Download MendeleyStructural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids
Yang, L., Hill, M., Wang, M., Panjikar, S., Stockigt, J.(2009) Angew Chem Int Ed Engl 48: 5211-5213
- PubMed: 19496101
- DOI: https://doi.org/10.1002/anie.200900150
- Primary Citation of Related Structures:
2WFL, 2WFM, 3GZJ - PubMed Abstract:
Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.
Organizational Affiliation:
Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, 383 Yu Hang Tang Road, Hangzhou 310058, China.
