Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
H Steiner, M Kostka, H Romig, G Basset, B Pesold… - Nature Cell …, 2000 - nature.com
H Steiner, M Kostka, H Romig, G Basset, B Pesold, J Hardy, A Capell, L Meyn, ML Grim…
Nature Cell Biology, 2000•nature.comEndoproteolysis 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.
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.
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.
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