The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by Pyrrolysine Synthase (PylD)

Felix Quitterer; Philipp Beck; Adelbert Bacher; Michael Groll

doi:10.1002/anie.201402595

The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by Pyrrolysine Synthase (PylD)

Felix Quitterer, Philipp Beck, Adelbert Bacher, Michael Groll

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

6 Scopus citations

Abstract

The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English (US)
Pages (from-to)	8150-8153
Number of pages	4
Journal	Angewandte Chemie International Edition
Volume	53
Issue number	31
DOIs	https://doi.org/10.1002/anie.201402595
State	Published - Jun 10 2014
Externally published	Yes

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): FIC/2010/07
Acknowledgements: This work was supported by the Hans-Fischer-Gesellschaft, by Award No. FIC/2010/07 from KAUST, and by the Deutsche Forschungsgemeinschaft (DFG, grant GR1861/7-1).
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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title = "The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by Pyrrolysine Synthase (PylD)",

abstract = "The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues. {\textcopyright} 2014 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: This work was supported by the Hans-Fischer-Gesellschaft, by Award No. FIC/2010/07 from KAUST, and by the Deutsche Forschungsgemeinschaft (DFG, grant GR1861/7-1). This publication acknowledges KAUST support, but has no KAUST affiliated authors.",

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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: This work was supported by the Hans-Fischer-Gesellschaft, by Award No. FIC/2010/07 from KAUST, and by the Deutsche Forschungsgemeinschaft (DFG, grant GR1861/7-1). This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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N2 - The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - The dehydrogenase PylD catalyzes the ultimate step of the pyrrolysine pathway by converting the isopeptide L-lysine-Nε-3R-methyl-D-ornithine to the 22nd proteinogenic amino acid. In this study, we demonstrate how PylD can be harnessed to oxidize various isopeptides to novel amino acids by combining chemical synthesis with enzyme kinetics and X-ray crystallography. The data enable a detailed description of the PylD reaction trajectory for the biosynthesis of pyrroline and tetrahydropyridine rings as constituents of pyrrolysine analogues. © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

UR - http://hdl.handle.net/10754/599914

UR - http://doi.wiley.com/10.1002/anie.201402595

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DO - 10.1002/anie.201402595

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EP - 8153

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 31

ER -

The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by Pyrrolysine Synthase (PylD)

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