Author:
Wang Hua,Zhang Huaidong,Mi Yanling,Ju Jianhua,Chen Qi,Zhang Houjin
Abstract
β-Carboline alkaloids (βCs), with tricyclic pyrido[3,4-b]indole rings, have important pharmacological and therapeutic value. In the biosynthesis of βCs, the Pictet–Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that are known to catalyse PS cyclization. It can also catalyse decarboxylation and oxidation. Here, the expression, crystallization and preliminary data analysis of McbB are reported. The crystals diffracted to 2.10 Å resolution and belonged to the monoclinic space groupP21, with unit-cell parametersa= 66.06,b= 85.48,c= 106.19 Å, α = 90.00, β = 106.77, γ = 90.00°. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Reference23 articles.
1. Alomar, M. L., Rasse-Suriani, F. A. O., Ganuza, A., Cóceres, V. M., Cabrerizo, F. M. & Angel, S. O. (2013). BMC Res. Notes, 6, 193.
2. iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM
3. Rapid Identification of Enzyme Variants for Reengineered Alkaloid Biosynthesis in Periwinkle
4. Lysine Decarboxylase Catalyzes the First Step of Quinolizidine Alkaloid Biosynthesis and Coevolved with Alkaloid Production in Leguminosae
5. Quinolizidine alkaloid biosynthesis: recent advances and future prospects
Cited by
2 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献