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)|
|Number of pages||4|
|Journal||Angewandte Chemie International Edition|
|State||Published - Jun 10 2014|
Bibliographical noteKAUST 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.