Author: ["Harald Steiner","Marcus Kostka","Helmut Romig","Gabriele Basset","Brigitte Pesold","John Hardy","Anja Capell","Liane Meyn","Melissa L. Grim","Ralf Baumeister","Katja Fechteler","Christian Haass"]
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Abstract
Endoproteolysis of β-amyloid precursor protein (βAPP) and Notch requires conserved aspartate residues in presenilins 1 and 2 (PS1 and PS2). Although PS1 and PS2 have therefore been proposed to be aspartyl proteases, no homology to other aspartyl proteases has been found. Here we identify homology between the presenilin active site and polytopic aspartyl proteases of bacterial origin, thus supporting the hypothesis that presenilins are novel aspartyl proteases.Cite this article
Steiner, H., Kostka, M., Romig, H. et al. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nat Cell Biol 2, 848–851 (2000). https://doi.org/10.1038/35041097 