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Title: Inhibitors and inactivators of serine proteases

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5332718

Inactivation of chymotrypsin by 3-benzyl-6-chloro-2-pyrone results in the formation of a covalent adduct in which the ..gamma..-oxygen of serine-195 is covalently attached to C-1 of (Z)-2-benzyl-pentenedioic acid. The carboxylate group of the inhibitor forms a salt bridge with histidine-57 and this prevents access of water to the active site. The structure was established through NMR and x-ray diffraction analysis at 1.9 A resolution. Fluoromethyl-ketones are inhibitors of chymotrypsin and pancreatic elastase. /sup 19/F NMR shows that the carbonyl-carbon of the enzyme bound inhibitor is tetrahedral, most probably, due to adduct formation with the active site serine. The efficacy of these inhibitors increases with the number of fluorine substituents and with increasing length of the peptide. For the elastase inhibitor AcProAlaCF/sub 3/ K/sub i/ = 3 x 10/sup -3/ M and for AcAlaAlaProAlaCF/sub 3/ K/sub i/ = 0.34 x 10/sup -6/ M. For the tetrapeptide k/sub on/ = 290 s/sup -1/ M/sup -1/. The lowering of K/sub i/ concomitant with structural change correlates well with the variation in V/K for the corresponding substrates. AcLeuPheCFH/sub 2/ is a weak inhibitor of chymotrypsin, K/sub i/ = 0.28 x 10/sup -3/ M, which irreversibly inactivates the enzyme by alkylating a histidine.

Research Organization:
Brandeis, Univ., Waltham, MA
OSTI ID:
5332718
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English