Abstract
Endoproteolysis of beta-amyloid precursor protein (betaAPP) 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid beta-Peptides / metabolism
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Amyloid beta-Protein Precursor / genetics
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Amyloid beta-Protein Precursor / metabolism
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Animals
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Aspartic Acid Endopeptidases / genetics
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Aspartic Acid Endopeptidases / metabolism*
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Aspartic Acid Endopeptidases / physiology
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Bacteria / enzymology
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Bacterial Proteins / metabolism
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Cell Line
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Conserved Sequence
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Endopeptidases*
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Glycine / genetics
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Glycine / metabolism*
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Humans
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Membrane Proteins / physiology
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Mutagenesis, Site-Directed
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Peptide Fragments / metabolism
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Presenilin-1
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Presenilin-2
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Receptors, Notch
Substances
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Amyloid beta-Peptides
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Amyloid beta-Protein Precursor
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Bacterial Proteins
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Membrane Proteins
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PSEN1 protein, human
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PSEN2 protein, human
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Peptide Fragments
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Presenilin-1
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Presenilin-2
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Receptors, Notch
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amyloid beta-protein (1-40)
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amyloid beta-protein (1-42)
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Endopeptidases
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prepilin peptidase protein, Bacteria
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Aspartic Acid Endopeptidases
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Glycine