title: Structural basis for specificity of propeptide-enzyme interaction in barley C1A cysteine peptidases.
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.
authors.affiliation: Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid, Pozuelo de Alarcón, Madrid, Spain.
authors.forename: Inés
authors.initials: I
authors.lastname: Cambra
authors.forename: David
authors.initials: D
authors.lastname: Hernández
authors.forename: Isabel
authors.initials: I
authors.lastname: Diaz
authors.forename: Manuel
authors.initials: M
authors.lastname: Martinez
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002401:Cathepsin B; D002417:Cattle; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D001467:Hordeum / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data
chemical_list: D004792:Enzyme Precursors; D003546:Cysteine Endopeptidases; D002401:Cathepsin B