Observatorio de I+D+i UPM

Memorias de investigación
Research Publications in journals:
Structural basis for specificity of propeptide-enzyme interaction in barley C1A cysteine peptidases
Year:2012
Research Areas
  • Natural sciences and health sciences,
  • Molecular biology
Information
Abstract
C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and non cognate enzymes. Besides, the propeptide from barley cathepsin B was not able to inhibit bovine cathepsin B. Modelling of their three-dimensional structures suggests that most propeptide inhibitory properties can be explained from the interaction between the propeptide and the mature cathepsin structures. Their potential use as biotechnological tools is discussed.
International
Si
JCR
Si
Title
Plos One
ISBN
1932-6203
Impact factor JCR
4,411
Impact info
Datos JCR del año 2010
Volume
5
10.1371/journal.pone.0037234
Journal number
From page
37234
To page
37240
Month
SIN MES
Ranking
Participants
  • Autor: Ines Cambra Marin (UPM)
  • Autor: David Hernandez (INIA)
  • Autor: M. Isabel Diaz Rodriguez (UPM)
  • Autor: Manuel Martinez Muñoz (UPM)
Research Group, Departaments and Institutes related
  • Creador: Grupo de Investigación: Interacciones moleculares planta-insecto.
  • Centro o Instituto I+D+i: Centro de Biotecnología y Genómica de Plantas, CBGP
  • Departamento: Biotecnología
S2i 2020 Observatorio de investigación @ UPM con la colaboración del Consejo Social UPM
Cofinanciación del MINECO en el marco del Programa INNCIDE 2011 (OTR-2011-0236)
Cofinanciación del MINECO en el marco del Programa INNPACTO (IPT-020000-2010-22)