Title of article :
Inhibition of S-ribosylhomocysteinase (LuxS) by substrate analogues modified at the ribosyl C-3 position Original Research Article
Author/Authors :
Stanislaw F. Wnuk، نويسنده , , Jenay Robert، نويسنده , , Adam J. Sobczak، نويسنده , , Brandon P. Meyers، نويسنده , , Venkata L.A. Malladi، نويسنده , , Jinge Zhu، نويسنده , , Bhaskar Gopishetty، نويسنده , , Dehua Pei and Wim G. J. Hol، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2009
Abstract :
S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether bond of S-ribosylhomocysteine (SRH) to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione (DPD), which is the precursor of type 2 autoinducer for bacterial cell–cell communication. In this work, we have synthesized several SRH analogues modified at the ribose C3 pos
Keywords :
Enzyme inhibition , LuxS enzyme , S-Ribosylhomocysteine , Fluoro sugars
Journal title :
Bioorganic and Medicinal Chemistry
Journal title :
Bioorganic and Medicinal Chemistry
