The soybean trypsin inhibitor (Kunitz) family  is one of the numerous
families of proteinase inhibitors. It comprise plant proteins which have
inhibitory activity against serine proteinases from the trypsin and subtilisin
families, thiol proteinases and aspartic proteinases as well as some proteins
that are probably involved in seed storage. This family is currently known to
group the following proteins:
Trypsin inhibitors A, B, C, KTI1, and KTI2 from soybean.
Trypsin inhibitor DE3 from coral beans (Erythrina sp.).
Trypsin inhibitor DE5 from sandal bead tree.
Trypsin inhibitors 1A (WTI-1A), 1B (WTI-1B), and 2 (WTI-2) from goa bean.
Trypsin inhibitor from Acacia confusa.
Trypsin inhibitor from silk tree.
Chymotrypsin inhibitor 3 (WCI-3) from goa bean.
Cathepsin D inhibitors PDI and NDI from potato , which inhibit both
cathepsin D (aspartic proteinase) and trypsin.
α-amylase/subtilisin inhibitors from barley and wheat.
All these proteins contain from 170 to 200 amino acid residues and one or two
intrachain disulfide bonds. The best conserved region is found in their N-terminal section and is used as a signature pattern.
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