Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 3, Pages 1498-1500Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja211524d
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Funding
- Fonds der Chemischen Industrie (Frankfurt/Main, Germany)
- German Science Foundation (DFG, Bad Godesberg, Germany)
- National Natural Science Foundation of China [20802066]
- Zhejiang Qianjiang talent plan [2011R10023]
- K. P. Chao High-Tech Foundation of Zhejiang University
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The Pictet-Spenglerase strictosidine synthase (STR1) has been recognized as a key enzyme in the biosynthesis of some 2000 indole alkaloids in plants, some with high therapeutic value. In this study, a novel function of STR1 has been detected which allows for the first time a simple enzymatic synthesis of the strictosidine analogue 3 harboring the piperazino[1,2-a]indole (PI) scaffold and to switch from the common tryptoline (hydrogenated carboline) to the rare PI skeleton. Insight into the reaction is provided by X-ray crystal analysis and modeling of STR1 ligand complexes. STR1 presently provides exclusively access to 3 and can act as a source to generate by chemoenzymatic approaches libraries of this novel class of alkaloids which may have new biological activities. Synthetic or natural monoterpenoid alkaloids with the PI core have not been reported before.
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