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Article

Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.

The Journal of biological chemistry - 28 Feb 2003

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

Abstract excerpt

Human tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysosomal serine protease that removes tripeptides from the free N termini of small polypeptides and also shows a minor endoprotease activity. Due to various naturally occurring mutations, an inherited deficiency of TPP I activity causes a fatal lysosomal storage disorder, classic late infantile neuronal ceroid lipofuscinosis (CLN2). In the present study,...

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PMID: 12488460
DOI: 10.1074/jbc.M211872200

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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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Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.PMID 12488460Read ↗

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

[Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation].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 ↗

Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.Semantic proximity Read ↗

Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders.Semantic proximity Read ↗

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

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

A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.Semantic proximity Read ↗

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

Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.Semantic proximity Read ↗

Role of N-glycosylation of human lysosomal phospholipase A2 for the formation of catalytically active enzyme.Semantic proximity Read ↗

Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.Semantic proximity Read ↗

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