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.
authors.affiliation: Center for Integrated Protein Science Munich (CIPSM), Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching (Germany).
authors.forename: Felix
authors.initials: F
authors.lastname: Quitterer
authors.forename: Philipp
authors.initials: P
authors.lastname: Beck
authors.forename: Adelbert
authors.initials: A
authors.lastname: Bacher
authors.forename: Michael
authors.initials: M
authors.lastname: Groll
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D008025:Ligases / Q000737:chemistry*; D008239:Lysine / Q000031:analogs & derivatives* / Q000737:chemistry; D011725:Pyridines / Q000138:chemical synthesis*; D011758:Pyrroles / Q000138:chemical synthesis*
chemical_list: D011725:Pyridines; D011758:Pyrroles; C013231:pyrroline; D008025:Ligases; C456839:pyrrolysine; D008239:Lysine; C023666:pyridine
keywords: amino acids; dehydrogenases; enzyme catalysis; protein crystallography; pyrrolysine