title: Structural and functional properties of kunitz proteinase inhibitors from leguminosae: a mini review.
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.
authors.affiliation: Universidade Federal de São Paulo, Rua Três de Maio, 100, 04044-020 São Paulo, SP, Brazil. olivaml.bioq@epm.br
authors.forename: Maria Luiza Vilela
authors.initials: ML
authors.lastname: Oliva
authors.forename: Rodrigo da Silva
authors.initials: Rda S
authors.lastname: Ferreira
authors.forename: Joana Gasperazzo
authors.initials: JG
authors.lastname: Ferreira
authors.forename: Cláudia Alessandra Andrade
authors.initials: CA
authors.lastname: de Paula
authors.forename: Carlos E
authors.initials: CE
authors.lastname: Salas
authors.forename: Misako Uemura
authors.initials: MU
authors.lastname: Sampaio
mesh_terms: D020134:Catalytic Domain; D007887:Fabaceae / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C053865:Kunitz-type protease inhibitor, plant; D010455:Peptides; D010940:Plant Proteins