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Expression and characterization of a cytosolic glucose 6 phosphate dehydrogenase isoform from barley (Hordeum vulgare) roots.
Castiglia, Daniela; Cardi, Manuela; Landi, Simone; Cafasso, Donata; Esposito, Sergio.
Afiliación
  • Castiglia D; Università di Napoli "Federico II", Dipartimento di Biologia, Via Cinthia, 6, I-80126 Napoli, Italy; CNR-IBBR (Istituto di Bioscienze e BioRisorse), Via Università, 133, I-80055 Portici (NA), Italy(1).
  • Cardi M; Università di Napoli "Federico II", Dipartimento di Biologia, Via Cinthia, 6, I-80126 Napoli, Italy.
  • Landi S; CNR-IBBR (Istituto di Bioscienze e BioRisorse), Via Università, 133, I-80055 Portici (NA), Italy(1).
  • Cafasso D; Università di Napoli "Federico II", Dipartimento di Biologia, Via Cinthia, 6, I-80126 Napoli, Italy.
  • Esposito S; Università di Napoli "Federico II", Dipartimento di Biologia, Via Cinthia, 6, I-80126 Napoli, Italy. Electronic address: sergio.esposito@unina.it.
Protein Expr Purif ; 112: 8-14, 2015 Aug.
Article en En | MEDLINE | ID: mdl-25888782
In plant cells, glucose 6 phosphate dehydrogenase (G6PDH-EC 1.1.1.49) regulates the oxidative pentose phosphate pathway (OPPP), a metabolic route involved in the production of NADPH for various biosynthetic processes and stress response. In this study, we report the overexpression of a cytosolic G6PDH isoform from barley (Hordeum vulgare) roots in bacteria, and the biochemical characterization of the purified recombinant enzyme (HvCy-G6PDH). A full-length cDNA coding for a cytosolic isoform of G6PDH was isolated, and the sequence was cloned into pET3d vector; the protein was overexpressed in Escherichia coli BL21 (DE3) and purified by anion exchange and affinity chromatography. The kinetic properties were calculated: the recombinant HvCy-G6PDH showed KMs and KINADPH comparable to those observed for the enzyme purified from barley roots; moreover, the analysis of NADPH inhibition suggested a competitive mechanism. Therefore, this enzyme could be utilised for the structural and regulatory characterization of this isoform in higher plants.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hordeum / Clonación Molecular / Raíces de Plantas / Glucosafosfato Deshidrogenasa / NADP Idioma: En Revista: Protein Expr Purif Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hordeum / Clonación Molecular / Raíces de Plantas / Glucosafosfato Deshidrogenasa / NADP Idioma: En Revista: Protein Expr Purif Asunto de la revista: BIOLOGIA MOLECULAR Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos