Characterization of the zinc binding site of bacterial phosphotriesterase

The bacterial phosphotriesterase has been found to require a divalent cation for enzymatic activity. This enzyme catalyzes the detoxification of organophosphorus insecticides and nerve agents. In an Escherichia coli expression system significantly higher concentrations of active enzyme could be prod...

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Veröffentlicht in:	The Journal of biological chemistry 1992-07, Vol.267 (19), p.13278-13283
Hauptverfasser:	OMBURO, G. A, KUO, J. M, MULLINS, L. S, RAUSHEL, F. M
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Aryldialkylphosphatase binding Binding Sites Biological and medical sciences Catalysis Cations, Divalent characterization Chelating Agents Enzyme Activation Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology gene expression Hydrogen-Ion Concentration Hydrolases Kinetics Magnetic Resonance Spectroscopy Metals - metabolism Phosphoric Monoester Hydrolases - antagonists & inhibitors Phosphoric Monoester Hydrolases - metabolism phosphotriesterase Plasmids Pseudomonas diminuta sites Spectrophotometry, Atomic zinc Zinc - metabolism
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