Anno2016
AutoriBenoni R, Pertinhez TA, Spyrakis F, Davalli S, Pellegrino S, Paredi GL, Pezzotti A, Bettati S, Campanini B, Mozzarelli A
AbstractO-acetylserine sulfhydrylase (OASS), the enzyme catalysing the last step of cysteine biosynthesis in bacteria, is involved in antibiotic resistance and biofilm formation. Since mammals lack OASS, it is a potential target for antimicrobials. However, a limited number of inhibitors has been developed and crystallized in complex with OASS. STD-NMR was applied to study the interaction of the inhibitory pentapeptide MNYDI with the CysK and CysM OASS isozymes from Salmonella Typhimurium. Results are in excellent agreement with docking and SAR studies and confirm the important role played by the C-terminal Ile5 and the arylic moiety at P3 in dictating affinity
RivistaFebs Letters (print)
ISSN0014-5793
Impact factor
Volume590
Pagina inizio943
Pagina fine953
Autori IBFAndrea MOZZARELLI
Linee di Ricerca IBFMD.P01.008.001
Sedi IBFIBF.PI