179087-83-3Relevant articles and documents
Flexizyme-Enabled Benchtop Biosynthesis of Thiopeptides
Fleming, Steven R.,Bartges, Tessa E.,Vinogradov, Alexander A.,Kirkpatrick, Christine L.,Goto, Yuki,Suga, Hiroaki,Hicks, Leslie M.,Bowers, Albert A.
, p. 758 - 762 (2019)
Thiopeptides are natural antibiotics that are fashioned from short peptides by multiple layers of post-translational modification. Their biosynthesis, in particular the pyridine synthases that form the macrocyclic antibiotic core, has attracted intensive research but is complicated by the challenges of reconstituting multiple-pathway enzymes. By combining select RiPP enzymes with cell free expression and flexizyme-based codon reprogramming, we have developed a benchtop biosynthesis of thiopeptide scaffolds. This strategy side-steps several challenges related to the investigation of thiopeptide enzymes and allows access to analytical quantities of new thiopeptide analogs. We further demonstrate that this strategy can be used to validate the activity of new pyridine synthases without the need to reconstitute the cognate prior pathway enzymes.
ANTIBACTERIAL COMPOUNDS
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Page/Page column 28, (2018/10/19)
Novel compounds having antimicrobial activitiy, in particular against Pseudomonas aeruginosa, Burkholderia cepaciaand/or Clostridium difficile, and a pharmaceutical composition containing the novel compound.
Internally stabilized selenocysteine derivatives: Syntheses, 77Se NMR and biomimetic studies
Phadnis, Prasad P.,Mugesh
, p. 2476 - 2481 (2007/10/03)
Selenocystine ([Sec]2) and aryl-substituted selenocysteine (Sec) derivatives are synthesized, starting from commercially available amino acid L-serine. These compounds are characterized by a number of analytical techniques such as NMR (1H, 13C and 77Se) and TOF mass spectroscopy. This study reveals that the introduction of amino/imino substituents capable of interacting with selenium may stabilize the Sec derivatives. This study further suggests that the oxidation-elimination reactions in Sec derivatives could be used for the generation of biologically active selenols having internally stabilizing substituents. The Royal Society of Chemistry 2005.