Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

Felix Quitterer; Philipp Beck; Adelbert Bacher; Michael Groll

doi:10.1002/anie.201301164

Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

Felix Quitterer, Philipp Beck, Adelbert Bacher, Michael Groll

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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.

Original language	English (US)
Pages (from-to)	7033-7037
Number of pages	5
Journal	Angewandte Chemie International Edition
Volume	52
Issue number	27
DOIs	https://doi.org/10.1002/anie.201301164
State	Published - May 29 2013
Externally published	Yes

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10.1002/anie.201301164

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title = "Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)",

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 {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

author = "Felix Quitterer and Philipp Beck and Adelbert Bacher and Michael Groll",

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.",

year = "2013",

month = may,

day = "29",

doi = "10.1002/anie.201301164",

language = "English (US)",

volume = "52",

pages = "7033--7037",

journal = "Angewandte Chemie International Edition",

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publisher = "John Wiley and Sons Ltd",

number = "27",

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T1 - Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

AU - Quitterer, Felix

AU - Beck, Philipp

AU - Bacher, Adelbert

AU - Groll, Michael

N1 - 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.

PY - 2013/5/29

Y1 - 2013/5/29

N2 - 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.

AB - 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.

UR - http://hdl.handle.net/10754/599762

UR - http://doi.wiley.com/10.1002/anie.201301164

UR - http://www.scopus.com/inward/record.url?scp=84879399790&partnerID=8YFLogxK

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DO - 10.1002/anie.201301164

M3 - Article

C2 - 23720358

SN - 1433-7851

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SP - 7033

EP - 7037

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 27

ER -

Structure and Reaction Mechanism of Pyrrolysine Synthase (PylD)

Abstract

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