Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase

A putative covalent, α-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and w...

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Veröffentlicht in:	Biochemical and biophysical research communications 1994-02, Vol.198 (3), p.850-856
Hauptverfasser:	Hammock, B.D., Pinot, F., Beetham, J.K., Grant, D.F., Arand, M.E., Oesch, F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acylation Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Enzymes and enzyme inhibitors Epoxide Hydrolases - antagonists & inhibitors Epoxide Hydrolases - isolation & purification Epoxide Hydrolases - metabolism Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Hydrolases Kinetics Mice Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Tritium
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Beschreibung
Zusammenfassung:	A putative covalent, α-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and was increased by incubation under acidic conditions. The structure of the intermediate was supported by microchemical methods.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1994.1121