TY - JOUR
T1 - The Formation of Pyrroline and Tetrahydropyridine Rings in Amino Acids Catalyzed by 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: 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.
PY - 2014/6/10
Y1 - 2014/6/10
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
UR - http://www.scopus.com/inward/record.url?scp=84905375698&partnerID=8YFLogxK
U2 - 10.1002/anie.201402595
DO - 10.1002/anie.201402595
M3 - Article
C2 - 24916332
SN - 1433-7851
VL - 53
SP - 8150
EP - 8153
JO - Angewandte Chemie International Edition
JF - Angewandte Chemie International Edition
IS - 31
ER -