104523-59-3Relevant articles and documents
Forming cross-linked peptidoglycan from synthetic gram-negative lipid II
Lebar, Matthew D.,Lupoli, Tania J.,Tsukamoto, Hirokazu,May, Janine M.,Walker, Suzanne,Kahne, Daniel
supporting information, p. 4632 - 4635 (2013/05/09)
The bacterial cell wall precursor, Lipid II, has a highly conserved structure among different organisms except for differences in the amino acid sequence of the peptide side chain. Here, we report an efficient and flexible synthesis of the canonical Lipid II precursor required for the assembly of Gram-negative peptidoglycan (PG). We use a rapid LC/MS assay to analyze PG glycosyltransfer (PGT) and transpeptidase (TP) activities of Escherichia coli penicillin binding proteins PBP1A and PBP1B and show that the native m-DAP residue in the peptide side chain of Lipid II is required in order for TP-catalyzed peptide cross-linking to occur in vitro. Comparison of PG produced from synthetic canonical E. coli Lipid II with PG isolated from E. coli cells demonstrates that we can produce PG in vitro that resembles native structure. This work provides the tools necessary for reconstituting cell wall synthesis, an essential cellular process and major antibiotic target, in a purified system.
THE FREE RADICAL CHEMISTRY OF CARBOXYLIC ESTERS OF 2-SELENOPYRIDINE-N-OXIDE: A CONVENIENT SYNTHESIS OF (L)-VINYLGLYCINE
Barton, Derek H. R.,Crich, David,Herve, Yolande,Potier, Pierre,Thierry, Josiane
, p. 4347 - 4358 (2007/10/02)
Optically pure (L)-vinylglycine has been synthesised by two different methods.The first of these involves protected (L)-glutamate esters of N-hydroxy-2-seleno-pyridine.Such esters are shown to undergo the same decarboxylative rearrangement as their thio-a
