ArticleMicrobial cell factories2025
Multi-layered engineering of Aspergillus terreus enhances biosynthesis of the plant-derived fungicide physcion.
Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundEmodin and its derivatives are important bioactive anthraquinones from rhubarb, with diverse pharmacological activities. Physcion, an O-methylated derivative of emodin, is a promising plant-derived fungicide and pharmaceutical lead. However, plant extraction yields are low and land-intensive, while microbial production is hampered by inefficient conversion and byproduct accumulation.
resultsHere, we identify a cytochrome P450 enzyme (CYP-H6231) that, with its dedicated redox partner cytochrome P450 reductase (CPR-H10273), converts emodin to ω-hydroxyemodin in Aspergillus terreus. Deletion of CYP-H6231 increased physcion titer by 1.8-fold and significantly improved product purity. Further engineering, via 3-O-methyltransferase overexpression, SAM pathway enhancement, and enzyme fusion, yielded only modest improvement (up to 37%), likely due to compromised strain robustness from the loss of CYP-H6231 mediated detoxification. Structural modeling and mutagenesis of CYP-H6231 revealed key residues for substrate recognition and catalysis.
conclusionsThis study reveals a detoxification bottleneck in anthraquinone biosynthesis and establishes two improved A. terreus platforms for scalable production of physcion and emodin, respectively, highlighting trade-offs between pathway efficiency and cellular fitness.
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