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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4.

Proprotein processing activity of the Kex2-like mammalian endoprotease PACE4 and its cleavage selectivity for sites with basic amino acid residues were determined. Using a recombinant vaccinia virus-based expression system, PACE4 was expressed in pig kidney PK(15) cells and, like two other Kex2-like endoproteases furin and PC6A, shown to correctly process the precursor of von Willebrand factor (pro-vWF). Furthermore, characteristics of the cleavage site selectivity of PACE4 were compared to those of furin and PC6A using the vWF cleavage site mutants vWFR-1G, vWFK-2A, and vWFR-4A as substrates. Cleavage site selectivity of PACE4 and PC6A appeared to be similar but they differed from that of furin.[1]

References

  1. Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4. Creemers, J.W., Groot Kormelink, P.J., Roebroek, A.J., Nakayama, K., Van de Ven, W.J. FEBS Lett. (1993) [Pubmed]
 
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