ArticleBiochemistry2016
Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Development of a novel anti-CEACAM5 VHH for SPECT imaging and potential cancer therapy applications.European journal of nuclear medicine and molecular imaging · 2025Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- Genome-Guided Discovery of the Myxobacterial Thiolactone-Containing Sorangibactins.ACS chemical biology · 2023Article
- Structural Characterization of anBiomolecules · 2020Article
- Stuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin Biosynthesis.Biochemistry · 2019Article
- Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study.Current opinion in structural biology · 2018Review
- Enantioselective reduction of sulfur-containing cyclic imines through biocatalysis.Nature communications · 2018Article
- Nonribosomal peptide synthetase biosynthetic clusters of ESKAPE pathogens.Natural product reports · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
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