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
-
3.4.14.1
-
cathepsins
-
lysosomal
-
periodontitis
-
palmoplantar
-
hyperkeratosis
-
papain
-
papillon-lefevre
-
keratoderma
-
teeth
-
elastase
-
granzyme
-
exopeptidase
-
proteinases
-
cystatins
-
dentition
-
aminopeptidases
-
granule-associated
-
chymase
-
synthesis
-
proenzyme
-
medicine
-
propeptide
-
papain-like
-
keratosis
-
ficin
-
ergic-53
-
nutrition
-
palmar
-
analysis
- 3.4.14.1
- cathepsins
- lysosomal
- periodontitis
-
palmoplantar
-
hyperkeratosis
- papain
- papillon-lefevre
- keratoderma
-
teeth
- elastase
-
granzyme
-
exopeptidase
- proteinases
- cystatins
-
dentition
- aminopeptidases
-
granule-associated
- chymase
- synthesis
- proenzyme
- medicine
- propeptide
-
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
results (
results (Substrates Products
Substrates Products on EC 3.4.14.1 - dipeptidyl-peptidase I
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SUBSTRATE 
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
5 Gly-Arg-2-naphthylamide + 5 H2O
(Gly-Arg-)5-2-naphthylamide + 4 2-naphthylamine
-
polymerization
polymers up to (Gly-Arg-)5-2-naphthylamide
?
alpha-Asp-Arg-2-naphthylamide + H2O
alpha-Asp-Arg + 2-naphthylamine
-
-
-
-
?
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gln-Tyr(3-NO2)-NH2 + H2O
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala + Ser-Gln-Tyr(3-NO2)-NH2
specific and selective substrate
-
-
?
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2)-NH2 + H2O
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala + Ser-Gly-Tyr(3-NO2)-NH2
specific and selective substrate
-
-
?
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Tyr(3-NO2)-NH2 + H2O
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala + Ser-Tyr(3-NO2)-NH2
-
-
-
?
beta-(2-thienyl)Ala-Phe-7-amido-4-methylcoumarin + H2O
beta-(2-thienyl)Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
glucagon + H2O
His-Ser + Thr-Phe + Thr-Ser + Asp-Tyr + Ser-Lys + Tyr-Leu + Asp-Ser + ?
-
-
further degradation of the hormone is prevented by the appearance of the NH2-terminal Arg
?
Gly-(beta-phenyl)-L-lactic acid methyl ester + H2O
Gly-(beta-phenyl)-L-lactic acid + methanol
-
-
-
?
Gly-Arg-4-methoxy-2-naphthylamide + H2O
Gly-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
2-naphthylamine + Gly-Phe
-
assay at 37°C, pH 5.5, reaction stopped by addition of glycine-NaOH
-
-
?
Gly-Phe-4-methoxy-2-naphthylamide + H2O
Gly-Phe + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Tyr(3'NO2)-Gly-Pro-Pro-Lys(epsilon-(2-aminobenzoyl))-Gly + H2O
Gly-Tyr(3'NO2) + Gly-Pro-Pro-Lys(epsilon-(2-aminobenzoyl))-Gly
-
-
-
-
?
glycine-L-alanine-4-methoxy-beta-naphthylamide + H2O
glycine-L-alanine + 4-methoxy-beta-naphthylamine
-
56.7% of the activity with glycine-L-arginine-4-methoxy-beta-naphthylamide
-
-
?
glycine-L-arginine-4-methoxy-beta-naphthylamide + H2O
glycine-L-arginine + 4-methoxy-beta-naphthylamine
-
-
-
-
?
glycine-L-arginine-beta-naphthylamide + H2O
glycine-L-arginine + beta-naphthylamine
-
90.1% of the activity with glycine-L-arginine-4-methoxy-beta-naphthylamide
-
-
?
glycine-L-phenylalanine-beta-naphthylamide + H2O
glycine-L-phenylalanine + beta-naphthylamine
-
96.5% of the activity with glycine-L-arginine-4-methoxy-beta-naphthylamide
-
-
?
glycine-L-phenylalanine-p-nitroanilide + H2O
glycine-L-phenylalanine + p-nitroaniline
-
-
-
?
H2N-Abu-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
H2N-Abu-Homo-Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
H2N-fulleroproline-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
H2N-fulleroproline-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
H2N-Leu-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
H2N-Nva-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
L-phenylalanine-L-arginine-4-methoxy-beta-naphthylamide + H2O
L-phenylalanine-L-arginine + 4-methoxy-beta-naphthylamine
-
87.2% of the activity with glycine-L-arginine-4-methoxy-beta-naphthylamide
-
-
?
L-Ser-L-Tyr-7-amido-4-methylcoumarin + H2O
L-Ser-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-enkephalin + H2O
Tyr-Gly + Gly-Phe-Leu
-
i.e. Tyr-Gly-Gly-Phe-Leu
no further degradation of the tripeptide
?
Met-enkephalin + H2O
Tyr-Gly + Gly-Phe-Met
-
-
further degradation of Gly-Phe-Met to Gly-Phe + Met
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
-
-
tri-alanine is resistant to further breakdown
?
Pro-Arg-7-amido-4-methylcoumarin + H2O
Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
secretin + H2O
His-Ser + Asp-Gly + Thr-Phe + Thr-Ser + Glu-Leu + Ser-Arg + Leu-Arg + Asp-Ser + Ala-Arg + Leu-Gln + ?
-
-
further degradation of the hormone is prevented by the appearance of the NH2-terminal Arg
?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
thyroglobulin + H2O
?
-
-
enzyme removes up to 12 amino acids from the N-terminus of porcine thyroglobulin, including a dipeptide with thyroxin on position 5. The newly formed N-terminus, Arg-Pro-, is not hydrolysed further
-
?
4 Gly-L-Phe-NH2 + 4 H2O
Gly-Phe-Gly-Phe-Gly-Phe-Gly-Phe-NH2 + 3 NH3
-
polymerization
-
-
?
4 Gly-L-Phe-NH2 + 4 H2O
Gly-Phe-Gly-Phe-Gly-Phe-Gly-Phe-NH2 + 3 NH3
-
transamidatin
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
-
-
further degradation of corticotropin is prevented by a penultimate prolyl residue
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
-
succesive removal of dipeptides from the NH2 terminus
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
-
-
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
-
succesive removal of dipeptides from the NH2 terminus
-
-
?
Gly-Arg-2-naphthylamide + H2O
Gly-Arg + 2-naphthylamine
-
-
-
-
?
Gly-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Phe-7-amido-4-methylcoumarin + H2O
Gly-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Phe-7-amido-4-methylcoumarin + H2O
Gly-Phe + 7-amino-4-methylcoumarin
-
assay at pH 5.5, 37°C
-
-
?
additional information
?
-
-
no activity with peptides involving Pro as the third residue
-
-
?
additional information
?
-
-
inability to remove dipeptides with an N-terminal Arg or Lys, and inability to cleave the bond on either side of Pro
-
-
?
additional information
?
-
-
the enzyme may be involved in mediating cell-cell intercommunication in Dictyostelium and in controlling cell movement during morphogenesis
-
-
?
additional information
?
-
-
substrates with blocked amino-termini, with Pro at the P1 position, Arg at the P2, or containing only single amino acids are not hydrolyzed
-
-
?
additional information
?
-
-
modest preference for peptides with nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
,n high affinity interaction between heparin and prochymase allows the 2 residue propeptide to be cleaved by dipeptidylpeptidase I
-
-
?
additional information
?
-
enzyme is involved in intracellular degradation of proteins
-
-
?
additional information
?
-
-
enzyme is involved in intracellular degradation of proteins
-
-
?
additional information
?
-
-
together with other proteases the enzyme plays a major part in degradation of ingested substances after endocytosis and in tissue damage following enzyme release
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
cathepsin C gene is a direct target for induction by interferon regulatory factor-8
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is involved in the final stages of oocyte maturation in crustacean species
-
-
?
additional information
?
-
-
dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation
-
-
?
additional information
?
-
-
inability to remove dipeptides with an N-terminal Arg or Lys, and inability to cleave the bond on either side of Pro
-
-
?
additional information
?
-
-
inability to remove dipeptides with an N-terminal Arg or Lys, and inability to cleave the bond on either side of Pro
-
-
?
additional information
?
-
-
the most favorable substrates are tripeptides or dipeptide amides that have as the NH2-terminal group a small residue and that have the aliphatic residue leucine at the penultimate position
-
-
?
additional information
?
-
-
the enzyme is involved in lysosomal protein degradation
-
-
?
additional information
?
-
-
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
-
-
?
