56-45-1Relevant articles and documents
Catechoserine, a new catecholate-type inhibitor of tumor cell invasion from Streptomyces sp.
Igarashi, Yasuhiro,Iida, Takako,Fukuda, Takao,Miyanaga, Satoshi,Sakurai, Hiroaki,Saiki, Ikuo,Miyanouchi, Koji
, p. 207 - 209 (2012)
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Versatile synthon for chirally β-deuterated L-amino acids and synthesis of (3R)- and (3S)-[3-2H1]-L-serine
Maeda, Yutaka,Tago, Keiko,Eguchi, Tadashi,Kakinuma, Katsumi
, p. 1248 - 1254 (1996)
A divergent and highly enantioselective synthetic methodology for producing chirally β-deuterated L-amino acids was developed. This method is based upon the chirality transcription approach, using diacetone-D-glucos-3- ulose (1) as a template. 3-C-[2-2H1]-Ethenyl-3-O-(N- benzyl)methylthioformimidoyl-D-allo-derivatives (3b and 3c), which are easily accessible from 1, were subjected to halonium ion-assisted cyclization to afford highly diastereoselectively and efficiently versatile 5-membered cyclic carbamate synthons having a stereochemically defined deuterated halomethyl group (4c and 4d, respectively). Subsequent straightforward transformation of these synthons gave rise to (3R)- and (3S)-[3-2H1]-L- serine. Further transformation of the crucial halomethyl group of 4a-c was also pursued to extend this methodology.
Ruckerbactin Produced by Yersinia ruckeri YRB Is a Diastereomer of the Siderophore Trivanchrobactin Produced by Vibrio campbellii DS40M4
Butler, Alison,Dulaney, Kalana,Reitz, Zachary L.,Stow, Parker R.,Thomsen, Emil
, p. 264 - 269 (2022/01/15)
The Gram-negative bacterium Yersinia ruckeri is the causative agent for enteric red mouth disease in salmonids. The genome of Y. ruckeri YRB contains a biosynthetic gene cluster encoding the biosynthesis of catechol siderophores that are diastereomeric with the known vanchrobactin class of siderophores, (DHBDArgLSer)(1–3). Ruckerbactin (1), produced by Y. ruckeri YRB, was found to be the linear tris-l-serine ester composed of l-arginine and 2,3-dihydroxybenzoic acid, (DHBLArgLSer)3. The biscatechol, (DHBLArgLSer)2 (2), and monocatechol, DHBLArgLSer (3), compounds were also isolated and characterized. The macrolactone of ruckerbactin was not detected. The presence of LArg in ruckerbactin makes it the diastereomer of trivanchrobactin with DArg. The electronic circular dichroism spectra of Fe(III)–ruckerbactin and Fe(III)–trivanchrobactin reveal the opposite enantiomeric configurations at the Fe(III) sites. Fe(III)–ruckerbactin adopts the Δ configuration, and Fe(III)–trivanchrobactin adopts the Λ configuration. Y. ruckeri YRB was also found to produce the antimicrobial agent holomycin (4).
Saccharochelins A-H, Cytotoxic Amphiphilic Siderophores from the Rare Marine Actinomycete Saccharothrix sp. D09
Bian, Xiaoying,Dai, Guangzhi,Jiao, Nianzhi,Liu, Yang,Ravichandran, Vinothkannan,Ren, Xiangmei,Shen, Qiyao,Sui, Haiyan,Zhang, Youming,Zhong, Lin,Zhou, Haibo
, p. 2149 - 2156 (2021/08/20)
Siderophores are secreted by microorganisms to survive in iron-depleted conditions, and they also possess tremendous therapeutic potential. Genomic-inspired isolation facilitated the identification of eight amphiphilic siderophores, saccharochelins A-H (1-8), from a rare marine-derived Saccharothrix species. Saccharochelins feature a series of fatty acyl groups appended to the same tetrapeptide skeleton. With the help of gene disruption and heterologous expression, we identified the saccharochelin biosynthetic pathway. The diversity of saccharochelins originates from the flexible specificity of the starter condensation (CS) domain at the beginning of the nonribosomal peptide synthetase (NRPS) toward various fatty acyl substrates. Saccharochelins showed cytotoxicity against several human tumor cell lines, with IC50 values ranging from 2.3 to 17 μM. Additionally, the fatty acid side chains of the saccharochelins remarkably affected the cytotoxicity, suggesting changing the N-terminal acyl groups of lipopeptides may be a promising approach to produce more potent derivatives.
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.