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Here we report a detailed analysis of magnesium (Mg 2+ ) ion effects on furin hydrolysis of fluorescent resonance energy transfer decapeptide substrates derived from canonical R-X-K/R-R furin cleavage motifs within certain viral envelope glycoproteins and eukaryotic proproteins. Using virus-derived sequences a selective activation of furin by Mg 2+  ions was observed as a result of cooperativity between furin subsites. Furin hydrolysis of the peptides Abz-SRRHKR↓FAGV-Q-EDDnp (from measles virus fusion protein F o ) and Abz-RERRRKKR↓GLFG-Q-EDDnp (from Asian avian influenza A, H5N1) was activated between 60- and 80-fold by MgCl 2 . It appears that virus envelope glycoprotein mutations have been selected to increase their susceptibility to furin within cells, a location where Mg 2+  is present in adequate concentrations for activation. Both the pH profile of furin and its intrinsic fluorescence were modified by Mg 2+  ions, which bind to furin with a  K  d  value of 1.1 m m .

biological chemistry

Effects of magnesium ions on recombinant human furin: selective activation of hydrolytic activity upon substrates derived from virus envelope glycoprotein