Abstract
The pH-profiles for the trypsin-catalyzed hydrolysis of non-N-acylated α-amino substrates were found to be complex. The profile for L-lysine methyl ester gave two rate constants and four acid-base equilibrium constants. The rate constants arise from two different ionic forms (structures) of the site which are reactive. The pKa values calculated from the profile are indicative of an ionizable amino, imidazoyl and carboxyl group at the site, and the free α-amino group in the substrate. A negative heat of ionization was obtained for the group with the smallest pKa, which is kinetic evidence for the existence of a free carboxyl at or near the site.
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