Molecular Characterization of a Geranyl Diphosphate-Specific Prenyltransferase Catalyzing Stilbenoid Prenylation from Morus alba
Zhuoheng Zhonga, Wei Zhua, Shengzhi Liua, Qijie Guana, Xi Chena, Wei Huanga, Tantan Wanga, Bingxian Yanga✉, Jingkui Tiana b✉
- aCollege of Biomedical Engineering & Instrument Science, Zhejiang University, Hangzhou, PR China
- bZhejiang-Malaysia Joint Research Center for Traditional Medicine, Zhejiang University, Hangzhou, PR China
- ✉Corresponding author
Papers open inside SciRah from the original publisher or repository; SciRah never hosts them.
Abstract
Pharmaceutically active compounds from medical plants are attractive as a major source for new drug development. Prenylated stilbenoids with increased lipophilicity are valuable secondary metabolites which possess a wide range of biological activities. So far, many prenylated stilbenoids have been isolated from Morus alba but the enzyme responsible for the crucial prenyl modification remains unknown. In the present study, a stilbenoid-specific prenyltransferase (PT), termed Morus alba oxyresveratrol geranyltransferase (MaOGT), was identified and functionally characterized in vitro. MaOGT recognized oxyresveratrol and geranyl diphosphate (GPP) as natural substrates, and catalyzed oxyresveratrol prenylation. Our results indicated that MaOGT shared common features with other aromatic PTs, e.g. multiple transmembrane regions, conserved functional domains and targeting to plant plastids. This distinct PT represents the first stilbenoid-specific PT accepting GPP as a natural prenyl donor, and could help identify additional functionally varied PTs in moraceous plants. Furthermore, MaOGT might be applied for high-efficiency and large-scale prenylation of oxyresveratrol to produce bioactive compounds for potential therapeutic applications.
TL;DRThis distinct PT, termed Morus alba oxyresveratrol geranyltransferase (MaOGT), was identified and functionally characterized in vitro and represents the first stilbenoid-specific PT accepting GPP as a natural prenyl donor, and could help identify additional functionally varied PTs in moraceous plants. (Semantic Scholar)

