Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions

Francesco Bellia; Valeria Lanza; Ikhlas Mohamed Mohamud Ahmed; Sara Garcia-Vinuales; Eva Veiss; Mariaconcetta Arizzi; Damiano Calcagno; Danilo Milardi; Giuseppe Grasso

doi:10.1039/C8MT00288F

Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions†

Francesco Bellia,^a Valeria Lanza,^a Ikhlas Mohamed Mohamud Ahmed,

^a Sara Garcia-Vinuales,^a Eva Veiss,^b Mariaconcetta Arizzi,^b Damiano Calcagno,^b Danilo Milardi

*^a and Giuseppe Grasso

*^b

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* Corresponding authors

^a Institute of Biostructures and Bioimaging, National Research Council, Catania, Italy
E-mail: danilo.milardi@cnr.it

^b Department of Chemistry, University of Catania, Catania, Italy
E-mail: grassog@unict.it

Abstract

Four specifically designed IDE mutants have been used to unveil the molecular basis of peptidase versus E1-like activity of the enzyme. We have found that physiological concentrations of copper(II) ions inhibit the proteolytic activity of the enzyme towards small and large substrates but have no effect on the E1-like activity of the enzyme.

Metallomics

Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions†

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