Five BBI sequences, representing five different second reactive sites, were heterologously expressed in the yeast Pichia pastoris. The recombinant proteins demonstrated to be active against trypsin, while three of them were also active against chymotrypsin, and one against human leukocyte elastase. Comparative modeling and protein docking were used to further investigate interactions between two grass pea BBI isoforms and their target proteases. Thus two reliable 3D models have been proposed, representing two potential ternary complexes, each constituted of an inhibitor and its target enzymes. (C) 2012 Elsevier Masson SAS. All rights reserved.

Isolation and characterization of novel variants of BBI coding genes from the legume Lathyrus sativus

De Paola Domenico;Blanco Emanuela;Sonnante Gabriella
2012

Abstract

Five BBI sequences, representing five different second reactive sites, were heterologously expressed in the yeast Pichia pastoris. The recombinant proteins demonstrated to be active against trypsin, while three of them were also active against chymotrypsin, and one against human leukocyte elastase. Comparative modeling and protein docking were used to further investigate interactions between two grass pea BBI isoforms and their target proteases. Thus two reliable 3D models have been proposed, representing two potential ternary complexes, each constituted of an inhibitor and its target enzymes. (C) 2012 Elsevier Masson SAS. All rights reserved.
2012
Istituto di Bioscienze e Biorisorse
Grass pea
Bowman-Birk isoforms
Proteolytic enzymes
Reactive site
Recombinant proteins
Inhibitory properties
Comparative modeling
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/339179
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