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

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

Author Oliva, Maria Luiza Vilela Autor UNIFESP Google Scholar
Ferreira, Rodrigo da Silva Autor UNIFESP Google Scholar
Ferreira, Joana Gasperazzo Autor UNIFESP Google Scholar
Paula, Claudia Alessandra Andrade de Autor UNIFESP Google Scholar
Salas, Carlos E. Google Scholar
Sampaio, Misako Uemura Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade Federal de Minas Gerais (UFMG)
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
Language English
Sponsor Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Date 2011-08-01
Published in Current Protein & Peptide Science. Sharjah: Bentham Science Publ Ltd, v. 12, n. 5, p. 348-357, 2011.
ISSN 1389-2037 (Sherpa/Romeo, impact factor)
Publisher Bentham Science Publ Ltd
Extent 348-357
Origin http://dx.doi.org/10.2174/138920311796391061
Access rights Closed access
Type Review
Web of Science ID WOS:000294414500003
URI http://repositorio.unifesp.br/11600/43469

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