Journal
BIOCHEMISTRY
Volume 55, Issue 38, Pages 5423-5433Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00735
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Funding
- National Institutes of Health (NIH) from the National Institute for Allergy and Infectious Disease [R01 AI77725, K02 AI093675]
- National Science Foundation (NSF) [CHE-1403293]
- Graduate Training Program in Dynamic Aspects of Chemical Biology NIH [T32 GM008545]
- NIH [S01 RR024664]
- NSF [0320648]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1403293] Funding Source: National Science Foundation
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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 angstrom resolution and a holo structure to 1.28 angstrom 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 synnthetase module during assembly line biosynthesis of the siderophore.
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