Unleashing the Synthetic Power of Plant Oxygenases: From Mechanism to Application
Name
Unleashing the synthetic power of plant oxygenases from mechanism to application_proof.pdf
Description
Accepted version
Size
3.15 MB
Format
Adobe PDF
Checksum (MD5)
d040c5b5c1a374671e8afb1d6a3eefa4
Author(s)
Mitchell, Andrew J.
Weng, Jing-Ke
Date Issued
January 2019
Journal
Plant Physiology
Publisher
American Society of Plant Biologists (ASPB)
Citation
Mitchell, Andrew J. and Jing-Ke Weng. "Unleashing the Synthetic Power of Plant Oxygenases: From Mechanism to Application." Plant Physiology 179, 3 (January 2019) © 2019 American Society of Plant Biologists
Version
Author's final manuscript
Abstract
Plant-specialized metabolites account for arguably the largest and most diverse pool of natural products accessible to humans. Conferring the plants’ selective traits, such as UV defense, pathogen resistance, and enhanced nutrient uptake, these chemicals are crucial to a species’ viability. During biosynthesis of these compounds, a vast array of specialized enzymes catalyze diverse chemical modifications, with oxidation being one of the most predominant (Smanski et al., 2016; Dong et al., 2018). Considering these observations, it is not surprising that within plant genomes, two families of oxygenases are the most abundant: the cytochrome P450 monooxygenases (P450s) and the iron/2-oxoglutarate-dependent oxygenases (Fe/2OGs). These and other oxygenases represent the synthetic workhorses of plant-specialized metabolism and also play key roles in primary metabolism, cellular regulation, and fitness. Furthermore, the challenging and selective chemistry they catalyze cannot currently be matched by synthetic chemists. Since many plant natural products serve as valuable pharmaceuticals and commodity chemicals, plant oxygenases represent a promising toolset for synthetic biologists to manipulate plant traits or develop biocatalysts (Harvey et al., 2015). Here, we review families of plant oxygenases and their chemistry and suggest potential applications.
MIT Department
Whitehead Institute for Biomedical Research
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1104/pp.18.01223
