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

Maria      Luiza Vilela Oliva; Rodrigo      da Silva Ferreira; Joana      Gasperazzo Ferreira; Claudia      Alessandra Andrade de Paula; Carlos      E Salas; Misako      Uemura Sampaio

doi:10.2174/138920311796391061

Abstract

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.

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