Rice bifunctional phytocystatin is a dual modulator of legumain and papain-like proteases

Author:

Christoff Ana Paula,Passaia Gisele,Salvati Caroline,Alves-Ferreira Márcio,Margis-Pinheiro Marcia,Margis RogerioORCID

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Publisher

Springer Science and Business Media LLC

Subject

Plant Science,Genetics,Agronomy and Crop Science,General Medicine

Reference70 articles.

1. Abe K, Emori Y, Kondo H, Arai S, Suzuki K (1988) The NH2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. J Biol Chem 263:7655–7659

2. Agrawal GK, Rakwal R, Tamogami S, Yonekura M, Akihiro K, Hikaru S (2002) Chitosan activates defense/stress response (s) in the leaves of Oryza sativa seedlings. Plant Physiol Biochem 40:1061–1069

3. Alvarez-Fernandez M, Barrett a J, Gerhartz B, Dando PM, Ni J, Abrahamson M (1999) Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site. J Biol Chem 274:19195–19203

4. Arai S, Watanabe H, Kondo H (1991) Papain activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln–Val–Val–Ala–Gly region conserved among cystatin superfamily members. J Biochem 109:294–298

5. Arai S, Matsumoto I, Emori Y, Abe K (2002) Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J Agric Food Chem 50:6612–6617

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