title: β-Sultams exhibit discrete binding preferences for diverse bacterial enzymes with nucleophilic residues.
abstract: β-Sultams are potent electrophiles that modify nucleophilic residues in selected enzyme active sites. We here identify and characterize some of the specific bacterial targets and show a unique inhibition of the azoreductase family.
authors.affiliation: Department of Chemistry, Center for Integrated Protein Science Munich (CIPSM), Technische Universität Müchen, Garching, Germany. stephan.sieber@tum.de.
authors.forename: Roman
authors.initials: R
authors.lastname: Kolb
authors.forename: Nina C
authors.initials: NC
authors.lastname: Bach
authors.forename: Stephan A
authors.initials: SA
authors.lastname: Sieber
mesh_terms: D043383:Adenosylhomocysteinase / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D020134:Catalytic Domain; D002851:Chromatography, High Pressure Liquid; D018360:Crystallography, X-Ray; D011485:Protein Binding; D019704:Protein Disulfide-Isomerases / Q000737:chemistry / Q000378:metabolism; D013449:Sulfonamides / Q000737:chemistry / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
chemical_list: D001426:Bacterial Proteins; D013449:Sulfonamides; C480101:beta-sultam; D043383:Adenosylhomocysteinase; D019704:Protein Disulfide-Isomerases