Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

Handle URI:
http://hdl.handle.net/10754/599762
Title:
Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)
Authors:
Quitterer, Felix; Beck, Philipp; Bacher, Adelbert; Groll, Michael
Abstract:
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.
Citation:
Quitterer F, Beck P, Bacher A, Groll M (2013) Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD). Angew Chem Int Ed 52: 7033–7037. Available: http://dx.doi.org/10.1002/anie.201301164.
Publisher:
Wiley-Blackwell
Journal:
Angewandte Chemie International Edition
KAUST Grant Number:
FIC/2010/07
Issue Date:
29-May-2013
DOI:
10.1002/anie.201301164
PubMed ID:
23720358
Type:
Article
ISSN:
1433-7851
Sponsors:
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).
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Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorQuitterer, Felixen
dc.contributor.authorBeck, Philippen
dc.contributor.authorBacher, Adelberten
dc.contributor.authorGroll, Michaelen
dc.date.accessioned2016-02-28T06:09:13Zen
dc.date.available2016-02-28T06:09:13Zen
dc.date.issued2013-05-29en
dc.identifier.citationQuitterer F, Beck P, Bacher A, Groll M (2013) Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD). Angew Chem Int Ed 52: 7033–7037. Available: http://dx.doi.org/10.1002/anie.201301164.en
dc.identifier.issn1433-7851en
dc.identifier.pmid23720358en
dc.identifier.doi10.1002/anie.201301164en
dc.identifier.urihttp://hdl.handle.net/10754/599762en
dc.description.abstractThe 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.en
dc.description.sponsorshipWe 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).en
dc.publisherWiley-Blackwellen
dc.subjectamino acidsen
dc.subjectdehydrogenasesen
dc.subjectMethanosarcina barkerien
dc.subjectPylDen
dc.subjectpyrrolysineen
dc.titleStructure and Reaction Mechanism of Pyrrolysine Synthase (PylD)en
dc.typeArticleen
dc.identifier.journalAngewandte Chemie International Editionen
dc.contributor.institutionTechnische Universitat Munchen, Munich, Germanyen
kaust.grant.numberFIC/2010/07en

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