4gmf › Citations

Two structures of a thiazolinyl imine reductase from Yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1.

Meneely KM, Lamb AL
Biochemistry 51 9002-13 (2012)
Cited: 12 times
EuropePMC logo PMID: 23066849

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.

Articles - 4gmf mentioned but not cited (2)

  1. Two structures of a thiazolinyl imine reductase from Yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1. Meneely KM, Lamb AL. Biochemistry 51 9002-9013 (2012)
  2. 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 55 5423-5433 (2016)


Reviews citing this publication (2)

  1. Imine reductases (IREDs). Mangas-Sanchez J, France SP, Montgomery SL, Aleku GA, Man H, Sharma M, Ramsden JI, Grogan G, Turner NJ. Curr Opin Chem Biol 37 19-25 (2017)
  2. Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study. Ronnebaum TA, Lamb AL. Curr Opin Struct Biol 53 1-11 (2018)

Articles citing this publication (8)

  1. Structure and activity of NADPH-dependent reductase Q1EQE0 from Streptomyces kanamyceticus, which catalyses the R-selective reduction of an imine substrate. Rodríguez-Mata M, Frank A, Wells E, Leipold F, Turner NJ, Hart S, Turkenburg JP, Grogan G. Chembiochem 14 1372-1379 (2013)
  2. InspIRED by Nature: NADPH-Dependent Imine Reductases (IREDs) as Catalysts for the Preparation of Chiral Amines. Grogan G, Turner NJ. Chemistry 22 1900-1907 (2016)
  3. Identification of imine reductase-specific sequence motifs. Fademrecht S, Scheller PN, Nestl BM, Hauer B, Pleiss J. Proteins 84 600-610 (2016)
  4. YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria. Ohlemacher SI, Xu Y, Kober DL, Malik M, Nix JC, Brett TJ, Henderson JP. J Biol Chem 293 19572-19585 (2018)
  5. Enantioselective reduction of sulfur-containing cyclic imines through biocatalysis. Zumbrägel N, Merten C, Huber SM, Gröger H. Nat Commun 9 1949 (2018)
  6. Data-Independent Acquisition Proteomics Unravels the Effects of Iron Ions on Coronatine Synthesis in Pseudomonas syringae pv. tomato DC3000. He Y, Yu S, Liu S, Tian H, Yu C, Tan W, Zhang J, Li Z, Jiang F, Duan L. Front Microbiol 11 1362 (2020)
  7. Genome-Guided Discovery of the Myxobacterial Thiolactone-Containing Sorangibactins. Gao Y, Walt C, Bader CD, Müller R. ACS Chem Biol 18 924-932 (2023)
  8. Structural Studies of Modular Nonribosomal Peptide Synthetases. Patel KD, Ahmed SF, MacDonald MR, Gulick AM. Methods Mol Biol 2670 17-46 (2023)


Quick links