Contribution of the active-site metal cation to the catalytic activity and to the conformational stability of phosphotriesterase: Temperature- and pH-dependence

Biochemical Journal

Volumn 380, Issue 3, 2004, Pages 627-633

  Rochu, Daniel ^a   Viguié, Nathalie ^a   Renault, Frédérique ^a   Crouzier, David ^a   Froment, Marie Thérèse ^a   Masson, Patrick ^a  

^a CENTRE DE RECHERCHES   (France)

Author keywords

Capillary electrophoresis; Metalloenzyme; Phosphotriesterase; Protein stability; Thermal unfolding

Indexed keywords

CATALYSTS; DETOXIFICATION; ELECTROPHORESIS; MUTAGENESIS; PESTICIDES; PH EFFECTS; POSITIVE IONS; REACTION KINETICS; THERMODYNAMIC STABILITY; TITRATION;

CONFORMATIONAL STABILITY; ISOELECTRIC FOCUSING; NERVE AGENTS; THERMAL DENATURATION;

TRANSITION METALS;

CADMIUM; COBALT; ISOPROTEIN; METAL ION; PHOSPHODIESTERASE; TRANSITION ELEMENT; ZINC;

ARTICLE; CAPILLARY ELECTROPHORESIS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME ENGINEERING; ENZYME INACTIVATION; ENZYME STABILITY; ISOELECTRIC FOCUSING; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STABILITY; STEADY STATE; SUBSTITUTION REACTION; TEMPERATURE DEPENDENCE; THERMOSTABILITY; TITRIMETRY;

BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CATIONS, DIVALENT; ELECTROPHORESIS, CAPILLARY; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; ISOELECTRIC POINT; ISOENZYMES; METALS; PHOSPHORIC TRIESTER HYDROLASES; PROTEIN CONFORMATION; PSEUDOMONAS; TEMPERATURE;

EID: 3042819076     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031861     Document Type: Article

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