Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type.
The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman--Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase was shown to interact only with the antichymotrypsin site (Leu-Ser) of BBI, whereas the antitrypsin site (Lys-Ser) of the inhibitor appeared to be vacant and capable of interaction with trypsin. The inhibition constants of duodenase by BBI, the BBI--trypsin complex, and STI were 4, 400, and 40 nM, respectively.
Gladysheva
I P
IP
School of Chemistry, Lomonosov Moscow State University, Moscow 119899, Russia.
Zamolodchikova
T S
TS
Sokolova
E A
EA
Larionova
N I
NI
D001667:Binding, Competitive; D007700:Kinetics; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000378:metabolism*; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000378:metabolism*
D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014360:Trypsin Inhibitor, Kunitz Soybean; D012697:Serine Endopeptidases; C078261:duodenase; D014357:Trypsin