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oai:docta.ucm.es:20.500.14352/943262024-09-12T23:52:55Zcom_20.500.14352_14col_20.500.14352_15

Martinez, Manuel Díaz Mendoza, María Mercedes Carrillo, Laura Diaz, Isabel 2024-01-22T11:35:59Z 2024-01-22T11:35:59Z 2007 Martinez, Manuel, et al. «Carboxy Terminal Extended Phytocystatins Are Bifunctional Inhibitors of Papain and Legumain Cysteine Proteinases». FEBS Letters, vol. 581, n.o 16, junio de 2007, pp. 2914-18. https://doi.org/10.1016/j.febslet.2007.05.042. 0014-5793 10.1016/j.febslet.2007.05.042 https://hdl.handle.net/20.500.14352/94326 1873-3468 https://doi.org/10.1016/j.febslet.2007.05.042 Plant legumains are cysteine proteinases putatively involved in processing endogenous proteins. Phytocystatins (PhyCys) have been described as plant inhibitors of papain-like cysteine proteinases. Some PhyCys contain a carboxy terminal extension with an amino acid motif (SNSL) similar to that involved in the inhibition of legumain-like proteins by human cystatins. The role of these carboxy terminal extended PhyCys as inhibitors of legumain-like cysteine proteinases is here shown by in vitro inhibition of human legumain and legumain-like activities from barley extracts. Moreover, site-directed mutagenesis has demonstrated that the asparagine of the SNSL motif is essential in this inhibition. We prove for first time the existence of legumain inhibitors in plants. eng open access Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases journal article