Communication

Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids†

  1. Liuqing Yang1,2,
  2. Marco Hill Dr.2,
  3. Meitian Wang Dr.3,
  4. Santosh Panjikar Dr.4,
  5. Joachim Stöckigt Prof. Dr.1,2

Article first published online: 3 JUN 2009

DOI: 10.1002/anie.200900150

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 48, Issue 28, pages 5211–5213, June 29, 2009

Additional Information

How to Cite

Yang, L., Hill, M., Wang, M., Panjikar, S. and Stöckigt, J. (2009), Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids. Angewandte Chemie International Edition, 48: 5211–5213. doi: 10.1002/anie.200900150

Author Information

  1. 1

    Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, 383 Yu Hang Tang Road, Hangzhou 310058 (China)

  2. 2

    Lehrstuhl für Pharmazeutische Biologie, Institut für Pharmazie, Johannes-Gutenberg Universität, Staudinger Weg 5, 55128 Mainz (Germany), Fax: (+49) 6131-392-3752

  3. 3

    Swiss Light Source PX III, Paul Scherrer Institute, 5232 Villigen (Switzerland)

  4. 4

    European Molecular Biology Laboratory Hamburg, Outstation Deutsches Elektronen-Synchrotron, Notkestrasse 85, 22603 Hamburg (Germany)

  1. †

    This work was supported by Deutsche Forschungsgemeinschaft (Bad Godesberg, Germany), Fonds der Chemischen Industrie (Frankfurt/Main, Germany), and K. P. Chao’s High-Tech Foundation at Zhejiang University (Hangzhou, China). We thank Prof. Dr. David E. Cane (Brown University, USA) for critical discussions.

Publication History

  1. Issue published online: 25 JUN 2009
  2. Article first published online: 3 JUN 2009
  3. Manuscript Received: 9 JAN 2009

Funded by

  • Deutsche Forschungsgemeinschaft
  • Fonds der Chemischen Industrie
  • Zhejiang University

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Keywords:

  • alkaloids;
  • biosynthesis;
  • enzyme catalysis;
  • esterases;
  • protein structures

Graphical Abstract

Thumbnail image of graphical abstract

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C9- from C10-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 α/β-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Abstract

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C9- from C10-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 α/β-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

View Full Article with Supporting Information (HTML) Get PDF (459K)