Discovering a uniform functional trade-off of the CBC-type 2,3-oxidosqualene cyclases and deciphering its chemical logic.

Many functionally promiscuous plant 2,3-oxidosqualene cyclases (OSCs) have been found, but complete functional reshaping is rarely reported. In this study, we have identified two new plant OSCs: a unique protostadienol synthase (PDS) and a common cycloartenol synthase (CAS) from (Sam.) Juzep.

Oxidosqualene Cyclases Involved in the Biosynthesis of Diverse Triterpenes in .

is an important economic plant that is rich in lipophilic triterpenols with pharmacological activities including antiallergic, anti-inflammatory, and anticancer activities. However, the key enzymes related to triterpene biosynthesis have seldom been studied in . Oxidosqualene cyclases (OSCs) are the rate-limiting enzymes related to triterpene biosynthesis.

Exploring the catalytic function and active sites of a novel -glycosyltransferase from .

is an immensely popular medicinal herb in China, which contains an abundant of mangiferin. As an important bioactive xanthone -glycoside, mangiferin possesses a variety of pharmacological activities and is derived from the cyclization reaction of a benzophenone -glycoside (maclurin). Biosynthetically, -glycosyltransferases are critical for the formation of benzophenone -glycosides.