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(H2N-Abu-Homo-Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-fulleroproline-Homo-Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Leu-Homo-Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Leu-Leu)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Nva-(4-phenyl)Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Nva-Homo-Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Pro-Homo-Phe)2-rhodamine + H2O
?
-
assay at pH 5.5, 37°C
-
-
?
(Pro-Arg)2-Rho + 2 H2O
rhodamine + 2 Pro-Arg
-
-
-
-
?
4 Gly-L-Phe-NH2 + 4 H2O
Gly-Phe-Gly-Phe-Gly-Phe-Gly-Phe-NH2 + 3 NH3
5 Gly-Arg-2-naphthylamide + 5 H2O
(Gly-Arg-)5-2-naphthylamide + 4 2-naphthylamine
-
polymerization
polymers up to (Gly-Arg-)5-2-naphthylamide
?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
-
-
-
-
?
Ala-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
-
-
-
-
?
Ala-Arg-NH2 + H2O
Ala-Arg + NH3
-
-
-
-
?
Ala-Leu-NH2 + H2O
Ala-Leu + NH3
-
-
-
-
?
Ala-Tyr-NH2 + H2O
Ala-Tyr + NH3
-
-
-
-
?
alpha-Asp-Arg-2-naphthylamide + H2O
alpha-Asp-Arg + 2-naphthylamine
-
-
-
-
?
alpha-D-Asp1-angiotensin II + H2O
?
-
low reaction rate
-
-
?
Asn1-angiotensin II + H2O
?
-
-
-
-
?
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
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
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
-
-
-
?
beta-Asp1-angiotensin II + H2O
?
-
low reaction rate
-
-
?
beta-corticotropin + H2O
Ser-Tyr + Ser-Met + Glu-His + Phe-Arg + Trp-Gly
Glu-His-2-naphthylamide + H2O
Glu-His + 2-naphthylamine
-
-
-
-
?
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-Ala-NH2 + H2O
Gly-Ala + NH3
-
-
-
-
?
Gly-Arg-2-naphthylamide + H2O
Gly-Arg + 2-naphthylamine
Gly-Arg-4-methoxy-2-naphthylamide + H2O
Gly-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg + 7-amino-4-methylcoumarin
Gly-Arg-7-amido-4-methylcoumarin + H2O
Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Arg-NH2 + H2O
?
-
polymerization
-
-
?
Gly-Arg-p-nitroanilide + H2O
Gly-Arg + p-nitroaniline
-
-
-
-
?
Gly-Gly-ethyl ester + H2O
Gly-Gly + ethanol
-
-
-
?
Gly-Gly-Gly + H2O
Gly-Gly + Gly
-
-
-
?
Gly-Gly-Phe-NH2 + H2O
Gly-Gly + Phe-NH2
-
-
-
-
?
Gly-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
Gly-L-Phe-NH2 + H2O
Gly-L-Phe + NH3
Gly-L-Trp-NH2 + H2O
Gly-L-Trp + NH3
-
-
-
?
Gly-L-Tyr-NH2 + H2O
Gly-L-Tyr + NH3
Gly-Leu-ethyl ester + H2O
Gly-Leu + ethanol
-
-
-
-
?
Gly-Leu-NH2 + H2O
Gly-Leu + NH3
-
-
-
-
?
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-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
Gly-Phe-4-methoxy-2-naphthylamide + H2O
Gly-Phe + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Phe-7-amido-4-methylcoumarin + H2O
Gly-Phe + 7-amino-4-methylcoumarin
Gly-Phe-ethyl ester + H2O
Gly-Phe + ethanol
-
-
-
?
Gly-Phe-methyl ester + H2O
Gly-Phe + methanol
-
-
-
-
?
Gly-Phe-p-nitroanilide + H2O
Gly-Phe + p-nitroaniline
-
-
-
-
?
Gly-Trp-2-naphthylamide + H2O
Gly-Trp + 2-naphthylamine
-
-
-
-
?
Gly-Trp-methyl ester + H2O
Gly-Trp + methanol
-
-
-
-
?
Gly-Trp-NH2 + H2O
?
-
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
-
-
-
-
?
Gly-Tyr-ethyl ester + H2O
Gly-Tyr + ethanol
-
-
-
-
?
Gly-Tyr-Gly + H2O
Gly-Tyr + 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
-
-
?
hexaalanine + H2O
Ala-Ala
-
-
-
?
His-Leu-NH2 + H2O
His-Leu + NH3
-
-
-
-
?
His-Ser-2-naphthylamide + H2O
His-Ser + 2-naphthylamine
-
-
-
-
?
His-Tyr-NH2 + H2O
His-Tyr + NH3
-
-
-
-
?
Ile-Leu-NH2 + H2O
Ile-Leu + NH3
-
-
-
-
?
Ile5-angiotensin II + H2O
?
-
-
-
-
?
L-His-L-Phe-NH2 + H2O
L-His-L-Phe + NH3
-
-
-
?
L-His-L-Tyr-NH2 + H2O
L-His-L-Tyr + NH3
-
-
-
?
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
?
Leu-Tyr-NH2 + H2O
Leu-Tyr + NH3
-
-
-
-
?
Lys-Gly-NH2 + H2O
Lys-Gly + NH3
-
-
-
-
?
Met-enkephalin + H2O
Tyr-Gly + Gly-Phe-Met
-
-
further degradation of Gly-Phe-Met to Gly-Phe + Met
?
Met-Met-Met + H2O
Met-Met + Met
-
-
-
?
pentaalanine + H2O
Ala-Ala + Ala-Ala-Ala
-
-
tri-alanine is resistant to further breakdown
?
Phe-Arg-2-naphthylamide + H2O
Phe-Arg + 2-naphthylamine
-
-
-
-
?
Phe-Phe-Phe + H2O
Phe-Phe + Phe
-
-
-
?
Pro-Arg-2-naphthylamide + H2O
Pro-Arg + 2-naphthylamine
-
-
-
-
?
Pro-Arg-7-amido-4-methylcoumarin + H2O
Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pro-Leu-NH2 + H2O
Pro-Leu + NH3
-
-
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
sarcosyl-Phe-ethyl ester + H2O
sarcosyl-Phe + ethanol
-
-
-
-
?
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
?
Ser-His-Ala + H2O
Ser-His + Ala
-
-
-
?
Ser-Leu-NH2 + H2O
Ser-Leu + NH3
-
-
-
-
?
Ser-Met-2-naphthylamide + H2O
Ser-Met + 2-naphthylamine
-
-
-
-
?
Ser-Met-Glu + H2O
Ser-Met + Glu
-
-
-
?
Ser-Tyr-2-naphthylamide + H2O
Ser-Tyr + 2-naphthylamine
-
-
-
-
?
Ser-Tyr-NH2 + H2O
Ser + Tyr + NH3
-
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
?
tetraglycine + H2O
Gly-Gly
-
-
-
?
tetraphenylalanine + H2O
Phe-Phe
-
-
-
?
Thr-Leu-NH2 + H2O
Thr-Leu + NH3
-
-
-
-
?
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
-
?
Val-Leu-NH2 + H2O
Val-Leu + NH3
-
-
-
-
?
additional information
?
-
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-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-L-Phe-NH2 + H2O
Gly-L-Phe + NH3
-
-
-
?
Gly-L-Phe-NH2 + H2O
Gly-L-Phe + NH3
-
-
-
-
?
Gly-L-Tyr-NH2 + H2O
Gly-L-Tyr + NH3
-
-
-
?
Gly-L-Tyr-NH2 + H2O
Gly-L-Tyr + NH3
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
-
-
-
-
?
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
-
-
?
Insulin B-chain + H2O
?
-
bovine, oxidized
-
-
?
Insulin B-chain + H2O
?
-
bovine, oxidized
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
-
-
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
-
-
-
-
?
tetracosactrin + H2O
?
-
-
-
-
?
tetracosactrin + H2O
?
-
-
-
-
?
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
?
-
-
-
-
-
?
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
-
-
?
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(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-chloro-2-hydroxypropyl (2Z)-2-(2-aminoacetamido)-3-phenylprop-2-enoate
-
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
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
1.5 mM, 81% residual activity
5-aminopentanoic acid ethyl ester
-
-
Ala-4(I)Phe-diazomethyl ketone
-
irreversible inhibitor
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
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-CHN2
presence down-regulates mast cell intracellular DPPI and chymase activities. Inhibitor Gly-Phe-CHN2 also inhibits the LTB4-activated neutrophils and neutrophil-elastase activities
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
Guanidinium chloride
-
reversible, significantly decreases the Km-value of substrate hydrolysis, without changing the maximal velocity
L-trans-epoxy-succinyl-leucylamido(4-guanidino)-butane
-
-
Leu-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
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-ethylmaleimine
-
1 mM, 46.4% residual activity
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
-
-
Phe-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
prop-2-en-1-yl 2-(2-amino-3-phenylpropanamido)prop-2-enoate
-
SAK2
-
peptide vinyl sulfone, covalent inhibitor
Trp-NH2
-
inhibition of the reaction with Gly-Gly-ethyl ester or Gly-L-Phe-NH2
3-[4-(1-amino-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
compound has more than 1000 and more than 100times more activity against isoforms DPAP1 and DPAP3, respectively, than against DPAP2
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-1-cyclopentylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
i.e. ML4118S
antipain
-
-
iodoacetamide
-
-
iodoacetate
-
-
iodoacetate
-
1 mM, 59.2% residual activity
leupeptin
-
-
leupeptin
-
1 mM, 39.1% residual activity
NEM
-
-
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
-
enzyme is pseudoirreversibly inhibited by a papain inhibitor, isolated from chicken egg white
-
additional information
-
proteinase inhibitor purified from rat liver, organ distribution of the inhibitor
-
additional information
-
proteinase inhibitors from rat serum and liver
-
additional information
-
not inhibited by Triton X-100
-
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0.01
(2S)-2-amino-N-[(1S)-2-(biphenyl-4-yl)-1-cyanoethyl]butanamide
Homo sapiens
-
-
0.0000017
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-4-phenyl-L-prolinamide
Homo sapiens
-
-
0.0000082
(4R)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-4-phenyl-L-prolinamide
Homo sapiens
-
-
0.000495
(4S)-4-chloro-N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
Homo sapiens
-
-
0.000336
(4S)-N-(1-cyanocyclopropyl)-4-(methylsulfanyl)-L-prolinamide
Homo sapiens
-
-
0.00088
(4S)-N-(1-cyanocyclopropyl)-4-fluoro-L-prolinamide
Homo sapiens
-
-
0.000192
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
Homo sapiens
-
-
0.000523
(4S)-N-[(1R,2S)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
Homo sapiens
-
-
0.000271
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(ethylsulfanyl)-L-prolinamide
Homo sapiens
-
-
0.000029
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-(methylsulfanyl)-L-prolinamide
Homo sapiens
-
-
0.000133
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-fluoro-L-prolinamide
Homo sapiens
-
-
0.001081
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methoxy-L-prolinamide
Homo sapiens
-
-
0.002502
(4S)-N-[(1S)-1-cyano-2-phenylethyl]-4-methyl-L-prolinamide
Homo sapiens
-
-
0.000067
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-(methylsulfanyl)-L-prolinamide
Homo sapiens
-
-
0.00025
(4S)-N-[(1S,2R)-2-benzyl-1-cyanocyclopropyl]-4-fluoro-L-prolinamide
Homo sapiens
-
-
0.002193
(4S)-N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-4-fluoro-L-prolinamide
Homo sapiens
-
-
0.000019
1-(2S-2-aminobutanoyl)-4-(2S-N-(2S-3-(2-naphthyl)propan-2-yl-amide)4-phenylbutan-2-yl-amide)semicarbazide
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.074
3-[4-(1-amino-2-phenylethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.00056
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.011
3-[4-(1-aminocyclohexyl)-1H-1,2,3-triazol-1-yl]-2-oxoheptyl 2,6-dimethylbenzoate
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.0007
3-[4-(1-aminoethyl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.00041
3-[4-(2-aminopentan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.0011
3-[4-(2-aminopropan-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.00042
3-[4-(2-methylpyrrolidin-2-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.00041
3-[4-(3-aminopentan-3-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.0007
3-[4-(4-aminoheptan-4-yl)-1H-1,2,3-triazol-1-yl]-1-(2,3,5,6-tetrafluorophenoxy)heptan-2-one
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
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
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
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
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
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
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
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
Plasmodium falciparum
-
determined after 30 min incubation of parasite lysate with 5 nM to 0.1 mM inhibitor, pH not specified in the publication, 25°C
0.000063
N-(1-cyano-2,2-dimethylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.00123
N-(1-cyano-2-phenylcyclopropyl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.001832
N-(1-cyanocyclobutyl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.000012
N-(1-cyanocyclopropyl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.001419
N-(2-cyanopropan-2-yl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.000017
N-(cyanomethyl)-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0001
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
Homo sapiens
-
-
0.000014
N-[(1R,2R)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0000038
N-[(1S)-1-cyano-2,2-diphenylethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0000058
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0002
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-methioninamide
Homo sapiens
-
-
0.00033
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-L-valinamide
Homo sapiens
-
-
0.00063
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-cysteinamide
Homo sapiens
-
-
0.00158
N-[(1S)-1-cyano-2-(1H-indol-3-yl)ethyl]-S-ethyl-L-homocysteinamide
Homo sapiens
-
-
0.0000003
N-[(1S)-1-cyano-2-(5-phenylthiophen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.000001
N-[(1S)-1-cyano-2-(naphthalen-2-yl)ethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0000051
N-[(1S)-1-cyano-2-cyclohexylethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.000215
N-[(1S)-1-cyano-2-methylpropyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0000009
N-[(1S)-1-cyano-2-phenylethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.004806
N-[(1S)-1-cyano-2-phenylethyl]-L-prolinamide
Homo sapiens
-
-
0.002545
N-[(1S)-1-cyano-2-[4-(methylsulfanyl)phenyl]ethyl]-L-prolinamide
Homo sapiens
-
-
0.000011
N-[(1S)-1-cyano-3-phenylpropyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.0000007
N-[(1S)-2-(1,3-benzothiazol-2-yl)-1-cyanoethyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.000017
N-[(1S,2S)-1-cyano-2-phenylcyclopropyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
-
0.011
N-[2-(1H-indol-3-yl)ethyl]-L-methioninamide
Homo sapiens
-
-
0.004
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
Homo sapiens
-
-
additional information
N-[(1S)-1-cyano-2,2-dimethylpropyl]-3-thiophen-2-yl-L-alaninamide
additional information
N-[(1S)-1-cyano-2,2-dimethylpropyl]-3-thiophen-2-yl-L-alaninamide
Homo sapiens
-
value above 0.003 mM
additional information
N-[(1S)-1-cyano-2-(4-fluorophenyl)ethyl]-L-prolinamide
Homo sapiens
-
value above 0.01 mM
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Mantle, D.
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Homo sapiens
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Biol. Chem. Hoppe-Seyler
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1985
Bos taurus
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Mainferme, F.; Wattiaux, R.; von Figura, K.
Synthesis, transport and processing of cathepsin C in Morris hepatoma 7777 cells and rat hepatocytes
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Rattus norvegicus
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Bos taurus
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Purification and characterization of thiol proteinase inhibitor from rat liver
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Rattus norvegicus
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Wakamatsu, N.; Kominami, E.; Katunuma, N.
Comparison of properties of thiol proteinase inhibitors from rat serum and liver
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Rattus norvegicus
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31
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1972
Rattus norvegicus
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Homo sapiens
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Human dipeptidyl-peptidase I. Gene characterization, localization, and expression
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Biochemistry
5
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1966
Bos taurus
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Voynick, I.M.; Fruton, J.S.
The specificity of dipeptidyl transferase
Biochemistry
7
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1968
Bos taurus
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Keilova, H.; Tomasek, V.
Inhibition of cathepsin C by papain inhibitor from chicken egg white and by complex of this inhibitor with cathepsin B1
Collect. Czech. Chem. Commun.
40
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1975
Bos taurus
-
brenda
Huisman, W.; Lanting, L.; Doddema, H.J.; Bouma, J.M.W.; Gruber, M.
Role of individual cathepsins in lysosomal protein digestion as tested by specific inhibitors
Biochim. Biophys. Acta
370
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1974
Rattus norvegicus
brenda
Metrione, R.M.; MacGeorge, N.L.
The mechanism of action of dipeptidyl aminopeptidase. Inhibition by amino acid derivatives and amines; activation by aromatic compounds
Biochemistry
14
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1975
Bos taurus
brenda
Matsuda, K.; Misaka, E.
Studies on cathepsins of rat liver lysosomes. I. Purification and multiple forms
J. Biochem.
76
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1974
Rattus norvegicus
brenda
Davies, P.; Allison, A.C.; Hylton, W.J.
The identification, properties and subcellular distribution of cathepsins B1 and C (dipeptidyl aminopeptidase 1) in human peripheral-blood leucocytes
Biochem. Soc. Trans.
2
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1974
Homo sapiens
-
brenda
McDonald, J.K.; Zeitman, B.B.; Callahan, P.X.; Ellis, S.
Angiotensinase activity of dipeptidyl aminopeptidase I (cathepsin C) of rat liver
J. Biol. Chem.
249
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1974
Rattus norvegicus
brenda
Alba, F.; Arenas, J.C.; Lopez, M.A.
Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents
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16
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1995
Rattus norvegicus
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McDonald, J.K.; Callahan, P.X.; Ellis, S.
Preparation and specificity of dipeptidyl aminopeptidase I
Methods Enzymol.
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1972
Bos taurus, Rattus norvegicus
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Calam, D.H.; Thomas, H.J.
Water-insoluble enzymes for peptide sequencing: dipeptidyl aminopeptidase I (cathepsin C), an enzyme with subunit structure
Biochim. Biophys. Acta
276
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1972
Bos taurus, Rattus norvegicus
brenda
Huang, F.L.; Tappel, A.L.
Properties of cathepsin C from rat liver
Biochim. Biophys. Acta
268
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1972
Rattus norvegicus
brenda
De Lumen, B.O.; Taylor, S.; Urribarri, N.; Tappel, A.L.
Subcellular localization of acid hydrolases in rat lungs
Biochim. Biophys. Acta
268
597-600
1972
Rattus norvegicus
brenda
McDonald, J.K.; Callahan, P.X.; Zeitman, B.B.; Ellis, S.
Inactivation and degradation of glucagon by dipeptidyl aminopeptidase I (cathepsin C) of rat liver
J. Biol. Chem.
244
6199-6208
1969
Rattus norvegicus
brenda
McDonald, J.K.; Reilly, T.J.; Zeitman, B.B.; Ellis, S.
Cathepsin C: a chloride-requiring enzyme
Biochem. Biophys. Res. Commun.
24
771-775
1966
Rattus norvegicus
brenda
Pal, S.; Raghav, N.; Kamboj, R.C.; Singh, H.
Dipeptidyl peptidase I from goat brain: purification, characterization and its action on Leu-enkephalin
Neurochem. Int.
22
59-68
1993
Capra hircus
brenda
McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S.
New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones
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244
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1969
Bos taurus, Rattus norvegicus
brenda
Pedersen, J.; Lauritzen, C.; Madsen, M.T.; Dahl, S.W.
Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases
Protein Expr. Purif.
15
389-400
1999
Meleagris gallopavo
brenda
Cigic, B.; Pain, R.H.
Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition
Biochem. Biophys. Res. Commun.
258
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1999
Homo sapiens
brenda
McGuire, M.J.; Lipsky, P.E.; Thiele, D.L.
Purification and characterization of dipeptidyl peptidase I from human spleen
Arch. Biochem. Biophys.
295
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1992
Homo sapiens
brenda
McGuire, M.J.; Lipsky, P.E.; Thiele, D.L.
Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I
J. Biol. Chem.
268
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1993
Homo sapiens, Mus musculus
brenda
Dikov, M.M.; Springman, E.B.; Yeola, S.; Serafin, W.E.
Processing of procarboxypeptidase A and other zymogens in murine mast cells
J. Biol. Chem.
269
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1994
Mus musculus
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Murakami, M.; Karnik, S.S.; Husain, A.
Human prochymase activation. A novel role for heparin in zymogen processing
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270
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1995
Homo sapiens
brenda
Jans, R.; Sartor, M.; Jadot, M.; Poumay, Y.
Calcium entry into keratinocytes induces exocytosis of lysosomes
Arch. Dermatol. Res.
296
30-41
2004
Homo sapiens
brenda
Bondebjerg, J.; Fuglsang, H.; Valeur, K.R.; Kaznelson, D.W.; Hansen, J.A.; Pedersen, R.O.; Krogh, B.O.; Jensen, B.S.; Lauritzen, C.; Petersen, G.; Pedersen, J.; Naerum, L.
Novel semicarbazide-derived inhibitors of human dipeptidyl peptidase I (hDPPI)
Bioorg. Med. Chem.
13
4408-4424
2005
Homo sapiens
brenda
Tamura, T.; Thotakura, P.; Tanaka, T.S.; Ko, M.S.; Ozato, K.
Identification of target genes and a unique cis element regulated by IRF-8 in developing macrophages
Blood
106
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2005
Mus musculus
brenda
Meade, J.L.; de Wynter, E.A.; Brett, P.; Sharif, S.M.; Woods, C.G.; Markham, A.F.; Cook, G.P.
A family with Papillon-Lefevre syndrome reveals a requirement for cathepsin C in granzyme B activation and NK cell cytolytic activity
Blood
107
3665-3668
2006
Homo sapiens
brenda
Berdowska, I.
Cysteine proteases as disease markers
Clin. Chim. Acta
342
41-69
2004
Homo sapiens
brenda
Vojdani, A.; Bazargan, M.; Vojdani, E.; Samadi, J.; Nourian, A.A.; Eghbalieh, N.; Cooper, E.L.
Heat shock protein and gliadin peptide promote development of peptidase antibodies in children with autism and patients with autoimmune disease
Clin. Diagn. Lab. Immunol.
11
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2004
Homo sapiens
brenda
Qiu, G.; Yamano, K.; Unuma, T.
Cathepsin C transcripts are differentially expressed in the final stages of oocyte maturation in kuruma prawn Marsupenaeus japonicus
Comp. Biochem. Physiol. B
140B
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2005
Penaeus japonicus
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brenda
de Haar, S.F.; Tigchelaar-Gutter, W.; Everts, V.; Beertsen, W.
Structure of the periodontium in cathepsin C-deficient mice
Eur. J. Oral Sci.
114
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2006
Homo sapiens
brenda
Hewitt, C.; McCormick, D.; Linden, G.; Turk, D.; Stern, I.; Wallace, I.; Southern, L.; Zhang, L.; Howard, R.; Bullon, P.; Wong, M.; Widmer, R.; Gaffar, K.A.; Awawdeh, L.; Briggs, J.; Yaghmai, R.; Jabs, E.W.; Hoeger, P.; Bleck, O.; Ruediger, S.G.; Petersilka, G.; Battino, M.; Brett, P.; Hattab, F.; Al-Hamed, M.; Sloan, P.; Toomes, C.; Dixon, M.; James, J.; Read, A.P.; Thakker, N.
The role of cathepsin C in Papillon-Lefevre syndrome, prepubertal periodontitis, and aggressive periodontitis
Hum. Mutat.
23
222-228
2004
Homo sapiens
brenda
Ishri, R.K.; Menzies, S.; Hersey, P.; Halliday, G.M.
Rapid downregulation of antigen processing enzymes in ex vivo generated human monocyte derived dendritic cells occur endogenously in extended cultures
Immunol. Cell Biol.
82
239-246
2004
Homo sapiens
brenda
Yuan, F.; Verhelst, S.H.; Blum, G.; Coussens, L.M.; Bogyo, M.
A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C
J. Am. Chem. Soc.
128
5616-5617
2006
Rattus norvegicus
brenda
Klemba, M.; Gluzman, I.; Goldberg, D.E.
A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
J. Biol. Chem.
279
43000-43007
2004
Plasmodium falciparum
brenda
Mallen-St Clair, J.; Pham, C.T.; Villalta, S.A.; Caughey, G.H.; Wolters, P.J.
Mast cell dipeptidyl peptidase I mediates survival from sepsis
J. Clin. Invest.
113
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2004
Mus musculus
brenda
Pham, C.T.; Ivanovich, J.L.; Raptis, S.Z.; Zehnbauer, B.; Ley, T.J.
Papillon-Lefevre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans
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2004
Homo sapiens (P53634), Homo sapiens
brenda
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Human B lymphoblastoid cells contain distinct patterns of cathepsin activity in endocytic compartments and regulate MHC class II transport in a cathepsin S-independent manner
J. Leukocyte Biol.
75
844-855
2004
Homo sapiens
brenda
Zhao, G.M.; Zhou, G.H.; Xu, X.L.; Peng, Z.Q.; Huan, Y.J.; Jing, Z.M.; Chen, M.W.
Studies on time-related changes of dipeptidyl peptidase during processing of Jinhua ham using response surface methodology
Meat Sci.
69
165-174
2004
Sus scrofa
brenda
Fabra, M.; Cerda, J.
Ovarian cysteine proteinases in the teleost Fundulus heteroclitus: molecular cloning and gene expression during vitellogenesis and oocyte maturation
Mol. Reprod. Dev.
67
282-294
2004
Fundulus heteroclitus
brenda
Hsiung, H.M.; Smiley, D.L.; Zhang, X.y.; Zhang, L.; Yan, L.Z.; Craft, L.; heiman, M.L.; Smith, D.P.
Potent peptide agonists for human melanocortin 3 and 4 receptors derived from enzymatic cleavages of human beta-MSH(5-22) by dipeptidyl peptidase I and dipeptidyl peptidase IV
Peptides
26
1988-1996
2005
Homo sapiens
brenda
Dabrowska, E.; Letko, M.; Roszkowska-Jakimiec, W.; Letko, R.; Jamiolkowski, J.
Effect of fluoride preparations on the activity of human salivary cathepsin C
Rocz. Akad. Med. Bialymst.
50
160-162
2005
Homo sapiens
-
brenda
Cheng, P.; Gong, J.; Wang, T.; Chen, J.; Liu, G.S.; Zhang, R.
Gene expression in rats with Barretts esophagus and esophageal adenocarcinoma induced by astroduodenoesophageal reflux
World J. Gastroenterol.
11
5117-5122
2005
Rattus norvegicus
brenda
Altorjay, A.; Paal, B.; Sohar, N.; Kiss, J.; Szanto, I.; Sohar, I.
Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus
World J. Gastroenterol.
11
5751-5756
2005
Homo sapiens
brenda
Tye, C.E.; Pham, C.T.; Simmer, J.P.; Bartlett, J.D.
DPPI may activate KLK4 during enamel formation
J. Dent. Res.
88
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2009
Mus musculus
brenda
Kim, K.H.; Pham, C.T.; Sleat, D.E.; Lobel, P.
Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis
Biochem. J.
415
225-232
2008
Mus musculus
brenda
Schneck, J.L.; Villa, J.P.; McDevitt, P.; McQueney, M.S.; Thrall, S.H.; Meek, T.D.
Chemical mechanism of a cysteine protease, cathepsin C, as revealed by integration of both steady-state and pre-steady-state solvent kinetic isotope effects
Biochemistry
47
8697-8710
2008
Homo sapiens
brenda
Qiu, L.; Jiang, S.; Huang, J.; Wang, W.; Zhang, D.; Wu, Q.; Yang, K.
Molecular cloning and mRNA expression of cathepsin C gene in black tiger shrimp (Penaeus monodon)
Comp. Biochem. Physiol. A
150
320-325
2008
Penaeus monodon (B4XEV1), Penaeus monodon
brenda
Noack, B.; Goergens, H.; Hempel, U.; Fanghaenel, J.; Hoffmann, T.; Ziegler, A.; Schackert, H.K.
Cathepsin C gene variants in aggressive periodontitis
J. Dent. Res.
87
958-963
2008
Homo sapiens
brenda
Akk, A.M.; Simmons, P.M.; Chan, H.W.; Agapov, E.; Holtzman, M.J.; Grayson, M.H.; Pham, C.T.
Dipeptidyl peptidase I-dependent neutrophil recruitment modulates the inflammatory response to Sendai virus infection
J. Immunol.
180
3535-3542
2008
Mus musculus
brenda
Latajka, R.; Jewginski, M.; Makowski, M.; Pawe?czak, M.; Huber, T.; Sewald, N.; Kafarski, P.
Pentapeptides containing two dehydrophenylalanine residues-synthesis, structural studies and evaluation of their activity towards cathepsin C
J. Pept. Sci.
14
1084-1095
2008
Homo sapiens
brenda
Hirasaka, K.; Tokuoka, K.; Nakao, R.; Yamada, C.; Oarada, M.; Imagawa, T.; Ishidoh, K.; Okumura, Y.; Kishi, K.; Nikawa, T.
Cathepsin C propeptide interacts with intestinal alkaline phosphatase and heat shock cognate protein 70 in human Caco-2 cells
J. Physiol. Sci.
58
105-111
2008
Rattus norvegicus
brenda
Guay, D.; Beaulieu, C.; Truchon, J.F.; Jagadeeswar Reddy, T.; Zamboni, R.; Bayly, C.I.; Methot, N.; Rubin, J.; Ethier, D.; David Percival, M.
Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C
Bioorg. Med. Chem. Lett.
19
5392-5396
2009
Homo sapiens
brenda
Li, J.; Petrassi, H.; Tumanut, C.; Masick, B.; Trussell, C.; Harris, J.
Substrate optimization for monitoring cathepsin C activity in live cells
Bioorg. Med. Chem.
17
1064-1070
2009
Homo sapiens
brenda
Kurban, M.; Wajid, M.; Shimomura, Y.; Bahhady, R.; Kibbi, A.G.; Christiano, A.M.
Evidence for a founder mutation in the cathepsin C gene in three families with Papillon-Lefevre syndrome
Dermatology
219
289-294
2009
Homo sapiens
brenda
Qiu, G.; Feng, H.; Yamano, K.
Expression and purification of active recombinant cathepsin C (dipeptidyl aminopeptidase I) of kuruma prawn marsupenaeus japonicus in insect cells
J. Biomed. Biotechnol.
2009
746289
2009
Penaeus japonicus
brenda
Deu, E.; Leyva, M.; Albrow, V.; Rice, M.; Ellman, J.; Bogyo, M.
Functional studies of plasmodium falciparum dipeptidyl aminopeptidase i using small molecule inhibitors and active site probes
Chem. Biol.
17
808-819
2010
Plasmodium falciparum
brenda
Tanaka, T.Q.; Deu, E.; Molina-Cruz, A.; Ashburne, M.J.; Ali, O.; Suri, A.; Kortagere, S.; Bogyo, M.; Williamson, K.C.
Plasmodium dipeptidyl aminopeptidases as malaria transmission-blocking drug targets
Antimicrob. Agents Chemother.
57
4645-4652
2013
Plasmodium berghei (A0A509AWF2), Plasmodium berghei, Plasmodium falciparum (Q8I0V1), Plasmodium falciparum, Plasmodium berghei ANKA (A0A509AWF2)
brenda
Sutherland, R.E.; Barry, S.S.; Olsen, J.S.; Salantes, D.B.; Caughey, G.H.; Wolters, P.J.
Dipeptidyl peptidase I controls survival from Klebsiella pneumoniae lung infection by processing surfactant protein D
Biochem. Biophys. Res. Commun.
450
818-823
2014
Mus musculus
brenda
Suban, D.; Zajc, T.; Renko, M.; Turk, B.; Turk, V.; Dolenc, I.
Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer rat thyroid cells liberate thyroxin from the N-terminus of thyroglobulin
Biochimie
94
719-726
2012
Rattus norvegicus
brenda
Legowska, M.; Hamon, Y.; Wojtysiak, A.; Grzywa, R.; Sie?czyk, M.; Burster, T.; Korkmaz, B.; Lesner, A.
Development of the first internally-quenched fluorescent substrates of human cathepsin C The application in the enzyme detection in biological samples
Arch. Biochem. Biophys.
612
91-102
2016
Homo sapiens (P53634), Homo sapiens
brenda
Chu, Y.; Guo, Y.; Walls, A.F.; Zhou, X.
The regulatory role of dipeptidyl peptidase I on the activation of immune granulocytes
Cell Biol. Int.
41
1093-1102
2017
Rattus norvegicus (P80067)
brenda
Hamon, Y.; Legowska, M.; Fergelot, P.; Dallet-Choisy, S.; Newell, L.; Vanderlynden, L.; Kord Valeshabad, A.; Acrich, K.; Kord, H.; Charalampos, T.; Morice-Picard, F.; Surplice, I.; Zoidakis, J.; David, K.; Vlahou, A.; Ragunatha, S.; Nagy, N.; Farkas, K.; Szell, M.; Goizet, C.; Schacher, B.; Battino, M.
Analysis of urinary cathepsin C for diagnosing Papillon-Lefevre syndrome
FEBS J.
283
498-509
2016
Homo sapiens (P53634), Homo sapiens
brenda
Wei, S.; Wang, S.; Yang, M.; Huang, Y.; Wei, J.; Huang, X.; Qin, Q.
Characterization of cathepsin C from orange-spotted grouper, Epinephelus coioides involved in SGIV infection
Fish Shellfish Immunol.
84
423-433
2019
Epinephelus coioides (A0A088BPG5), Epinephelus coioides
brenda
Hamon, Y.; Legowska, M.; Herve, V.; Dallet-Choisy, S.; Marchand-Adam, S.; Vanderlynden, L.; Demonte, M.; Williams, R.; Scott, C.J.; Si-Tahar, M.; Heuze-Vourch, N.; Lalmanach, G.; Jenne, D.E.; Lesner, A.; Gauthier, F.; Korkmaz, B.
Neutrophilic cathepsin C is maturated by a multistep proteolytic process and secreted by activated cells during inflammatory lung diseases
J. Biol. Chem.
291
8486-8499
2016
Homo sapiens (P53634), Homo sapiens
brenda
Durose, W.W.; Shimizu, T.; Li, J.; Abe, M.; Sakimura, K.; Chetsawang, B.; Tanaka, K.F.; Suzumura, A.; Tohyama, K.; Ikenaka, K.
Cathepsin C modulates myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis
J. Neurochem.
148
413-425
2019
Mus musculus (P97821), Mus musculus
brenda
Makowski, M.; Lenartowicz, P.; Oszywa, B.; Jewginski, M.; Pawelczak, M.; Kafarski, P.
Synthesis of dehydrodipeptide esters and their evaluation as inhibitors of cathepsin C
Med. Chem. Res.
24
3157-3165
2015
Bos taurus (Q3ZCJ8)
brenda
Khaket, T.; Dhanda, S.; Jodha, D.; Singh, J.
Biochemical studies on dipeptidyl peptidase I (cathepsin C) from germinated Vigna radiata seeds
Process Biochem.
51
1015-1027
2016
Vigna radiata
-
brenda
Rebernik, M.; Lenarcic, B.; Novinec, M.
The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease
Protein Expr. Purif.
157
21-27
2019
Homo sapiens (P53634)
brenda