ArticleThe Journal of biological chemistry2010
Catalytic role of the metal ion in the metallo-beta-lactamase GOB.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Biochemical properties and substrate specificity of GOB-38 in Elizabethkingia anophelis.Scientific reports · 2025Article
- Revisiting the Metallo-International journal of microbiology · 2025Review
- LysR-type transcriptional regulatorFrontiers in cellular and infection microbiology · 2025Article
- Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.Frontiers in chemistry · 2023Review
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.Protein science : a publication of the Protein Society · 2020Article
- A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Nature communications · 2017Article
- Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Antimicrobial agents and chemotherapy · 2016Article
- Overcoming differences: The catalytic mechanism of metallo-β-lactamases.FEBS letters · 2015Review
- Draft Genome Sequence of Strain ATCC 33958, Reported To Be Elizabethkingia miricola.Genome announcements · 2015Article
- Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Journal of the American Chemical Society · 2014Article
- Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.Inorganic chemistry · 2012Article
- On the active site of mononuclear B1 metallo β-lactamases: a computational study.Journal of computer-aided molecular design · 2012Article
- Carbapenem resistance in Elizabethkingia meningoseptica is mediated by metallo-β-lactamase BlaB.Antimicrobial agents and chemotherapy · 2012Article
- In vivo impact of Met221 substitution in GOB metallo-β-lactamase.Antimicrobial agents and chemotherapy · 2012Article
- Mechanisms of resistance and clinical relevance of resistance to β-lactams, glycopeptides, and fluoroquinolones.Mayo Clinic proceedings · 2012Review
- The CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase activity.Extremophiles : life under extreme conditions · 2012Article
- Carbapenems: past, present, and future.Antimicrobial agents and chemotherapy · 2011Review
- Structure of apo- and monometalated forms of NDM-1--a highly potent carbapenem-hydrolyzing metallo-β-lactamase.PloS one · 2011Article
- QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Journal of the American Chemical Society · 2010Article
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3 authors.
Funding
Abstract
Metallo-beta-lactamases (MbetaLs) stand as one of the main mechanisms of bacterial resistance toward carbapenems. The rational design of an inhibitor for MbetaLs has been limited by an incomplete knowledge of their catalytic mechanism and by the structural diversity of their active sites. Here we show that the MbetaL GOB from Elizabethkingia meningoseptica is active as a monometallic enzyme by using different divalent transition metal ions as surrogates of the native Zn(II) ion. Of the metal derivatives in which Zn(II) is replaced, Co(II) and Cd(II) give rise to the most active enzymes and are shown to occupy the same binding site as the native ion. However, Zn(II) is the only metal ion capable of stabilizing an anionic intermediate that accumulates during nitrocefin hydrolysis, in which the C-N bond has already been cleaved. This finding demonstrates that the catalytic role of the metal ion in GOB is to stabilize the formation of this intermediate prior to nitrogen protonation. This role may be general to all MbetaLs, whereas nucleophile activation by a Zn(II) ion is not a conserved mechanistic feature.
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