Chemical replacement of P1' serine residue at the second reactive site of soybean protease inhibitor C-II.
The P1' Ser(50) at the second reactive site of soybean protease inhibitor C-II was replaced with arginine to confirm the contribution of this residue to the inhibition. The Arg derivative had less trypsin inhibitory activity (Ki = 1 X 10(-7) M) than the Ser derivative (Ki = 2 X 10(-8) M), in contrast to the results obtained from studies on peanut protease inhibitor B-III reported in the previous paper (J. Biochem. 101, 723-728 (1987)). These results suggest that each Bowman-Birk type inhibitor has an amino acid at the P1' position inherently best suited to maintaining its inhibitory activity, and that serine is not unique for the P1' amino acid in Bowman-Birk type inhibitors.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D011487:Protein Conformation; D012694:Serine / Q000032:analysis*; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000032:analysis* / Q000494:pharmacology; D014361:Trypsin Inhibitors / Q000032:analysis*
D000596:Amino Acids; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014361:Trypsin Inhibitors; D012694:Serine