Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions. Issue 2 (10th January 2019)

• Record Type: Journal Article
• Authors: Bellia, Francesco; Lanza, Valeria; Ahmed, Ikhlas Mohamed Mohamud; Garcia-Vinuales, Sara; Veiss, Eva; Arizzi, Mariaconcetta; Calcagno, Damiano; Milardi, Danilo; Grasso, Giuseppe
• Is Part Of: Metallomics. Volume 11:Issue 2(2019)
• Page Start: 278
• Page End: 281
• Publication Date: 2019-01-10
• Subjects: Metals -- Physiological effect -- Periodicals; 572.51
• DOI: 10.1039/c8mt00288f
• Languages: English
• ISSNs: 1756-5901

Abstract

Abstract : Four specifically designed IDE mutants have been used to unveil the molecular basis of peptidase versus E1-like activity of the enzyme. 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.