128693-75-4Relevant academic research and scientific papers
Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme
Miller, David J.,Hammond, Stephen M.,Anderluzzi, Daniela,Bugg, Timothy D. H.
, p. 131 - 142 (2007/10/03)
Pseudo-tri- and -tetra-peptide aminoalkylphosphinic acids of general structure X-LyS-PO2H-Gly-Ala have been synthesised as transition state analogues for D-Ala-D-Ala adding enzyme. The key synthetic step used to assemble the C-terminal dipeptide unit is a modified Arbusov reaction, coupling bromopropionyl-D-alanine methyl ester to a silylated aminoalkylphosphonite. Kinetic assays with the purified E. coli enzyme reveal that the phosphinate analogues act as reversible competitive inhibitors, with Ki values in the range 200-700 μM. Extended analogues mimicking the peptide chain of the UDPMurNAc-L-Ala-γ-D-Glu-m-DAP substrate show increased binding affinity for the enzyme active site. These are the first reported inhibitors for D-Ala-D-Ala adding enzyme.
1-Aminoalkylphosphonous Acids. Part 1. Isosteres of the Protein Amino Acids
Baylis, E. Keith,Campbell, Colin D.,Dingwall, John G.
, p. 2845 - 2853 (2007/10/02)
The synthesis of 1-aminoalkylphosphonous acids, isosteres of the protein amino acids, by addition of hypophosphorous acid to diphenylmethylimines is described.These analogues of glycine, alanine, valine, leucine, isoleucine, phenylalanine, tyrosine, tryptophan, serine, threonine, methionine, cysteine, cystine, glutamic acid, lysine, ornithine, arginine, and proline have been prepared and the analogues of alanine, valine, leucine, phenylalanine, and methionine resolved.The alanine, valine and methionine analogues have interesting antimicrobial activity and the alanine analogue has plant growth inhibiting properties.Oxidation of the appropriate 1-aminoalkylphosphonous acids gave the 1-aminoalkylphosphonic acid analogues of (+/-)-alanine, (-)-alanine, (+/-)-valine, (-)-valine, (+/-)-serine, (+/-)-threonine, (+/-)-lysine, (-)-leucine, and (+/-)-ornithine.
