Unleashing the Synthetic Power of Plant Oxygenases: From Mechanism to Application

• Main Authors: Mitchell, Andrew J. (Author), Weng, Jing-Ke (Author)
• Other Authors: Whitehead Institute for Biomedical Research (Contributor), Massachusetts Institute of Technology. Department of Biology (Contributor)
• Format: Article
• Language: English
• Published: American Society of Plant Biologists (ASPB), 2020-07-20T20:23:28Z.
• Subjects: Article
• Online Access: Get fulltext

 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.