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)

Angew Chem Int Ed Engl. 2014 Jul 28;53(31):8150-3. doi: 10.1002/anie.201402595. Epub 2014 Jun 10.

Authors

Felix Quitterer¹, Philipp Beck, Adelbert Bacher, Michael Groll

Affiliation

¹ Center for Integrated Protein Science Munich (CIPSM), Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching (Germany).

PMID: 24916332
DOI: 10.1002/anie.201402595

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.

Keywords: amino acids; dehydrogenases; enzyme catalysis; protein crystallography; pyrrolysine.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Catalysis
Catalytic Domain
Ligases / chemistry*
Lysine / analogs & derivatives*
Lysine / chemistry
Pyridines / chemical synthesis*
Pyrroles / chemical synthesis*

Substances

Pyridines
Pyrroles
pyrroline
Ligases
pyrrolysine
Lysine
pyridine