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- W990069178 abstract "Publisher Summary The use of the chloromethyl ketones Tos-PheCH 2 C1 (TPCK) and Tos-LysCH 2 C1 (TLCK) as specific reagents for chymotrypsin and trypsin, respectively, is one of the classic demonstrations of the value of affinity labels for enzyme studies. Subsequently, halomethyl ketones were used for characterization of functional groups and sequences in active sites, as probes of structure by providing labeled proteins that contain spectroscopic handles, in crystallographic studies of substrate binding sites, and in the study of the biological function of proteases. The reaction of a serine protease with most substrate-related haloketones probably first involves the formation of an enzyme inhibitor complex in which the inhibitor is recognized by specific interactions between the side chain of the P 1 amino acid residue and the S 1 or primary substrate binding site of the enzyme. Irreversible inhibition takes place within this complex by covalent bond formation between the active-site histidine residue and a methylene group of the inhibitor. This chapter discusses the synthesis, kinetics of reaction and applications of the reaction of serine proteases with halomethyl ketones." @default.
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- W990069178 date "1977-01-01" @default.
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- W990069178 title "[16] Reaction of serine proteases with halomethyl ketones" @default.
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- W990069178 doi "https://doi.org/10.1016/s0076-6879(77)46020-8" @default.
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