Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type

  • Biochemistry (Mosc). 1999 Nov;64(11):1244-9.
I P Gladysheva  1 ,  T S Zamolodchikova ,  E A Sokolova ,  N I Larionova
Affiliations
  • 1. School of Chemistry, Lomonosov Moscow State University, Moscow 119899, Russia.
PMID: 10611528
Abstract

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.

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