3.4.14.9: tripeptidyl-peptidase I
This is an abbreviated version!
For detailed information about tripeptidyl-peptidase I, go to the full flat file.
Word Map on EC 3.4.14.9
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3.4.14.9
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infantile
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neurodegenerative
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lincl
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late-infantile
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lipofuscinoses
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batten
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curvilinear
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palmitoyl-protein
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pepstatin-insensitive
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cdc28p
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serine-carboxyl
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lipopigments
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molecular biology
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diagnostics
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medicine
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analysis
- 3.4.14.9
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infantile
- neurodegenerative
-
lincl
-
late-infantile
- lipofuscinoses
- batten
-
curvilinear
- palmitoyl-protein
-
pepstatin-insensitive
- cdc28p
-
serine-carboxyl
-
lipopigments
- molecular biology
- diagnostics
- medicine
- analysis
Reaction
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity =
Synonyms
aminopeptidase, tripeptidyl, I, AO090166000084, ceroid lipofuscinosis 2 protease, CLN2, CLN2 protein, CLN2p, EC 3.4.14.8, LPIC, lysosomal pepstatin insensitive protease, N-terminal tripeptidyl exopeptidase, SedB, SedC, SedD, sedolisin B, sedolisin C, sedolisin D, TPP I, TPP-I, Tpp1, TPP1F, TPPI, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl exopeptidase, tripeptidyl peptidase, tripeptidyl peptidase 1, tripeptidyl peptidase I, tripeptidyl peptidase-I, tripeptidyl-peptidase 1, tripeptidyl-peptidase I, TTP-I, v4-7
ECTree
3.4.14.9 tripeptidyl-peptidase IAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.14.9 - tripeptidyl-peptidase I
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid-beta + H2O
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AbetaCy3 peptides are released from the nanofibrils due to TPP1 activity
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additional information
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TPP1F is binding partner of Dictyostelium discoideum intracellular transmembrane protein GPHR, i.e. Golgi pH regulator. A region encompassing the DUF3735 (GPHR_N) domain of GPHR is responsible for the interaction. In TPP1F, the binding site is located in the prodomain of the protein. GPHR is present in subcellular membranous compartments reaching from endoplasmic reticulum membranes to membranes of the endo-lysosomal system
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additional information
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TPP1F is binding partner of Dictyostelium discoideum intracellular transmembrane protein GPHR, i.e. Golgi pH regulator. A region encompassing the DUF3735 (GPHR_N) domain of GPHR is responsible for the interaction. In TPP1F, the binding site is located in the prodomain of the protein. GPHR is present in subcellular membranous compartments reaching from endoplasmic reticulum membranes to membranes of the endo-lysosomal system
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additional information
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classical late infantile neuronal ceroid lipofuscinosis is an autosomal recessive disease caused by mutations in the CLN2 gene resulting in functional defects of the gene product tripeptidyl-peptidase I. This disease is associated with a progressive neurodegenerative course beginning at the age of two years with developmental stagnation, finally leading to a complete loss of motor function, vision and speech by the age of 10 years
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additional information
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elevated enzyme activity of tripeptidyl peptidase I and other lysosomal enzymes in Sjoegren's syndrome patients may play a role in tissue damage by accelerated breakdown of glycoproteins in lysosomes
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additional information
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TPP I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B. The inability of cells from patients with late-infantile neuronal ceroid lipofuscinosis (CNL2) to degrade neuromedin B and other neuropeptides may contribute to the pathogenesis of the disease
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additional information
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dipeptidyl-peptidase I cannot functionally compensate for the loss of tripeptidyl-peptidase I
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additional information
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an inherited deficiency of tripeptidyl peptidase I activity causes a fatal lysosomal storage disorder, classic late infantile neuronal ceroid lipofuscinosis, CLN2
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additional information
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exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils
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