Abstract
Propynyl, hexynyl and t-butylethynyl diethyl phosphates were found to be very powerful covalent inhibitors of serine enzymes. Esterases were inhibited with second-order rate constants of 10(7)-10(8) m(-1) min(-1). Most proteases were inhibited with a rate constant of 10(4)-10(5) M(-1) min(-1). By inhibiting chymotrypsin with (3-14C)-1-propynyl diethyl phosphate, it was established that inhibition was caused by binding of the phosphate group to the enzyme active site.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Dehydrogenase / antagonists & inhibitors
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Binding Sites
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Cholinesterase Reactivators / pharmacology
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Kinetics
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L-Lactate Dehydrogenase / antagonists & inhibitors
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Muramidase / antagonists & inhibitors
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Organophosphorus Compounds / pharmacology*
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Serine Proteinase Inhibitors / pharmacology*
Substances
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Cholinesterase Reactivators
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Organophosphorus Compounds
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Serine Proteinase Inhibitors
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L-Lactate Dehydrogenase
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Aldehyde Dehydrogenase
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Muramidase