Fig. 7: MIA structure diversification is primarily driven by the activities of physically clustered CAD-like reductases, BBE-like oxidases, and non-clustered CYPs. | Nature Communications

Fig. 7: MIA structure diversification is primarily driven by the activities of physically clustered CAD-like reductases, BBE-like oxidases, and non-clustered CYPs.

From: Ancient gene clusters govern the initiation of monoterpenoid indole alkaloid biosynthesis and C3 stereochemistry inversion

Fig. 7: MIA structure diversification is primarily driven by the activities of physically clustered CAD-like reductases, BBE-like oxidases, and non-clustered CYPs.

The biosynthetic framework of major MIA subclasses is depicted with representative intermediate structures. Arrows indicate the biosynthetic direction, with corresponding enzyme names and illustrations of the gene clusters to which they belong, positioned adjacent to each transformation step. This schematic highlights the central role of gene clusters (STR, GS, reserpine, Redox1/DPAS, and HYS/THAS4 clusters) in directing the biosynthesis of strictosidine and stepwise conversion of strictosidine aglycone into diverse strychnos, akuammiline, aspidosperma, iboga, spirooxindole, and other scaffolds. SGD strictosidine β-glucosidase, GS geissoschizine synthase, THAS tetrahydroalstonine synthase, HYS heteroyohimbine synthase, YOS yohimban synthase, DCS demethyldihydrocorynantheine/demethylcorynantheidine synthase, SBE sarpagan bridge enzyme, RHS rhazimal synthase, GO geissoschizine oxidase, SAT stemmadinine O-acetyltransferase, ASO O-acetylstemmadenine oxidase, DPAS dihydroprecondylocarpine synthase, HYC3O heteroyohimbine/yohimbine/corynanthe C3-oxidase, HYC3R heteroyohimbine/yohimbine/corynanthe C3-reductase.

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