ArticleBiochemistry2012
Two structures of a thiazolinyl imine reductase from Yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 21 citations in OpenAlex.
- Two ubiquitous aldo-keto reductases in the genus Papaver support a patchwork model for morphine pathway evolution.Communications biology · 2024Article
- Genome-Guided Discovery of the Myxobacterial Thiolactone-Containing Sorangibactins.ACS chemical biology · 2023Article
- Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Data-Independent Acquisition Proteomics Unravels the Effects of Iron Ions on Coronatine Synthesis inFrontiers in microbiology · 2020Article
- YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria.The Journal of biological chemistry · 2018Article
- 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
- Holo Structure and Steady State Kinetics of the Thiazolinyl Imine Reductases for Siderophore Biosynthesis.Biochemistry · 2016Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The thiazolinyl imine reductase from Yersinia enterocolitica (Irp3) catalyzes the NADPH-dependent reduction of a thiazoline ring in an intermediate for the formation of the siderophore yersiniabactin. Two structures of Irp3 were determined in the apo (1.85 Å) and NADP(+)-bound (2.31 Å) forms. Irp3 is structurally homologous to sugar oxidoreductases such as glucose-fructose oxidoreductase and 1,5-anhydro-d-fructose reductase, as well as to biliverdin reductase. A homology model of the thiazolinyl imine reductase from Pseudomonas aeruginosa (PchG) was generated. Extensive loop insertions are observed in the C-terminal domain that are unique to Irp3 and PchG and not found in the structural homologues that recognize small molecular substrates. These loops are hypothesized to be important for binding of the nonribosomal peptide synthetase modules (found in HMWP1 and PchF, respectively) to which the substrate of the reductase is covalently attached. A catalytic mechanism for the donation of a proton from a general acid (either histidine 101 or tyrosine 128) and the donation of a hydride from C4 of nicotinamide of the NADPH cofactor is proposed for reduction of the carbon-nitrogen double bond of the thiazoline.
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