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Alkynyl phosphates are potent inhibitors of serine enzyme
Author(s) -
Segal Dina,
Shalitin Channa,
Shalitin Yechiel,
Fischer David R.,
Stang Peter J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00795-8
Subject(s) - serine , enzyme , chemistry , proteases , phosphate , chymotrypsin , propynyl , biochemistry , carbamoyl phosphate synthetase , covalent bond , stereochemistry , enzyme inhibitor , serine proteinase inhibitors , reaction rate constant , serine protease , kinetics , trypsin , protease , organic chemistry , physics , quantum mechanics
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‐ 14 C)‐1‐propynyl diethyl phosphate, it was established that inhibition was caused by binding of the phosphate group to the enzyme active site.