Alkynyl phosphates are potent inhibitors of serine enzyme.
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.
Segal
D
D
Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Shalitin
C
C
Shalitin
Y
Y
Fischer
D R
DR
Stang
P J
PJ
D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors; D001665:Binding Sites; D002801:Cholinesterase Reactivators / Q000494:pharmacology; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors; D009113:Muramidase / Q000037:antagonists & inhibitors; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*
D002801:Cholinesterase Reactivators; D009943:Organophosphorus Compounds; D015842:Serine Proteinase Inhibitors; D007770:L-Lactate Dehydrogenase; D000444:Aldehyde Dehydrogenase; D009113:Muramidase