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).
Leveraging Peptaibol Biosynthetic Promiscuity for Next-Generation Antiplasmodial Therapeutics
Lee, Jin Woo,Collins, Jennifer E.,Wendt, Karen L.,Chakrabarti, Debopam,Cichewicz, Robert H.
supporting information, p. 503 - 517 (2021/03/01)
Malaria remains a worldwide threat, afflicting over 200 million people each year. The emergence of drug resistance against existing therapeutics threatens to destabilize global efforts aimed at controlling Plasmodium spp. parasites, which is expected to leave vast portions of humanity unprotected against the disease. To address this need, systematic testing of a fungal natural product extract library assembled through the University of Oklahoma Citizen Science Soil Collection Program has generated an initial set of bioactive extracts that exhibit potent antiplasmodial activity (EC50 25 μM, selectivity index > 250). The unique chemodiversity afforded by these fungal isolates serves to unlock new opportunities for translating peptaibols into a bioactive scaffold worthy of further development.
Structure-guided engineering of: Pseudomonas dacunhae l-aspartate β-decarboxylase for l-homophenylalanine synthesis
Zhang, Min,Hu, Pengfei,Zheng, Yu-Cong,Zeng, Bu-Bing,Chen, Qi,Zhang, Zhi-Jun,Xu, Jian-He
, p. 13876 - 13879 (2020/11/18)
Structure-guided engineering of Pseudomonas dacunhael-aspartate β-decarboxylase (AspBDC) resulted in a double mutant (R37A/T382G) with remarkable 15400-fold improvement in specific activity reaching 216 mU mg-1, towards the target substrate 3(R)-benzyl-l-aspartate. A novel strategy for enzymatic synthesis of l-homophenylalanine was developed by using the variant as a biocatalyst affording 75% product yield within 12 h. Our results underscore the potential of engineered AspBDC for the biocatalytic synthesis of pharmaceutically relevant and value added unnatural l-amino acids.
