ArticleBiochemistry2006
Mechanistic studies on the mononuclear ZnII-containing metallo-beta-lactamase ImiS from Aeromonas sobria.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.International journal of molecular sciences · 2015Pooled it
- Revisiting the Metallo-International journal of microbiology · 2025Review
- 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 characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1.The Journal of antimicrobial chemotherapy · 2020Article
- Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism.Biomolecules · 2020Review
- PFM-Like Enzymes Are a Novel Family of Subclass B2 Metallo-β-Lactamases from Pseudomonas synxantha Belonging to the Pseudomonas fluorescens Complex.Antimicrobial agents and chemotherapy · 2020Article
- A Noncanonical Metal Center Drives the Activity of the Sediminispirochaeta smaragdinae Metallo-β-lactamase SPS-1.Biochemistry · 2018Article
- Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis.MedChemComm · 2016Article
- Overcoming differences: The catalytic mechanism of metallo-β-lactamases.FEBS letters · 2015Review
- Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.ACS medicinal chemistry letters · 2015Article
- Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification,Chemical science · 2015Article
- Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Biochemistry · 2014Article
- Molecular mechanisms of substrate recognition and specificity of New Delhi metallo-β-lactamase.Antimicrobial agents and chemotherapy · 2014Article
- Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.Journal of the American Chemical Society · 2014Article
- New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases.Bioorganic & medicinal chemistry letters · 2013Article
- A quantum mechanics/molecular mechanics study on the hydrolysis mechanism of New Delhi metallo-β-lactamase-1.Journal of computer-aided molecular design · 2013Article
- Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.PloS one · 2013Article
- Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the post-hydrolysis reactions.PloS one · 2012Article
- Analysis of the functional contributions of Asn233 in metallo-β-lactamase IMP-1.Antimicrobial agents and chemotherapy · 2011Article
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6 authors.
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Abstract
In an effort to understand the reaction mechanism of a B2 metallo-beta-lactamase, steady-state and pre-steady-state kinetic and rapid freeze quench electron paramagnetic resonance (EPR) studies were conducted on ImiS and its reaction with imipenem and meropenem. pH dependence studies revealed no inflection points in the pH range of 5.0-8.5, while proton inventories demonstrated at least 1 rate-limiting proton transfer. Site-directed mutagenesis studies revealed that Lys224 plays a catalytic role in ImiS, while the side chain of Asn233 does not play a role in binding or catalysis. Stopped-flow fluorescence studies on ImiS, which monitor changes in tryptophan fluorescence on the enzyme, and its reaction with imipenem and meropenem revealed biphasic fluorescence time courses with a rate of fluorescence loss of 160 s(-)(1) and a slower rate of fluorescence regain of 98 s(-)(1). Stopped-flow UV-vis studies, which monitor the concentration of substrate, revealed a rapid loss in absorbance during catalysis with a rate of 97 s(-)(1). These results suggest that the rate-limiting step in the reaction catalyzed by ImiS is C-N bond cleavage. Rapid freeze quench EPR studies on Co(II)-substituted ImiS demonstrated the appearance of a rhombic signal after 10 ms that is assigned to a reaction intermediate that has a five-coordinate metal center. A distinct product (EP) complex was also observed and began to appear in 18-19 ms. When these results are taken together, they allow for a reaction mechanism to be offered for the B2 metallo-beta-lactamases and demonstrate that the mono- and dinuclear Zn(II)-containing enzymes share a common rate-limiting step, which is C-N bond cleavage.
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