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Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

journal contribution
posted on 2023-05-18, 11:05 authored by Zhang, Y, van Dijk, ADJ, Scaffidi, A, Flematti, GR, Hofmann, M, Charnikhova, T, Verstappen, F, Hepworth, J, van der Krol, S, Leyser, O, Steven SmithSteven Smith, Zwanenburg, B, Al-Babili, S, Ruyter-Spira, C, Bouwmeester, HJ
Strigolactones (SLs) are a class of phytohormones and rhizosphere signaling compounds with high structural diversity. Three enzymes, carotenoid isomerase DWARF27 and carotenoid cleavage dioxygenases CCD7 and CCD8, were previously shown to convert all-trans-β-carotene to carlactone (CL), the SL precursor. However, how CL is metabolized to SLs has remained elusive. Here, by reconstituting the SL biosynthetic pathway in Nicotiana benthamiana, we show that a rice homolog of Arabidopsis MORE AXILLARY GROWTH 1 (MAX1), encodes a cytochrome P450 CYP711 subfamily member that acts as a CL oxidase to stereoselectively convert CL into ent-2’-epi-5-deoxystrigol (B-C lactone ring formation), the presumed precursor of rice SLs. A protein encoded by a second rice MAX1 homolog then catalyzes the conversion of ent-2’-epi-5-deoxystrigol to orobanchol. We therefore report that two members of CYP711 enzymes can catalyze two distinct steps in SL biosynthesis, identifying the first enzymes involved in B-C ring closure and a subsequent structural diversification step of SLs.


Publication title

Nature Chemical Biology










School of Natural Sciences


Nature Publishing Group

Place of publication

United Kingdom

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Copyright 2014 Nature America

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Expanding knowledge in the biological sciences

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