AI Article Synopsis
- Tetrandrine is a potent small molecule effective against the Ebola virus, derived from the plant Stephania tetrandra.
- The study focuses on a key enzyme, S-adenosyl-L-methionine: (S)-norcoclaurine-6-O-methyltransferase (6OMT), which plays a crucial role in the biosynthesis of tetrandrine.
- Researchers identified four 6OMT-like genes and demonstrated that one of them, St6OMT1, efficiently converts (S)-norcoclaurine to (S)-coclaurine, aiding future studies in synthetic biology for alkaloid production.
Article Abstract
Tetrandrine is the most effective small molecule that has been found to inhibit the Ebola virus. It is a typical bisbenzylisoquinoline alkaloid and is the main active ingredient in Stephania tetrandra. Metabolic engineering and synthetic biology are potential methods for efficient and rapid acquisition of tetrandrine. S-adenosyl-L-methionine: (S)-norcoclaurine-6-O-methyltransferase (6OMT) is a rate-limiting step involved in the biosynthesis of tetrandrine. In this study, we identify S-adenosyl-L-methionine: (S)-norcoclaurine-6-O-methyltransferase from S. tetrandra, which catalyzes the conversion of (S)-norcoclaurine to (S)-coclaurine. Four 6OMT-like genes were cloned from S. tetrandra. An in vitro enzyme assay showed that St6OMT1 could catalyze the conversion of (S)-norcoclaurine to produce (S)-coclaurine. St6OMT2 can catalyze the production of very few (S)-coclaurine molecules, accompanied by more by-products with m/z 300, compared to St6OMT1. The newly discovered 6OMTs will provide an optional genetic component for benzylisoquinoline alkaloid (BIA) synthetic biology research. This work will lay the foundation for the analysis of the biosynthetic pathway of tetrandrine in S. tetrandra.
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| http://dx.doi.org/10.1016/j.jplph.2020.153181 | DOI Listing |
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