{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rodkey EA"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["18358-69"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4042847"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["135(49)"],"pubmed_abstract":["The inhibition of the class A SHV-1 β-lactamase by 7-(tert-butoxycarbonyl)methylidenecephalosporin sulfone was examined kinetically, spectroscopically, and crystallographically. An 1.14 Å X-ray crystal structure shows that the stable acyl-enzyme, which incorporates an eight-membered ring, is a covalent derivative of Ser70 linked to the 7-carboxy group of 2-H-5,8-dihydro-1,1-dioxo-1,5-thiazocine-4,7-dicarboxylic acid. A cephalosporin-derived enzyme complex of this type is unprecedented, and the rearrangement leading to its formation may offer new possibilities for inhibitor design. The observed acyl-enzyme derives its stability from the resonance stabilization conveyed by the β-aminoacrylate (i.e., vinylogous urethane) functionality as there is relatively little interaction of the eight-mem"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["β-Lactamase inhibition by 7-alkylidenecephalosporin sulfones: allylic transposition and formation of an unprecedented stabilized acyl-enzyme."],"pmcid":["PMC4042847"],"funding_grant_id":["R01AI072219","R01AI100560","R01 AI063517","R01 AI100560","GM54072","R01AI063517","R01 AI062968","R56 GM054072","AI062968","R01 GM054072","R01 AI072219","R56 AI062968"],"pubmed_authors":["Carey PR","Che T","Buynak JD","Bethel CR","Smith KM","McLeod DC","van den Akker F","Rodkey EA","Bonomo RA","Xu Y","Chai W"],"additional_accession":[]},"is_claimable":false,"name":"β-Lactamase inhibition by 7-alkylidenecephalosporin sulfones: allylic transposition and formation of an unprecedented stabilized acyl-enzyme.","description":"The inhibition of the class A SHV-1 β-lactamase by 7-(tert-butoxycarbonyl)methylidenecephalosporin sulfone was examined kinetically, spectroscopically, and crystallographically. An 1.14 Å X-ray crystal structure shows that the stable acyl-enzyme, which incorporates an eight-membered ring, is a covalent derivative of Ser70 linked to the 7-carboxy group of 2-H-5,8-dihydro-1,1-dioxo-1,5-thiazocine-4,7-dicarboxylic acid. A cephalosporin-derived enzyme complex of this type is unprecedented, and the rearrangement leading to its formation may offer new possibilities for inhibitor design. The observed acyl-enzyme derives its stability from the resonance stabilization conveyed by the β-aminoacrylate (i.e., vinylogous urethane) functionality as there is relatively little interaction of the eight-mem","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Dec","modification":"2026-04-29T11:45:12.702Z","creation":"2026-04-14T03:07:01.589Z"},"accession":"S-EPMC4042847","cross_references":{"pubmed":["24219313"],"doi":["10.1021/ja403598g"]}}