Struktur und Reaktionsmechanismus der Pyrrolysinsynthase (PylD)

Felix Quitterer; Philipp Beck; Adelbert Bacher; Michael Groll

doi:10.1002/ange.201301164

Struktur und Reaktionsmechanismus der Pyrrolysinsynthase (PylD)

Felix Quitterer, Philipp Beck, Adelbert Bacher, Michael Groll

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

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.

Original language	English (US)
Pages (from-to)	7171-7175
Number of pages	5
Journal	Angewandte Chemie
Volume	125
Issue number	27
DOIs	https://doi.org/10.1002/ange.201301164
State	Published - May 29 2013
Externally published	Yes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): FIC/2010/07
Acknowledgements: Wir danken den Mitarbeitern der Beamline X06SA am Paul Scherrer Institut, Swiss Light Source, Villigen (Schweiz), für Hilfe bei der Datensammlung und Katrin Gärtner für ihre hervorragende Mitarbeit. Weiterhin danken wir Dr. Anja List für Hilfestellung und Diskussion. Diese Arbeit wurde durch die Hans-Fischer-Gesellschaft, durch Award No. FIC/2010/07 der King Abdullah University of Science and Technology (KAUST) und durch die Deutsche Forschungsgemeinschaft (DFG, Nr. GR1861/7-1) unterstützt.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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10.1002/ange.201301164

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title = "Struktur und Reaktionsmechanismus der Pyrrolysinsynthase (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.",

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: Wir danken den Mitarbeitern der Beamline X06SA am Paul Scherrer Institut, Swiss Light Source, Villigen (Schweiz), f{\"u}r Hilfe bei der Datensammlung und Katrin G{\"a}rtner f{\"u}r ihre hervorragende Mitarbeit. Weiterhin danken wir Dr. Anja List f{\"u}r Hilfestellung und Diskussion. Diese Arbeit wurde durch die Hans-Fischer-Gesellschaft, durch Award No. FIC/2010/07 der King Abdullah University of Science and Technology (KAUST) und durch die Deutsche Forschungsgemeinschaft (DFG, Nr. GR1861/7-1) unterst{\"u}tzt. This publication acknowledges KAUST support, but has no KAUST affiliated authors.",

year = "2013",

month = may,

day = "29",

doi = "10.1002/ange.201301164",

language = "English (US)",

volume = "125",

pages = "7171--7175",

journal = "Angewandte Chemie",

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AU - Quitterer, Felix

AU - Beck, Philipp

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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.

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.

UR - http://hdl.handle.net/10754/599784

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

U2 - 10.1002/ange.201301164

DO - 10.1002/ange.201301164

M3 - Article

SN - 0044-8249

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JO - Angewandte Chemie

JF - Angewandte Chemie

IS - 27

ER -

Struktur und Reaktionsmechanismus der Pyrrolysinsynthase (PylD)

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