Abstract
Protein degradation is essential for the life and death of every cell. Proteins are broken down to their constitutive amino acids by a succession of peptidases, both in lysosomes and in the cytosol. Tripeptidyl-peptidases I and II are enzymes that can 'count to three' and release N-terminal tripeptides from oligopeptides generated by different endopeptidases. The tripeptides are then degraded by other exopeptidases to release amino acids and dipeptides. Mutations in tripeptidyl-peptidase I have recently been associated with a lysosomal storage disease, late infantile neuronal ceroid lipofuscinosis.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Aminopeptidases
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Cysteine Endopeptidases / metabolism
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Cytosol / metabolism
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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Endopeptidases / genetics
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Endopeptidases / metabolism*
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Humans
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Lysosomal Storage Diseases / metabolism
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Lysosomes / metabolism*
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Multienzyme Complexes / metabolism
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Neuronal Ceroid-Lipofuscinoses / metabolism
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Peptides / metabolism
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Proteasome Endopeptidase Complex
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Proteins / metabolism*
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Serine Endopeptidases / metabolism
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Serine Proteases
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Tripeptidyl-Peptidase 1
Substances
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Multienzyme Complexes
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Peptides
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Proteins
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Tripeptidyl-Peptidase 1
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Endopeptidases
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Serine Proteases
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Aminopeptidases
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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tripeptidyl-peptidase 2
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TPP1 protein, human
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Serine Endopeptidases
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex