The reaction of tris-(choline chloride) phosphate with eel cholinesterase
| Autor: | Joseph W. Amshey, George M. Steinberg |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
Decamethonium Compounds
Binding Competitive Medicinal chemistry Choline Chemical kinetics chemistry.chemical_compound Organophosphorus Compounds Reaction rate constant Animals Organic chemistry Cholinesterase Binding Sites Eels biology Organothiophosphorus Compounds General Medicine Tetraethylammonium Compounds Phosphate Acetylcholinesterase Dissociation constant Kinetics chemistry Potentiometry biology.protein Spectrophotometry Ultraviolet Cholinesterase Inhibitors Mathematics Tetraethylammonium bromide Protein Binding Choline chloride |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 284:157-163 |
| ISSN: | 0005-2744 |
| Popis: | Tris-(choline chloride) phosphate (TCCP) has been observed to slowly and progressively inhibit eel acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7). The kinetics of the inhibition reaction are consistent with a mechanism involving binding of the inhibitor to the enzyme followed by a rate-limiting irreversible reaction producing inactive enzyme. The dissociation constant of the enzyme-inhibitor complex and the rate constant of the inactivation reaction have been determined to be 0.036 M and 0.2 min−1, respectively. The quaternary reversible inhibitor tetraethylammonium bromide competes with TCCP for the reaction site. TCCP does not noticeably reduce the inhibition of enzyme by decamethonium bromide as does the structurally analogous compound flaxedil. The results obtained with TCCP are compared with available data on the relative enzymic reactivity of alkoxy and thiolo esters of phosphoric acid. |
| Databáze: | OpenAIRE |
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