All proteins, which amino acid sequences shown in Fig. 7, are the
inhibitors of trypsin and interact with the enzyme by "canonical"
substrate-like mechanism. Highly conservative motif PVRFI (positions
66e70), located in the large peptide loop formed by C49-C98,
is present in all inhibitor sequences. Biochemical studies of
proteinase inhibitors PKPI [6,18] have demonstrated earlier that
this motif represented the reactive site for trypsin inhibition, with
the arginine at position 68, being the active residue. These studies
have also revealed a disulfide bond between the cysteine residues
at position 49 and 98 (Fig. 7), which formed so-called “canonical”
loop, necessary for trypsin inhibition.We indicated that PKCI could
bind simultaneously both trypsin and chymotrypsin. So the second
reactive center for chymotrypsin inhibition must be present in its
molecule.
All proteins, which amino acid sequences shown in Fig. 7, are the
inhibitors of trypsin and interact with the enzyme by "canonical"
substrate-like mechanism. Highly conservative motif PVRFI (positions
66e70), located in the large peptide loop formed by C49-C98,
is present in all inhibitor sequences. Biochemical studies of
proteinase inhibitors PKPI [6,18] have demonstrated earlier that
this motif represented the reactive site for trypsin inhibition, with
the arginine at position 68, being the active residue. These studies
have also revealed a disulfide bond between the cysteine residues
at position 49 and 98 (Fig. 7), which formed so-called “canonical”
loop, necessary for trypsin inhibition.We indicated that PKCI could
bind simultaneously both trypsin and chymotrypsin. So the second
reactive center for chymotrypsin inhibition must be present in its
molecule.
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