3.4.14.1: dipeptidyl-peptidase I
This is an abbreviated version!
For detailed information about dipeptidyl-peptidase I, go to the full flat file.
Word Map on EC 3.4.14.1
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3.4.14.1
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cathepsins
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lysosomal
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periodontitis
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palmoplantar
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hyperkeratosis
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papain
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papillon-lefevre
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keratoderma
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teeth
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elastase
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granzyme
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exopeptidase
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proteinases
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cystatins
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dentition
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aminopeptidases
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granule-associated
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chymase
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synthesis
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proenzyme
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medicine
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propeptide
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papain-like
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keratosis
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ficin
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ergic-53
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nutrition
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palmar
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analysis
- 3.4.14.1
- cathepsins
- lysosomal
- periodontitis
-
palmoplantar
-
hyperkeratosis
- papain
- papillon-lefevre
- keratoderma
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teeth
- elastase
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granzyme
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exopeptidase
- proteinases
- cystatins
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dentition
- aminopeptidases
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granule-associated
- chymase
- synthesis
- proenzyme
- medicine
- propeptide
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papain-like
- keratosis
- ficin
-
ergic-53
- nutrition
-
palmar
- analysis
Reaction
Release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro =
Synonyms
Cat C, CATC, cathepsin C, cathepsin J, CTSC, DAP I, DDPI, dipeptide arylamidase I, dipeptidyl aminopeptidase I, dipeptidyl peptidase I, dipeptidyl peptidase I/cathepsin C, dipeptidyl transferase, DPAP1, DPAP2, DPP I, DPP-I, DPPI, EC 3.4.4.9, hDPPI, PBANKA_146070, PFL2290w
ECTree
3.4.14.1 dipeptidyl-peptidase IAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.14.1 - dipeptidyl-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
additional information
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the enzyme may be involved in mediating cell-cell intercommunication in Dictyostelium and in controlling cell movement during morphogenesis
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?
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,n high affinity interaction between heparin and prochymase allows the 2 residue propeptide to be cleaved by dipeptidylpeptidase I
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?
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enzyme is involved in intracellular degradation of proteins
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?
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enzyme is involved in intracellular degradation of proteins
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?
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together with other proteases the enzyme plays a major part in degradation of ingested substances after endocytosis and in tissue damage following enzyme release
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?
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the enzyme plays a requisite role in the post-translational processing and activation of members of the family of granule serine proteases expressed in bone marrow-derived effector cells
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?
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cathepsin C is required for granzyme B activation in unstimulated human natural killer cells. However in vitro activation of Papillon-Lefevre syndrome natural killer cells with interleukin-2 restores cytolytic function and granzyme B activity by a cathepsin C-independent mechanism
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?
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loss of DPPI activity in patients with Papillon-Lefevre syndrome is associated with severe reduction in the activity and stability of neutrophil-derived serine proteases
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?
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loss of DPPI activity in patients with Papillon-Lefevre syndrome is associated with severe reduction in the activity and stability of neutrophil-derived serine proteases
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?
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mutation in the cathepsin C gene are not the cause of all early-onset periodontal disease, and currently there is no evidence for the existence of a class of patients who do not have the full Papillon-Lefevre syndrome disease phenotype, but suffer isolated aggressive periodontitis because they have a low-activity cathepsin C gene variant
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?
additional information
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Papillon-Lefèvre syndrome is a rare autosomal recessive disease that involves severe periodontitis and hyperkeratosis of the hand palms and foot soles. Gene analysis of the CTSC gene in two families with Papillon-Lefèvre syndrome demonstrates that in the patients with Papillon-Lefèvre syndrome the absence of cathepsin C activity coincides with absence of activity of the serine proteinases elastase, cathepsin G and proteinase 3
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?
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the enzyme may play a role in converting the endogenous beta-MSH(5-22) to more potent peptides that regulate energy homeostasis in the hypothalamus
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?
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cathepsin C has a broad substrate specificity being able to hydrolyse out nearly every possible dipeptide unit, with the exception of those containing basic amino acids (Arg or Lys) at N-terminal position or Pro on either side of the scissile bond
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?
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the enzyme is involved in the processing of murine mast cell prochymase and procathepsin G, but does not process mast cell pro-carboxypeptidase A or protryptase
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?
additional information
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the enzyme plays a requisite role in the post-translational processing and activation of members of the family of granule serine proteases expressed in bone marrow-derived effector cells
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?
additional information
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cathepsin C gene is a direct target for induction by interferon regulatory factor-8
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?
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DPPI activates granule-associated serine proteases, several of which play important roles in host responses to bacterial infection. DPPI is a key regulator of survival from septic peritonitis
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?
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DPPI and neutrophils play a critical role in Sendai virus-induced asthma phenotype as a result of a DPPI-dependent neutrophil recruitment and cytokine response
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?
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the enzyme is involved in the final stages of oocyte maturation in crustacean species
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?
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dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation
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?
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the enzyme is involved in lysosomal protein degradation
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?
additional information
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cathepsin C may stimulate the sorting to the lysosome, at least in part, contributing to the degradation of intestinal alkaline phosphatase in Caco-2 cells, the propeptide of cathepsin C interacts with heat shock cognate protein 70 which is required for a step in chaperone-mediated lysosomal protein degradation
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