ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2012
Temperature- and pressure-dependent stopped-flow kinetic studies of jack bean urease. Implications for the catalytic mechanism.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 82 citations in OpenAlex.
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- An overview: metal-based inhibitors of urease.Journal of enzyme inhibition and medicinal chemistry · 2023Review
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- Enzyme Inhibitory Kinetics and Molecular Docking Studies of Halo-Substituted Mixed Ester/Amide-Based Derivatives as Jack Bean Urease Inhibitors.BioMed research international · 2020Article
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- Catalytic enzymes are active matter.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Urease-aided calcium carbonate mineralization for engineering applications: A review.Journal of advanced research · 2018Review
- Ureases: Historical aspects, catalytic, and non-catalytic properties - A review.Journal of advanced research · 2018Review
- Detection of DNA Amplicons of Polymerase Chain Reaction Using Litmus Test.Scientific reports · 2017Article
- Inhibition of Urease by Disulfiram, an FDA-Approved Thiol Reagent Used in Humans.Molecules (Basel, Switzerland) · 2016Article
- Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP.Biophysical journal · 2015Article
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- Hot biological catalysis: isothermal titration calorimetry to characterize enzymatic reactions.Journal of visualized experiments : JoVE · 2014Article
- Kinetics and mechanism of jack bean urease inhibition by Hg2+.Chemistry Central journal · 2012Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Urease, a Ni-containing metalloenzyme, features an activity that has profound medical and agricultural implications. The mechanism of this activity, however, has not been as yet thoroughly established. Accordingly, to improve its understanding, in this study we analyzed the steady-state kinetic parameters of the enzyme (jack bean), K (M) and k (cat), measured at different temperatures and pressures. Such an analysis is useful as it provides information on the molecular nature of the intermediate and transition states of the catalytic reaction. We measured the parameters in a noninteracting buffer using a stopped-flow technique in the temperature range 15-35 °C and in the pressure range 5-132 MPa, the pressure-dependent measurements being the first of their kind performed for urease. While temperature enhanced the activity of urease, pressure inhibited the enzyme; the inhibition was biphasic. Analyzing K (M) provided the characteristics of the formation of the ES complex, and analyzing k (cat), the characteristics of the activation of ES. From the temperature-dependent measurements, the energetic parameters were derived, i.e. thermodynamic ΔH (o) and ΔS (o) for ES formation, and kinetic ΔH ( ≠ ) and ΔS ( ≠ ) for ES activation, while from the pressure-dependent measurements, the binding ΔV (b) and activation ΔV(#)(cat) volumes were determined. The thermodynamic and activation parameters obtained are discussed in terms of the current proposals for the mechanism of the urease reaction, and they are found to support the mechanism proposed by Benini et al. (Structure 7:205-216; 1999), in which the Ni-Ni bridging hydroxide--not the terminal hydroxide--is the nucleophile in the catalytic reaction.
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