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 journalArticlepeer-review

3 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 languageEnglish (US)
Pages (from-to)8150-8153
Number of pages4
JournalAngewandte Chemie International Edition
Volume53
Issue number31
DOIs
StatePublished - Jun 10 2014
Externally publishedYes

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