1186-90-9Relevant articles and documents
Genomics-driven discovery of taiwachelin, a lipopeptide siderophore from Cupriavidus taiwanensis
Kreutzer, Martin F.,Nett, Markus
, p. 9338 - 9343 (2012)
A genome mining study led to the identification of a previously unrecognised siderophore biosynthesis gene cluster in the nitrogen-fixing bacterium Cupriavidus taiwanensis LMG19424. Based upon predicted structural residues, a convenient strategy for an NMR-assisted isolation of the associated metabolite was designed. The structure of the purified siderophore, taiwachelin, was fully characterized by spectroscopic methods and chemical derivatisation.
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Liwschitz,Y. et al.
, p. 2104 - 2105 (1967)
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Jones,C.W. et al.
, p. 4363 - 4366 (1969)
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Okai et al.
, p. 2154,2158 (1967)
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Ambiguity of NRPS Structure Predictions: Four Bidentate Chelating Groups in the Siderophore Pacifibactin
Hardy, Clifford D.,Butler, Alison
, p. 990 - 997 (2019)
Identified through a bioinformatics approach, a nonribosomal peptide synthetase gene cluster in Alcanivorax pacificus encodes the biosynthesis of the new siderophore pacifibactin. The structure of pacifibactin differs markedly from the bioinformatic prediction and contains four bidentate metal chelation sites, atypical for siderophores. Genome mining and structural characterization of pacifibactin is reported herein, as well as characterization of pacifibactin variants accessible due to a lack of adenylation domain fidelity during biosynthesis. A spectrophotometric titration of pacifibactin with Fe(III) and 13C NMR spectroscopy of the Ga(III)-pacifibactin complex establish 1:1 metal:pacifibactin coordination and reveal which of the bidentate binding groups are coordinated to the metal. The photoreaction of Fe(III)-pacifibactin, resulting from Fe(III) coordination of the β-hydroxyaspartic acid ligands, is reported.
IMPROVED RESOLUTION OF beta -HYDROXY-DL-ASPARTIC ACID ON OPTICALLY ACTIVE RESIN CONTAINING L-LYSINE OR L-ORNITHINE. erythro
Anpeiji,Toritani,Kawada,Kondo,Murai,Okai,Yoshida,Imai
, p. 2994 - 2998 (1983)
A series of experiments on column chromatography of the optically active resin containing L-lysine or L-ornithine were carried out with pyridinium acetate and ammonium acetate solvent systems as the eluents. threo- beta -Hydroxy-DL-aspartic acid was found to be resolved on the optically active resin containing L-lysine with ammonium acetate solvent system; erythro- beta -hydroxy-DL-aspartic acid could be resolved on that containing L-ornithine with pyridinium acetate solvent system. The threo or erthro racemate was resolved on a preparative scale, and the resolution including the complete characterization of enantiomers resolved was first accomplished.
Stalobacin: Discovery of Novel Lipopeptide Antibiotics with Potent Antibacterial Activity against Multidrug-Resistant Bacteria
Matsui, Kouhei,Matsui, Kouhei,Kan, Yukiko,Kikuchi, Junko,Matsushima, Keisuke,Takemura, Miki,Maki, Hideki,Kozono, Iori,Ueda, Taichi,Minagawa, Kazuyuki
supporting information, p. 6090 - 6095 (2020/07/10)
A novel lipopeptide antibiotic, stalobacin I (1), was discovered from a culture broth of an unidentified Gram-negative bacterium. Stalobacin I (1) had a unique chemical architecture composed of an upper and a lower half peptide sequence, which were linked via a hemiaminal methylene moiety. The sequence of 1 contained an unusual amino acid, carnosadine, 3,4-dihydroxyariginine, 3-hydroxyisoleucine, and 3-hydroxyaspartic acid, and a novel cyclopropyl fatty acid. The antibacterial activity of 1 against a broad range of drug-resistant Gram-positive bacteria was much stronger than those of last resort antibiotics such as vancomycin, linezolid, and telavancin (MIC 0.004-0.016 μg/mL). Furthermore, compound 1 induced a characteristic morphological change in Gram-positive and Gram-negative strains by inflating the bacterial cell body. The absolute configuration of a cyclopropyl amino acid, carnosadine, was determined by the synthetic study of its stereoisomers, which was an essential component for the strong activity of 1.
