Ontology highlight
ABSTRACT:
SUBMITTER: Salsi E
PROVIDER: S-EPMC2804909 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Salsi Enea E Bayden Alexander S AS Spyrakis Francesca F Amadasi Alessio A Campanini Barbara B Bettati Stefano S Dodatko Tetyana T Cozzini Pietro P Kellogg Glen E GE Cook Paul F PF Roderick Steven L SL Mozzarelli Andrea A
Journal of medicinal chemistry 20100101 1
The inhibition of cysteine biosynthesis in prokaryotes and protozoa has been proposed to be relevant for the development of antibiotics. Haemophilus influenzae O-acetylserine sulfhydrylase (OASS), catalyzing l-cysteine formation, is inhibited by the insertion of the C-terminal pentapeptide (MNLNI) of serine acetyltransferase into the active site. Four-hundred MNXXI pentapeptides were generated in silico, docked into OASS active site using GOLD, and scored with HINT. The terminal P5 Ile accounts ...[more]