RT Journal Article
T1 Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
A1 Martinez, Manuel
A1 Díaz Mendoza, María Mercedes
A1 Carrillo, Laura
A1 Diaz, Isabel
AB 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.
PB FEBS Press
SN 0014-5793
YR 2007
FD 2007
LK https://hdl.handle.net/20.500.14352/94326
UL https://hdl.handle.net/20.500.14352/94326
LA eng
NO 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.
NO 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.
NO Ministerio de Educación y Ciencia (España)
NO Universidad Politécnica de Madrid
DS Docta Complutense
RD 8 abr 2025