Holo structure and steady state kinetics of the thiazolinyl imine reductases for siderophore biosynthesis

Kathleen M. Meneely, Trey A. Ronnebaum, Andrew P. Riley, Thomas E. Prisinzano, Audrey L. Lamb

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

Thiazolinyl imine reductases catalyze the NADPH-dependent reduction of a thiazoline to a thiazolidine, a required step in the formation of the siderophores yersiniabactin (Yersinia spp.) and pyochelin (Pseudomonas aeruginosa). These stand-alone nonribosomal peptide tailoring domains are structural homologues of sugar oxidoreductases. Two closed structures of the thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) are presented here: an NADP+-bound structure to 1.45 Å resolution and a holo structure to 1.28 Å resolution with NADP+ and a substrate analogue bound. Michaelis-Menten kinetics were measured using the same substrate analogue and the homologue from P. aeruginosa, PchG. The data presented here support the hypothesis that tyrosine 128 is the likely general acid residue for catalysis and also highlight the phosphopantetheine tunnel for tethering of the substrate to the nonribosomal peptide synthetase module during assembly line biosynthesis of the siderophore.

Original languageEnglish
Pages (from-to)5423-5433
Number of pages11
JournalBiochemistry
Volume55
Issue number38
DOIs
StatePublished - Sep 27 2016

Bibliographical note

Publisher Copyright:
© 2016 American Chemical Society.

ASJC Scopus subject areas

  • Biochemistry

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