| Structural highlights
Function
BLBV2_ECOLX Class B beta-lactamase which confers resistance to the beta-lactam antibiotics, including penicillins, cephalosporins and carbapenems (PubMed:20498317, PubMed:31744917). Acts via hydrolysis of the beta-lactam ring (PubMed:20498317, PubMed:24965651). Has penicillin-, cephalosporin- and carbapenem-hydrolyzing activities (PubMed:20498317, PubMed:24965651).[1] [2] [3]
References
- ↑ Borgianni L, Vandenameele J, Matagne A, Bini L, Bonomo RA, Frère JM, Rossolini GM, Docquier JD. Mutational analysis of VIM-2 reveals an essential determinant for metallo-beta-lactamase stability and folding. Antimicrob Agents Chemother. 2010 Aug;54(8):3197-204. PMID:20498317 doi:10.1128/AAC.01336-09
- ↑ King AM, Reid-Yu SA, Wang W, King DT, De Pascale G, Strynadka NC, Walsh TR, Coombes BK, Wright GD. Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance. Nature. 2014 Jun 26;510(7506):503-6. PMID:24965651 doi:10.1038/nature13445
- ↑ Cheng Z, Shurina BA, Bethel CR, Thomas PW, Marshall SH, Thomas CA, Yang K, Kimble RL, Montgomery JS, Orischak MG, Miller CM, Tennenbaum JL, Nix JC, Tierney DL, Fast W, Bonomo RA, Page RC, Crowder MW. A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc Conditions. MBio. 2019 Nov 19;10(6). pii: mBio.02412-19. doi: 10.1128/mBio.02412-19. PMID:31744917 doi:http://dx.doi.org/10.1128/mBio.02412-19
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