Universidad de Zaragoza Repository

Resumen: The cytosolic form of phosphoenolpyruvate carboxykinase (PCK1) plays a regulatory role in gluconeogenesis and glyceroneogenesis. The role of the mitochondrial isoform (PCK2) remains unclear. We report the partial purification and kinetic and functional characterization of human PCK2. Kinetic properties of the enzyme are very similar to those of the cytosolic enzyme. PCK2 has an absolute requirement for Mn2+ ions for activity; Mg2+ ions reduce the Km for Mn2+ by about 60 fold. Its specificity constant is 100 fold larger for oxaloacetate than for phosphoenolpyruvate suggesting that oxaloacetate phosphorylation is the favored reaction in vivo. The enzyme possesses weak pyruvate kinase-like activity (kcat=2.7 s-1). When overexpressed in HEK293T cells it enhances strongly glucose and lipid production showing that it can play, as the cytosolic isoenzyme, an active role in glyceroneogenesis and gluconeogenesis.
Idioma: Inglés
DOI: 10.1016/j.bbrep.2016.06.007
Año: 2016
Publicado en: Biochemistry and Biophysics Reports 7 (2016), 124-129
ISSN: 2405-5808
Financiación: info:eu-repo/grantAgreement/ES/DGA/A51
Financiación: info:eu-repo/grantAgreement/ES/MEC/AGL2015–66177-R
Financiación: info:eu-repo/grantAgreement/ES/UZ/2015- BIO-01
Tipo y forma: Article (Published version)
Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)
Área (Departamento): Tecnología de Alimentos (Departamento de Producción Animal y Ciencia de los Alimentos)

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Exportado de SIDERAL (2016-07-12-14:49:32)

Este artículo se encuentra en las siguientes colecciones:
Articles > Artículos por área > Bioquímica y Biología Molecular
Articles > Artículos por área > Tecnología de Alimentos

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