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Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases Martinez, Manuel Díaz Mendoza, María Mercedes Carrillo, Laura Diaz, Isabel 577.112 PhyCys Phytocystatins Barley Cystatin Cysteine proteinase inhibitor Legumain Papain Biotecnología 2306 Química Orgánica The financial support from the Ministerio de Educación y Ciencia (BFU2005-00603) and from the Universidad Politécnica de Madrid (AL07-PID-008) is gratefully acknowledged. 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. Ministerio de Educación y Ciencia (España) Universidad Politécnica de Madrid Depto. de Bioquímica y Biología Molecular Fac. de Ciencias Biológicas TRUE pub 2024-01-22T11:35:59Z 2024-01-22T11:35:59Z 2007 journal article VoR https://hdl.handle.net/20.500.14352/94326 0014-5793 10.1016/j.febslet.2007.05.042 1873-3468 eng 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. open access application/pdf FEBS Press