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Article

N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.

The Journal of biological chemistry - 26 Mar 2004

Wujek Peter, Kida Elizabeth, Walus Marius, Wisniewski Krystyna E, Golabek Adam A

Abstract excerpt

Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides. Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis. Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443. To analyze the role of N-glycosylation in the function of the enzyme,...

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Identifiers

PMID: 14702339
DOI: 10.1074/jbc.M313173200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.PMID 14702339Read ↗

Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.Semantic proximity Read ↗

Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.Semantic proximity Read ↗

Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.Semantic proximity Read ↗

Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

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Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.Semantic proximity Read ↗

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