Information on EC 3.4.14.1 - dipeptidyl-peptidase I

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.14.1
-
RECOMMENDED NAME
GeneOntology No.
dipeptidyl-peptidase I
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, dipeptide
-
polymerization of dipeptide amides
-
-
-
-
transamidation
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CATC
-
-
cathepsin C
-
-
-
-
cathepsin C
-
-
cathepsin C
-
-
cathepsin C
B4XEV1
-
cathepsin C
-
-
cathepsin J
-
-
-
-
cathepsin J
-
-
cathepsin J
-
-
DAP I
-
-
-
-
DDPI
-
-
dipeptide arylamidase I
-
-
-
-
dipeptidyl aminopeptidase I
-
-
-
-
dipeptidyl aminopeptidase I
-
-
dipeptidyl aminopeptidase I
-
-
dipeptidyl peptidase I
-
-
dipeptidyl peptidase I
-
-
dipeptidyl peptidase I
-
-
dipeptidyl peptidase I/cathepsin C
-
-
dipeptidyl transferase
-
-
-
-
DPP I
-
-
DPP I
B4XEV1
-
DPP I
-
-
DPP-I
-
-
DPPI
-
-
-
-
DPPI
-
-
EC 3.4.4.9
-
-
formerly
-
hDPPI
-
-
CAS REGISTRY NUMBER
COMMENTARY
9032-68-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
under native conditions the enzyme may be aggregated with beta-hexosaminidase, beta-galactosidase and alpha-fucosidase
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
giant tiger prawn
UniProt
Manually annotated by BRENDA team
multiple forms: cathepsin CI, CII, and CIII are immunologically closely related if not identical
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
mutations in the cathepsin C gene result in an autosomal recessive disorder, Papillon-Lefevre syndrome
physiological function
-
may activate kallikrein-4 during enamel formation
physiological function
-
inhibition results in the formation of an immature trophozoite that leads to parasite death
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(H2N-Abu-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-fulleroproline-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-Leu-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-Leu-Leu)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-Nva-(4-phenyl)Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-Nva-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(H2N-Pro-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
(Pro-Arg)2-Rho + 2 H2O
rhodamine + 2 Pro-Arg
show the reaction diagram
-
-
-
-
?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Ala-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Ala-Arg-NH2 + H2O
Ala-Arg + NH3
show the reaction diagram
-
-
-
-
?
Ala-Leu-NH2 + H2O
Ala-Leu + NH3
show the reaction diagram
-
-
-
-
?
Ala-Tyr-NH2 + H2O
Ala-Tyr + NH3
show the reaction diagram
-
-
-
-
?
alpha-Asp-Arg-2-naphthylamide + H2O
alpha-Asp-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
alpha-D-Asp1-angiotensin II + H2O
?
show the reaction diagram
-
low reaction rate
-
-
?
Asn1-angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
beta-Asp1-angiotensin II + H2O
?
show the reaction diagram
-
low reaction rate
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
show the reaction diagram
-
-
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
show the reaction diagram
-
-
further degradation of corticotropin is prevented by a penultimate prolyl residue
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
show the reaction diagram
-
succesive removal of dipeptides from the NH2 terminus
-
-
?
Glu-His-2-naphthylamide + H2O
Glu-His + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
glucagon + H2O
His-Ser + Thr-Phe + Thr-Ser + Asp-Tyr + Ser-Lys + Tyr-Leu + Asp-Ser + ?
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
?
Gly-Ala-NH2 + H2O
Gly-Ala + NH3
show the reaction diagram
-
-
-
-
?
Gly-Arg-2-naphthylamide + H2O
Gly-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Arg-2-naphthylamide + H2O
Gly-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Arg-2-naphthylamide + H2O
(Gly-Arg-)5-2-naphthylamide + 2-naphthylamine
show the reaction diagram
-
polymerization
polymers up to (Gly-Arg-)5-2-naphthylamide
?
Gly-Arg-4-methoxy-2-naphthylamide + H2O
Gly-Arg + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
-
Gly-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Arg-NH2 + H2O
?
show the reaction diagram
-
polymerization
-
-
?
Gly-Arg-p-nitroanilide + H2O
Gly-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Gly-Gly-ethyl ester + H2O
Gly-Gly + ethanol
show the reaction diagram
-
-
-
?
Gly-Gly-Gly + H2O
Gly-Gly + Gly
show the reaction diagram
-
-
-
?
Gly-Gly-Phe-NH2 + H2O
Gly-Gly + Phe-NH2
show the reaction diagram
-
-
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-L-Phe-NH2 + H2O
Gly-Phe-Gly-Phe-Gly-Phe-Gly-Phe-NH2
show the reaction diagram
-
polymerization
-
-
?
Gly-L-Phe-NH2 + H2O
Gly-Phe-Gly-Phe-Gly-Phe-Gly-Phe-NH2
show the reaction diagram
-
transamidatin
-
-
?
Gly-L-Phe-NH2 + H2O
Gly-L-Phe + NH3
show the reaction diagram
-
-
-
-
?
Gly-L-Phe-NH2 + H2O
Gly-L-Phe + NH3
show the reaction diagram
-
-
-
?
Gly-L-Trp-NH2 + H2O
Gly-L-Trp + NH3
show the reaction diagram
-
-
-
?
Gly-L-Tyr-NH2 + H2O
Gly-L-Tyr + NH3
show the reaction diagram
-
-
-
-
?
Gly-L-Tyr-NH2 + H2O
Gly-L-Tyr + NH3
show the reaction diagram
-
-
-
?
Gly-Leu-ethyl ester + H2O
Gly-Leu + ethanol
show the reaction diagram
-
-
-
-
?
Gly-Leu-NH2 + H2O
Gly-Leu + NH3
show the reaction diagram
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
-
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
-
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
2-naphthylamine + Gly-Phe
show the reaction diagram
-
assay at 37C, pH 5.5, reaction stopped by addition of glycine-NaOH
-
-
?
Gly-Phe-4-methoxy-2-naphthylamide + H2O
Gly-Phe + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Phe-7-amido-4-methylcoumarin + H2O
Gly-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
Gly-Phe-ethyl ester + H2O
Gly-Phe + ethanol
show the reaction diagram
-
-
-
?
Gly-Phe-methyl ester + H2O
Gly-Phe + methanol
show the reaction diagram
-
-
-
-
?
Gly-Phe-p-nitroanilide + H2O
Gly-Phe + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Gly-Trp-2-naphthylamide + H2O
Gly-Trp + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Gly-Trp-methyl ester + H2O
Gly-Trp + methanol
show the reaction diagram
-
-
-
-
?
Gly-Trp-NH2 + H2O
?
show the reaction diagram
-
polymerization
-
-
?
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
show the reaction diagram
-
-
-
-
?
Gly-Tyr-ethyl ester + H2O
Gly-Tyr + ethanol
show the reaction diagram
-
-
-
-
?
Gly-Tyr-Gly + H2O
Gly-Tyr + Gly
show the reaction diagram
-
-
-
-
?
H2N-Abu-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
H2N-Abu-Homo-Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
H2N-fulleroproline-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
H2N-fulleroproline-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
H2N-Leu-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
H2N-Nva-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37C
-
-
?
hexaalanine + H2O
Ala-Ala
show the reaction diagram
-
-
-
?
His-Leu-NH2 + H2O
His-Leu + NH3
show the reaction diagram
-
-
-
-
?
His-Ser-2-naphthylamide + H2O
His-Ser + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
His-Tyr-NH2 + H2O
His-Tyr + NH3
show the reaction diagram
-
-
-
-
?
Ile-Leu-NH2 + H2O
Ile-Leu + NH3
show the reaction diagram
-
-
-
-
?
Ile5-angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
Insulin B-chain + H2O
?
show the reaction diagram
-
bovine, oxidized
-
-
?
L-His-L-Phe-NH2 + H2O
L-His-L-Phe + NH3
show the reaction diagram
-
-
-
?
L-His-L-Tyr-NH2 + H2O
L-His-L-Tyr + NH3
show the reaction diagram
-
-
-
?
L-Ser-L-Tyr-7-amido-4-methylcoumarin + H2O
L-Ser-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
Tyr-Gly + Gly-Phe-Leu
show the reaction diagram
-
i.e. Tyr-Gly-Gly-Phe-Leu
no further degradation of the tripeptide
?
Leu-Tyr-NH2 + H2O
Leu-Tyr + NH3
show the reaction diagram
-
-
-
-
?
Lys-Gly-NH2 + H2O
Lys-Gly + NH3
show the reaction diagram
-
-
-
-
?
Met-enkephalin + H2O
Tyr-Gly + Gly-Phe-Met
show the reaction diagram
-
-
further degradation of Gly-Phe-Met to Gly-Phe + Met
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
tri-alanine is resistant to further breakdown
?
Phe-Arg-2-naphthylamide + H2O
Phe-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Phe-Phe-Phe + H2O
Phe-Phe + Phe
show the reaction diagram
-
-
-
?
Pro-Arg-2-naphthylamide + H2O
Pro-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Pro-Arg-7-amido-4-methylcoumarin + H2O
Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Leu-NH2 + H2O
Pro-Leu + NH3
show the reaction diagram
-
-
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
show the reaction diagram
-
-
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
show the reaction diagram
-
-
-
-
?
sarcosyl-Phe-ethyl ester + H2O
sarcosyl-Phe + ethanol
show the reaction diagram
-
-
-
-
?
secretin + H2O
His-Ser + Asp-Gly + Thr-Phe + Thr-Ser + Glu-Leu + Ser-Arg + Leu-Arg + Asp-Ser + Ala-Arg + Leu-Gln + ?
show the reaction diagram
-
-
further degradation of the hormone is prevented by the appearance of the NH2-terminal Arg
?
Ser-His-Ala + H2O
Ser-His + Ala
show the reaction diagram
-
-
-
?
Ser-Leu-NH2 + H2O
Ser-Leu + NH3
show the reaction diagram
-
-
-
-
?
Ser-Met-2-naphthylamide + H2O
Ser-Met + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Ser-Met-Glu + H2O
Ser-Met + Glu
show the reaction diagram
-
-
-
?
Ser-Tyr-2-naphthylamide + H2O
Ser-Tyr + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Ser-Tyr-NH2 + H2O
Ser + Tyr + NH3
show the reaction diagram
-
-
-
-
?
tetracosactrin + H2O
?
show the reaction diagram
-
-
-
-
?
tetraglycine + H2O
Gly-Gly
show the reaction diagram
-
-
-
?
tetraphenylalanine + H2O
Phe-Phe
show the reaction diagram
-
-
-
?
Thr-Leu-NH2 + H2O
Thr-Leu + NH3
show the reaction diagram
-
-
-
-
?
Val-Leu-NH2 + H2O
Val-Leu + NH3
show the reaction diagram
-
-
-
-
?
Met-Met-Met + H2O
Met-Met + Met
show the reaction diagram
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no activity with peptides involving Pro as the third residue
-
-
-
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
?
-
-
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
?
-
-
modest preference for peptides with nonpolar residues in the P1 position
-
-
-
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 the processing of murine mast cell prochymase and procathepsin G, but does not process mast cell pro-carboxypeptidase A or protryptase
-
-
-
additional information
?
-
-
,n high affinity interaction between heparin and prochymase allows the 2 residue propeptide to be cleaved by dipeptidylpeptidase I
-
-
-
additional information
?
-
P53634
enzyme is involved in intracellular degradation of proteins
-
-
-
additional information
?
-
-
the enzyme is involved in lysosomal protein degradation
-
-
-
additional information
?
-
-
the enzyme may be involved in mediating cell-cell intercommunication in Dictyostelium and in controlling cell movement during morphogenesis
-
-
-
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 gene is a direct target for induction by interferon regulatory factor-8
-
-
-
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
?
-
-
dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation
-
-
-
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
?
-
-
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-Lefvre 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-Lefvre syndrome demonstrates that in the patients with Papillon-Lefvre 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 is involved in the final stages of oocyte maturation in crustacean species
-
-
-
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
?
-
-
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
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
-
-
-
-
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
?
-
-
,n high affinity interaction between heparin and prochymase allows the 2 residue propeptide to be cleaved by dipeptidylpeptidase I
-
-
-
additional information
?
-
P53634
enzyme is involved in intracellular degradation of proteins
-
-
-
additional information
?
-
-
the enzyme is involved in lysosomal protein degradation
-
-
-
additional information
?
-
-
the enzyme may be involved in mediating cell-cell intercommunication in Dictyostelium and in controlling cell movement during morphogenesis
-
-
-
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 gene is a direct target for induction by interferon regulatory factor-8
-
-
-
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
?
-
-
dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation
-
-
-
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
?
-
-
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-Lefvre 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-Lefvre syndrome demonstrates that in the patients with Papillon-Lefvre 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 is involved in the final stages of oocyte maturation in crustacean species
-
-
-
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
?
-
-
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
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Br-
-
absolute requirement for halide ions, 10 mM Cl- or Br- required
Br-
-
absolute requirement for halide ions, the efficacy in decreasing order: Cl-, Br-, I-, F-
Cl-
-
absolute requirement for halide ions, 10 mM Cl- or Br- required
Cl-
-
20 mM, required for maximal activity
Cl-
-
-
Cl-
-
absolute requirement for halide ions, the efficacy in decreasing order: Cl-, Br-, I-, F-
F-
-
absolute requirement for halide ions, the efficacy in decreasing order: Cl-, Br-, I-, F-
I-
-
absolute requirement for halide ions, the efficacy in decreasing order: Cl-, Br-, I-, F-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-4-phenyl-L-prolinamide
-
-
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-4-phenyl-L-prolinamide
-
-
(4S)-4-chloro-N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
-
-
(4S)-N-(1-cyanocyclopropyl)-4-(methylsulfanyl)-L-prolinamide
-
-
(4S)-N-(1-cyanocyclopropyl)-4-fluoro-L-prolinamide
-
-
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
-
-
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
-
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(ethylsulfanyl)-L-prolinamide
-
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-L-prolinamide
-
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-L-prolinamide
-
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methoxy-L-prolinamide
-
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methyl-L-prolinamide
-
-
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
-
-
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
-
-
(4S)-N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-4-fluoro-L-prolinamide
-
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(2-naphthyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 19 nM
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(benzo[b]-thiophen-3-yl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 22 nM
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(indol-3-yl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 21 nM
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(m-fluorophenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 31 nM, competitive inhibition, selective for DPP I over other cysteine and serine proteases, noncytotoxic
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(m-methoxyphenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 39 nM
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(p-chlorophenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 45 nM
3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(1-amino-2-phenylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-2-oxoheptyl 2,6-dimethylbenzoate
-
-
3-[4-(1-aminoethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(2-aminopentan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(2-aminopropan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(2-methylpyrrolidin-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(3-aminopentan-3-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-(4-aminoheptan-4-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-[(1R)-1-amino-1-cyclopentylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-[(1S)-1-amino-1-cyclohexylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-[(1S)-1-amino-1-cyclopentylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
3-[4-[4-(methylamino)heptan-4-yl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
-
5-aminopentanoic acid ethyl ester
-
-
Ala-4(I)Phe-diazomethyl ketone
-
irreversible inhibitor
-
antipain
-
-
Arg-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Benzoyl-Arg-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
beta-Ala-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
-
beta-alanine ethyl ester
-
-
Boc-Gly-DELTA(Z)Phe-AbuPO(OMe)2
-
-
Butylamine
-
reaction with Gly-Gly-ethyl ester, Gly-Gly-NH2 or Gly-Phe-NH2
Cystatin
-
-
-
ethylamine
-
-
fluoride
-
fluoride preparations inhibit activity of cathepsin C in saliva
FY01
-
FY01 is a selective reagent for DPPI and can efficiently label its target in an activity-dependent manner in both crude tissue extracts and intact cells
gamma-aminobutyryl ethyl ester
-
-
-
Glu-alpha-methyl ester
-
inhibition of the reaction with Gly-Gly-ethyl ester, weak inhibition of reaction with Gly-L-Phe-NH2
-
Glucagon
-
competitive inhibition of His-Ser-2-naphthylamide hydrolysis
Gly-beta-Ala-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Gly-DELTA(Z)Phe-AlaPO(OEt)2-trifluoroacetic acid
-
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly
-
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly-OMe
-
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe
-
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe-OMe
-
-
Gly-Gly-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Gly-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Gly-Phe-NH2
-
competitive inhibition of His-Ser-2-naphthylamide hydrolysis
glycinamide
-
reaction with Gly-Gly-ethyl ester, Gly-Gly-NH2 or Gly-Phe-NH2
glycine ethyl ester
-
-
Guanidinium chloride
-
reversible, significantly decreases the Km-value of substrate hydrolysis, without changing the maximal velocity
Hexylamine
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetate
-
-
L-trans-epoxy-succinyl-leucylamido(4-guanidino)-butane
-
-
Leu-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Leupeptin
-
-
Leupeptin
-
-
Lys-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester, weak inhibition of reaction with Gly-L-Phe-NH2
N-(1-cyano-2,2-dimethylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
N-(1-cyano-2-phenylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
N-(1-cyanocyclobutyl)-3-thiophen-2-yl-L-alaninamide
-
-
N-(1-cyanocyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
N-(2-cyanopropan-2-yl)-3-thiophen-2-yl-L-alaninamide
-
-
N-(cyanomethyl)-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
N-[(1R,2R)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2,2-dimethylpropyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2,2-diphenylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-methioninamide
-
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-valinamide
-
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-cysteinamide
-
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-homocysteinamide
-
-
N-[(1S)-1-cyano-2-(4-fluorophenyl)ethyl]-L-prolinamide
-
-
N-[(1S)-1-cyano-2-(5-phenylthiophen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-(naphthalen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-cyclohexylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-methylpropyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-phenylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
-
-
N-[(1S)-1-cyano-2-[4-(methylsulfanyl)phenyl]ethyl]-L-prolinamide
-
-
N-[(1S)-1-cyano-3-phenylpropyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S)-2-(1,3-benzothiazol-2-yl)-1-cyanoethyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
-
-
N-[2-(1H-indol-3-yl)ethyl]-L-methioninamide
-
-
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
p-Hydroxymercuriphenyl sulfonate
-
-
Pentylamine
-
-
Phe-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Propylamine
-
-
SAK2
-
peptide vinyl sulfone, covalent inhibitor
-
Sodium deoxycholate
-
-
Trp-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
Methylamine
-
-
additional information
-
proteinase inhibitor isolated from human whole saliva
-
additional information
-
purification and characterization of a low molecular mass cysteine proteinase inhibitor from human amniotic fluid
-
additional information
-
proteinase inhibitor purified from rat liver, organ distribution of the inhibitor
-
additional information
-
proteinase inhibitors from rat serum and liver
-
additional information
-
enzyme is pseudoirreversibly inhibited by a papain inhibitor, isolated from chicken egg white
-
additional information
-
not inhibited by Triton X-100
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
beta-mercaptoethylamine
-
SH compound required, efficient activator at 25 mM
Cys
-
L-Cys, SH compound required, efficient activator at 25 mM
Cys
-
activates
dithioerythritol
-
SH compound required, efficient activator at 25 mM
dithioerythritol
-
5 mM, activates
DL-homocysteine
-
SH compound required, efficient activator at 25 mM
GSH
-
SH compound required, efficient activator at 25 mM
mercaptoethanol
-
SH compound required, efficient activator at 25 mM
Phenol
-
activates reaction with Gly-Gly-ethyl ester and Gly-Gly-NH2, no effect on reaction with Gly-Phe-NH2
Pyridine
-
activates reaction with Gly-Gly-ethyl ester and Gly-Gly-NH2, no effect on reaction with Gly-Phe-NH2
sulfhydryl activators
-
required
-
mercaptoethylamine
-
activates
additional information
B4XEV1, -
the temporal expression of cathepsinC mRNA in the hepatopancreas is up-regulated by lipopolysaccharide stimulation and reaches the maximum level at 4 h post-stimulation, and then drops back to the original level gradually
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.31
-
alpha-Asp-Arg-beta-naphthylamide
-
-
0.44
-
Asn1-angiotensin II
-
-
0.027
-
Glucagon
-
removal of His-Ser
0.1
-
Gly-Arg-2-naphthylamide
-
-
0.14
-
Gly-Arg-4-methoxy-beta-naphthylamide
-
-
5.3
-
Gly-Gly-ethyl ester
-
-
4
-
Gly-Leu-ethyl ester
-
-
1.5
-
Gly-Phe-ethyl ester
-
-
1.3
-
Gly-Phe-methyl ester
-
-
0.63
-
Gly-Trp-methyl ester
-
-
1.5
-
Gly-Trp-methyl ester
-
-
6
-
Gly-Tyr-NH2
-
-
19
-
glycyl-(beta-phenyl)L-lactic acid methyl ester
-
-
0.022
-
His-Ser-2-naphthylamide
-
-
0.34
-
Ile5-angiotensin II
-
-
6.4
-
L-Ser-L-Tyr-7-amido-4-methylcoumarin
-
in D2O, pH 5.6, at 21C
61
-
sarcosyl-Phe-ethyl ester
-
-
-
2.5
-
Val-Leu-NH2
-
-
17
-
L-Ser-L-Tyr-7-amido-4-methylcoumarin
-
in H2O, pH 5.6, at 21C
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
87
-
Asn1-angiotensin II
-
removal of the first dipeptide
81
-
Glucagon
-
removal of His-Ser
74
-
Gly-Gly-ethyl ester
-
-
126
-
Gly-Leu-ethyl ester
-
-
98
-
Gly-Phe-ethyl ester
-
-
61
-
Gly-Phe-methyl ester
-
-
293
-
Gly-Trp-methyl ester
-
-
90
-
Gly-Tyr-ethyl ester
-
-
210
-
glycyl-(beta-phenyl)L-lactic acid methyl ester
-
-
116
-
His-Ser-2-naphthylamide
-
-
87
-
Ile5-angiotensin II
-
removal of the first dipeptide
157
-
sarcosyl-Phe-ethyl ester
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000015
-
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
0.000045
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(m-fluorophenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
-
1.563
-
Gly-DELTA(Z)Phe-AlaPO(OEt)2-trifluoroacetic acid
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
0.05
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
0.173
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly-OMe
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
0.122
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
0.324
-
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe-OMe
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
0.0000002
-
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.0018
-
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.681
-
tert-butyloxycarbonyl-Gly-DELTA(Z)Phe-AbuPO(OMe)2
-
at 37C in acetate buffer (pH 5) containing NaCl (10 mM)
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
-
-
0.0000017
-
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-4-phenyl-L-prolinamide
-
-
0.0000082
-
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-4-phenyl-L-prolinamide
-
-
0.000495
-
(4S)-4-chloro-N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
-
-
0.000336
-
(4S)-N-(1-cyanocyclopropyl)-4-(methylsulfanyl)-L-prolinamide
-
-
0.00088
-
(4S)-N-(1-cyanocyclopropyl)-4-fluoro-L-prolinamide
-
-
0.000192
-
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
-
-
0.000523
-
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
-
-
0.000271
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(ethylsulfanyl)-L-prolinamide
-
-
0.000029
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-L-prolinamide
-
-
0.000133
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-L-prolinamide
-
-
0.001081
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methoxy-L-prolinamide
-
-
0.002502
-
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methyl-L-prolinamide
-
-
0.000067
-
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
-
-
0.00025
-
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
-
-
0.002193
-
(4S)-N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-4-fluoro-L-prolinamide
-
-
0.000019
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(2-naphthyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 19 nM
0.000022
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(benzo[b]-thiophen-3-yl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 22 nM
0.000021
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(indol-3-yl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 21 nM
0.000031
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(m-fluorophenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 31 nM, competitive inhibition, selective for DPP I over other cysteine and serine proteases, noncytotoxic
0.000039
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(m-methoxyphenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 39 nM
0.000045
-
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(p-chlorophenyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
-
IC50: 45 nM
0.000186
-
3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.074
-
3-[4-(1-amino-2-phenylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.00056
-
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.011
-
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-2-oxoheptyl 2,6-dimethylbenzoate
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.0007
-
3-[4-(1-aminoethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.00041
-
3-[4-(2-aminopentan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.0011
-
3-[4-(2-aminopropan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.00042
-
3-[4-(2-methylpyrrolidin-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.00041
-
3-[4-(3-aminopentan-3-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.0007
-
3-[4-(4-aminoheptan-4-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.000019
-
3-[4-[(1R)-1-amino-1-cyclopentylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.0007
-
3-[4-[(1S)-1-amino-1-cyclohexylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.014
-
3-[4-[(1S)-1-amino-1-cyclopentylethyl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.0077
-
3-[4-[4-(methylamino)heptan-4-yl]-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25C
0.000063
-
N-(1-cyano-2,2-dimethylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
0.00123
-
N-(1-cyano-2-phenylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
0.001832
-
N-(1-cyanocyclobutyl)-3-thiophen-2-yl-L-alaninamide
-
-
0.000012
-
N-(1-cyanocyclopropyl)-3-thiophen-2-yl-L-alaninamide
-
-
0.001419
-
N-(2-cyanopropan-2-yl)-3-thiophen-2-yl-L-alaninamide
-
-
0.000017
-
N-(cyanomethyl)-3-thiophen-2-yl-L-alaninamide
-
-
0.0001
-
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.0000038
-
N-[(1S)-1-cyano-2,2-diphenylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.0000058
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.0002
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-methioninamide
-
-
0.00033
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-valinamide
-
-
0.00063
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-cysteinamide
-
-
0.0000003
-
N-[(1S)-1-cyano-2-(5-phenylthiophen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.000001
-
N-[(1S)-1-cyano-2-(naphthalen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.0000051
-
N-[(1S)-1-cyano-2-cyclohexylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.000215
-
N-[(1S)-1-cyano-2-methylpropyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.0000009
-
N-[(1S)-1-cyano-2-phenylethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.004806
-
N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
-
-
0.002545
-
N-[(1S)-1-cyano-2-[4-(methylsulfanyl)phenyl]ethyl]-L-prolinamide
-
-
0.000011
-
N-[(1S)-1-cyano-3-phenylpropyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.0000007
-
N-[(1S)-2-(1,3-benzothiazol-2-yl)-1-cyanoethyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.000017
-
N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
-
-
0.011
-
N-[2-(1H-indol-3-yl)ethyl]-L-methioninamide
-
-
0.004
-
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.000014
-
N-[(1R,2R)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
-
-
additional information
-
N-[(1S)-1-cyano-2,2-dimethylpropyl]-3-thiophen-2-yl-L-alaninamide
-
value above 0.003 mM
0.00158
-
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-homocysteinamide
-
-
additional information
-
N-[(1S)-1-cyano-2-(4-fluorophenyl)ethyl]-L-prolinamide
-
value above 0.01 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.019
-
-
-
18.6
-
-
-
additional information
-
-
specific activity increases during development being highest during the culmination stage before decreasing during sorocarp formation
additional information
-
-
0.0753 micromol/min/mg after incubation for 40 h at pH 5.5
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
-
5
6
-
Asn1-angiotensin II or Ile5-angiotensin II as substrate
5.2
-
-
His-Ser-beta-naphthylamide as substrate
5.5
-
-
assay at
5.5
-
-
assay at
6
-
-
Gly-Arg-4-methoxy-beta-naphthylamide as substrate
6.3
-
-
removal of His-Ser from glucagon
7.2
7.8
-
-
additional information
-
-
insolubilization has no effect on the pH-optimum
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
7.5
-
50% of maximal activity at pH 4.0 and at pH 7.5
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
50
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
-
B4XEV1, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expressed at relatively low levels in brain
Manually annotated by BRENDA team
-
, CD4(+) spleen cells; CD8(+) T cells
Manually annotated by BRENDA team
-
very low cathepsin C activity in culture medium of untreated keratinocytes, suggesting that the constitutive exocytosis of lysosomes is weak in keratinocytes. Treatment with 0.03 mM ionomycin for 50 min induces the release of about 20% of cathepsin C activity. Incubation of keratinocytes for 30 min with 1 mM calcium and 0.01 mM ionomycin causes a significant release of cathepsin C activity
Manually annotated by BRENDA team
-
cathepsin C activity in monocyte derived dendritic cells (ex vivo) decreases dramatically as they mature
Manually annotated by BRENDA team
-
gene for cathepsin C is upregulated compared to Barrett's esophagus
Manually annotated by BRENDA team
-
activity of dipeptidyl-peptidase I increases significantly as compared to the normal esophageal mucosa
Manually annotated by BRENDA team
-
epithelium from normal control Barrett's esophagus
Manually annotated by BRENDA team
-
activity of dipeptidyl-peptidase I increases significantly as compared to the normal gastric mucosa
Manually annotated by BRENDA team
-
activity of dipeptidyl-peptidase I increases significantly as compared to the normal gastric mucosa
Manually annotated by BRENDA team
B4XEV1, -
highest expression level in heart
Manually annotated by BRENDA team
-
decrease of enzyme activity in kidney cancer
Manually annotated by BRENDA team
-
highest expression in kidney
Manually annotated by BRENDA team
-
decrease in enzyme activity compared to normal kidney
Manually annotated by BRENDA team
-
from peripheral blood
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
bone marrow mast cell
Manually annotated by BRENDA team
-
Biceps femoris, enzyme activity during processing of Jinhua ham
Manually annotated by BRENDA team
-
of peripheral blood. DPPI deficiency in patients with Papillon-Lefevre syndrome
Manually annotated by BRENDA team
-
similar mRNA levels of cathepsin C are found throughout the oocyte growth or vitellogenesis period
Manually annotated by BRENDA team
B4XEV1, -
highest expression level in ovary
Manually annotated by BRENDA team
additional information
-
almost similar level of IgG, IgM, and IgA antibodies to DPP I and CD13 in patients with mixed connective tissue disease and autism, but not in controls
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in B-lymphoblastoid cells cathepsin is distrubuted between late endosomes and lysosomes
Manually annotated by BRENDA team
-
may by associated in a native matrix
Manually annotated by BRENDA team
-
in B-lymphoblastoid cells cathepsin is distrubuted between late endosomes and lysosomes
Manually annotated by BRENDA team
-
trafficking route for the enzyme through the parasitophorous vacuole to the food vacuole
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
B4XEV1, -
calculated from amino acid sequence
51000
-
-
Western blot
100000
-
-
gel filtration
150000
-
-
gel filtration
180000
-
-
gel filtration
200000
-
-
gel filtration
210000
-
-
-
210000
-
-
equilibrium sedimentation
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 200000, SDS-PAGE without reduction; x * 55000, SDS-PAGE with prior reduction
?
-
x * 22000, SDS-PAGE in presence of 2-mercaptoethanol
?
-
x * 24000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
glycoprotein
side-chain modification
-
glycoprotein
proteolytic modification
-
the proenzyme has a MW of 77400 Da after signal peptide cleavage
side-chain modification
-
glycoprotein with mannose 6-phosphate residues
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
8
-
stable
4.6
-
-
stable up to 50C
5
-
-
90 min, about 10% loss of activity
5.5
-
-
stable up to 60C
8
-
-
90 min, about 75% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
immobilized enzyme, stable up to
50
-
-
soluble enzyme, stable up to
50
-
-
at pH 4.6, stable up to
60
-
-
at pH 5.5, stable up to
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, about 50% loss of activity after 4 days and 5 assay cycles, immobilized enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for months
-
-15C, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protein A affinity chromatography and Superdex 200 gel filtration
-
11.1% yield after affinity chromatography on Ni-chelating resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in CHO cells
-
expression in the High Five insect cell line
-
-
P97821
expressed in DPPI-deficient mice
-
cathepsin C propeptide-green fluorescence protein chimera protein is expressed in Caco-2 cells, overexpression of cathepsin C propeptide does not affect cathepsin C activity in Caco-2 cells because the propeptide itself does not have the catalytic domain of cathepsin C
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
highest expression at maturation
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R272P
-
missense mutation found in patients affected with classical features of Papillon-Lefevre syndrome
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
use in peptide sequence studies
synthesis
-
specific and efficient method for complete removal of polyhistidine purification tags from the N-termini of target proteins
medicine
-
mast cell DPPI harms the septic host. DPPI is a novel potential therapeutic target for treatment of sepsis
analysis
-
use in peptide sequence studies
nutrition
-
muscle DPP I may be a key enzyme responsible for the generation of dipeptides in Jinhua ham processing