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dc.contributor.author
Lufrano, Daniela
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dc.contributor.author
Cotabarren, Juliana
dc.contributor.author
Garcia Pardo, Javier
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Fernandez Alvarez, Roberto
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Tort, Olivia
dc.contributor.author
Tanco, Sebastián
dc.contributor.author
Avilés, Francesc Xavier
dc.contributor.author
Lorenzo, Julia
dc.contributor.author
Obregon, Walter David
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dc.date.available
2018-06-26T16:16:15Z
dc.date.issued
2015-12
dc.identifier.citation
Lufrano, Daniela; Cotabarren, Juliana; Garcia Pardo, Javier; Fernandez Alvarez, Roberto; Tort, Olivia; et al.; Biochemical characterization of a novel carboxypeptidase inhibitor from a variety of Andean potatoes; Pergamon-Elsevier Science Ltd; Phytochemistry; 120; 12-2015; 36-45
dc.identifier.issn
0031-9422
dc.identifier.uri
http://hdl.handle.net/11336/50079
dc.description.abstract
Natural protease inhibitors of metallocarboxypeptidases are rarely reported. In this work, the cloning, expression and characterization of a proteinaceous inhibitor of the A/B-type metallocarboxypeptidases, naturally occurring in tubers of Solanum tuberosum, subsp. andigenum cv. Imilla morada, are described. The obtained cDNA encoded a polypeptide of 80 residues, which displayed the features of metallocarboxypeptidase inhibitor precursors from the Potato Carboxypeptidase Inhibitor (PCI) family. The mature polypeptide (39 residues) was named imaPCI and in comparison with the prototype molecule of the family (PCI from S. tuberosum subsp. tuberosum), its sequence showed one difference at its N-terminus and another three located at the secondary binding site, a region described to contribute to the stabilization of the complex inhibitor-target enzyme. In order to gain insights into the relevance of the secondary binding site in nature, a recombinant form of imaPCI (rimaPCI) having only differences at the secondary binding site with respect to recombinant PCI (rPCI) was cloned and expressed in Escherichia coli. The rimaPCI exhibited a molecular mass of 4234.8 Da by MALDI-TOF/MS. It displayed potent inhibitory activity towards A/B-type carboxypeptidases (with a Ki in the nanomolar range), albeit 2-4-fold lower inhibitory capacity compared to its counterpart rPCI. This result is in agreement with our bioinformatic analysis, which showed that the main interaction established between the secondary binding site of rPCI and the bovine carboxypeptidase A is likely lost in the case of rimaPCI. These observations reinforce the importance of the secondary binding site of PCI-family members on inhibitory effects towards A/B-type metallocarboxypeptidases. Furthermore, as a simple proof of concept of its applicability in biotechnology and biomedicine, the ability of rimaPCI to protect human epidermal growth factor from C-terminal cleavage and inactivation by carboxypeptidases A and B was demonstrated.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Pergamon-Elsevier Science Ltd
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Andean Potatoes
dc.subject
Plant Protease Inhibitor
dc.subject
Potato Carboxypeptidase Inhibitor
dc.subject
Secondary Binding Site
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Solanaceae
dc.subject
Solanum Tuberosum
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Biochemical characterization of a novel carboxypeptidase inhibitor from a variety of Andean potatoes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-26T13:45:13Z
dc.journal.volume
120
dc.journal.pagination
36-45
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Lufrano, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Cotabarren, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
dc.description.fil
Fil: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Fernandez Alvarez, Roberto. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Tort, Olivia. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Tanco, Sebastián. Universitat Autònoma de Barcelona; España. University of Ghent; Bélgica
dc.description.fil
Fil: Avilés, Francesc Xavier. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Lorenzo, Julia. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
dc.journal.title
Phytochemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0031942215300893
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.phytochem.2015.09.010
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