Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

Felix Quitterer, Philipp Beck, Adelbert Bacher, Michael Groll

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The final step in the biosynthesis of the 22nd genetically encoded amino acid, pyrrolysine, is catalyzed by PylD, a structurally and mechanistically unique dehydrogenase. This catalyzed reaction includes an induced-fit mechanism achieved by major structural rearrangements of the N-terminal helix upon substrate binding. Different steps of the reaction trajectory are visualized by complex structures of PylD with substrate and product. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish (US)
Pages (from-to)7033-7037
Number of pages5
JournalAngewandte Chemie International Edition
Issue number27
StatePublished - May 29 2013
Externally publishedYes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): FIC/2010/07
Acknowledgements: We thank the staff of the beamline X06SA at the Paul Scherrer Institute, Swiss Light Source, Villigen (Switzerland) for their help with data collection and Katrin Gartner for excellent technical assistance. We acknowledge Dr. Anja List who participated in the PylD project. This work was supported by the Hans-Fischer-Gesellschaft, by Award No. FIC/2010/07 from the King Abdullah University of Science and Technology (KAUST), and by the Deutsche Forschungsgemeinschaft (DFG, grant GR1861/7-1).
This publication acknowledges KAUST support, but has no KAUST affiliated authors.


Dive into the research topics of 'Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)'. Together they form a unique fingerprint.

Cite this