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Scaffold tailoring by a newly detected Pictet-Spenglerase activity of strictosidine synthase: from the common tryptoline skeleton to the rare piperazino-indole framework.
Wu, Fangrui; Zhu, Huajian; Sun, Lianli; Rajendran, Chitra; Wang, Meitian; Ren, Xin; Panjikar, Santosh; Cherkasov, Artem; Zou, Hongbin; Stöckigt, Joachim.
Afiliación
  • Wu F; Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
J Am Chem Soc ; 134(3): 1498-500, 2012 Jan 25.
Article en En | MEDLINE | ID: mdl-22229634
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Piperazinas / Rauwolfia / Carbolinas / Liasas de Carbono-Nitrógeno / Indoles Idioma: En Revista: J Am Chem Soc Año: 2012 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Piperazinas / Rauwolfia / Carbolinas / Liasas de Carbono-Nitrógeno / Indoles Idioma: En Revista: J Am Chem Soc Año: 2012 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos