ArticleThe Biochemical journal2004
Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: temperature- and pH-dependence.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 49 citations in OpenAlex.
- Activation and thermal stabilization of a recombinant γ-glutamyltranspeptidase from Bacillus licheniformis ATCC 27811 by monovalent cations.Applied microbiology and biotechnology · 2022Article
- Mechanical Bond Approach to Introducing Self-Adaptive Active Sites in Covalent Organic Frameworks for Zinc-Catalyzed Organophosphorus Degradation.ACS central science · 2021Article
- Pollen-inspired enzymatic microparticles to reduce organophosphate toxicity in managed pollinators.Nature food · 2021Article
- Computational enzymology for degradation of chemical warfare agents: promising technologies for remediation processes.AIMS microbiology · 2017Article
- Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.Applied and environmental microbiology · 2015Article
- Mechanistic study of manganese-substituted glycerol dehydrogenase using a kinetic and thermodynamic analysis.PloS one · 2014Article
- The effect of conformational variability of phosphotriesterase upon N-acyl-L-homoserine lactone and paraoxon binding: insights from molecular dynamics studies.Molecules (Basel, Switzerland) · 2013Article
- Article
- Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus.PloS one · 2012Article
- Conformational variability of organophosphorus hydrolase upon soman and paraoxon binding.The journal of physical chemistry. B · 2011Article
- Molecular dynamics simulations of the detoxification of paraoxon catalyzed by phosphotriesterase.Journal of computational chemistry · 2009Article
- Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.Archives of biochemistry and biophysics · 2009Article
- Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site.The Biochemical journal · 2006Article
- A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties.Extremophiles : life under extreme conditions · 2005Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphotriesterase (PTE) detoxifies nerve agents and organophosphate pesticides. The two zinc cations of the PTE active centre can be substituted by other transition metal cations without loss of activity. Furthermore, metal-substituted PTEs display differences in catalytic properties. A prerequisite for engineering highly efficient mutants of PTE is to improve their thermostability. Isoelectric focusing, capillary electrophoresis and steady-state kinetics analysis were used to determine the contribution of the active-site cations Zn2+, Co2+ or Cd2+ to both the catalytic activity and the conformational stability of the corresponding PTE isoforms. The three isoforms have different pI values (7.2, 7.5 and 7.1) and showed non-superimposable electrophoretic titration curves. The overall structural alterations, causing changes in functional properties, were found to be related to the nature of the bound cation: ionic radius and ion electronegativity correlate with Km and kcat respectively. In addition, the pH-dependent activity profiles of isoforms were different. The temperature-dependent profiles of activity showed maximum activity at T < or =35 degrees C, followed by an activation phase near 45-48 degrees C and then inactivation which was completed at 60 degrees C. Analysis of thermal denaturation of the PTEs provided evidence that the activation phase resulted from a transient intermediate. Finally, at the optimum activity between pH 8 and 9.4, the thermostability of the different PTEs increased as the pH decreased, and the metal cation modulated stability (Zn2+-, Co2+- and Cd2+-PTE showed different T (m) values of 60.5-67 degrees C, 58-64 degrees C and 53-64 degrees C respectively). Requirements for optimum activity of PTE (displayed by Co2+-PTE) and maximum stability (displayed by Zn2+-PTE) were demonstrated.
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