Structural highlights
Function
[STSY_RAUSE] Catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis.
Publication Abstract from PubMed
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.
Scaffold Tailoring by a Newly Detected Pictet-Spenglerase Activity of Strictosidine Synthase: From the Common Tryptoline Skeleton to the Rare Piperazino-indole Framework.,Wu F, Zhu H, Sun L, Rajendran C, Wang M, Ren X, Panjikar S, Cherkasov A, Zou H, Stockigt J J Am Chem Soc. 2012 Jan 25;134(3):1498-500. Epub 2012 Jan 9. PMID:22229634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wu F, Zhu H, Sun L, Rajendran C, Wang M, Ren X, Panjikar S, Cherkasov A, Zou H, Stockigt J. Scaffold Tailoring by a Newly Detected Pictet-Spenglerase Activity of Strictosidine Synthase: From the Common Tryptoline Skeleton to the Rare Piperazino-indole Framework. J Am Chem Soc. 2012 Jan 25;134(3):1498-500. Epub 2012 Jan 9. PMID:22229634 doi:10.1021/ja211524d
