Ontology highlight
ABSTRACT:
SUBMITTER: Trenti F
PROVIDER: S-EPMC7944568 | biostudies-literature | 2021 Mar
REPOSITORIES: biostudies-literature
Trenti Francesco F Yamamoto Kotaro K Hong Benke B Paetz Christian C Nakamura Yoko Y O'Connor Sarah E SE
Organic letters 20210224 5
The enzymatic basis for quinine <b>1</b> 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 <b>2</b> from strictosidine aglycone <b>3</b>. Additionally, the discovery of an <i>O</i>-methyltransferase specific for 6'-hydroxycinchoninone <b>4</b> suggested th ...[more]