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Substrate Analog and NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocoliticaSubstrate Analog and NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica
Structural highlights
FunctionPublication Abstract from PubMedThiazolinyl 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 A resolution and a holo structure to 1.28 A 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. Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.,Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL Biochemistry. 2016 Sep 15. PMID:27601130[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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