Journal
ORGANIC LETTERS
Volume 23, Issue 5, Pages 1793-1797Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.1c00206
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Funding
- European Research Council [788301]
- Horizon 2020 (MIAMI)
- Alexander von Humboldt Foundation
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Transcriptomic data led to the discovery of three enzymes involved in the biosynthesis of quinine, with a medium-chain alcohol dehydrogenase and an esterase being key in producing the biosynthetic intermediate dihydrocorynantheal from strictosidine aglycone. Additionally, the specific O-methyltransferase for 6'-hydroxycinchoninone suggested the final step order to be cinchoninone hydroxylation, methylation, and keto-reduction.
The enzymatic basis for quinine 1 biosynthesis was investigated. Transcriptomic data from the producing plant led to the discovery of three enzymes involved in the early and late steps of the pathway. A medium-chain alcohol dehydrogenase (CpDCS) and an esterase (CpDCE) yielded the biosynthetic intermediate dihydrocorynantheal 2 from strictosidine aglycone 3. Additionally, the discovery of an O-methyltransferase specific for 6'-hydroxycinchoninone 4 suggested the final step order to be cinchoninone 16/17 hydroxylation, methylation, and keto-reduction.
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