elusive. Here, we identify LHRS (Lonicera hydroxylase rhodoxanthin synthase), a variant β-carotene hydroxylase (BCH)–type integral membrane diiron enzyme that mediates the conversion of β-carotene into rhodoxanthin. We identify residues that are critical to rhodoxanthin formation by LHRS. Substitution of only three residues converts a typical BCH into a multifunctional enzyme that mediates a multistep pathway from β-carotene to rhodoxanthin via a series of distinct oxidation steps in which the product of each step becomes the substrate for the next catalytic cycle. We propose a biosynthetic pathway from β-carotene to rhodoxanthin. American Association for the Advancement of Science 2020-04-22 /pmc/articles/PMC7176425/ /pubmed/32426461 http://dx.doi.org/10.1126/sciadv.aay9226 Text en Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Royer, John Shanklin, John Balch-Kenney, Nathalie Mayorga, Maria Houston, Peter de Jong, René M. McMahon, Jenna Laprade, Lisa Blomquist, Paul Berry, Timothy Cai, Yuanheng LoBuglio, Katherine Trueheart, Joshua Chevreux, Bastien Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title | Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title_full | Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title_fullStr | Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title_full_unstemmed | Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title_short | Rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
title_sort | rhodoxanthin synthase from honeysuckle; a membrane diiron enzyme catalyzes the multistep conversation of β-carotene to rhodoxanthin |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7176425/ https://www.ncbi.nlm.nih.gov/pubmed/32426461 http://dx.doi.org/10.1126/sciadv.aay9226 |
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