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Structural and Functional Properties of Kunitz Proteinase Inhibitors from Leguminosae: A Mini Review

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Seed proteins that inhibit proteinases are classified in families based on amino acid sequence similarity, nature of reactive site and mechanism of action, and are used as tools for investigating proteinases in physiological and pathological events. More recently, the plant Kunitz family of inhibitors with two disulphide bridges was enlarged with members containing variable number of cysteine residues, ranging from no cysteine at all to more than four residues. The characteristic of these proteins, as well the interactions with their target proteinases, are briefly discussed.







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Keywords: Chymotrypsin; Kunitz Proteinase Inhibitors; MEROPS; actin; amino acid sequence; cysteine residues; disulphide bridges; kunitz inhibitors; leguminosae; plant inhibitors; primary structure; proteolysis; reactive site; seed proteins; trypsin inhibitors

Document Type: Research Article

Publication date: 01 August 2011

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