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. 1993 Dec 20;336(1):65-9.
doi: 10.1016/0014-5793(93)81610-c.

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

J W Creemers  1 , P J Groot Kormelink, A J Roebroek, K Nakayama, W J Van de Ven
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Free article

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

J W Creemers et al. FEBS Lett. .
Free article

Abstract

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.

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