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Information on EC 3.4.14.1 - dipeptidyl-peptidase I and Organism(s) Homo sapiens

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro
Synonyms
cathepsin c, dppi, dipeptidyl peptidase i, dpp i, dpap1, dipeptidyl aminopeptidase i, dap i, dpp-i, cathepsin j, cat c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cathepsin C
cathepsin J
DAP I
-
-
-
-
dipeptide arylamidase I
-
-
-
-
dipeptidyl aminopeptidase I
-
-
-
-
dipeptidyl peptidase I
-
-
dipeptidyl transferase
-
-
-
-
DPP I
-
-
DPP-I
-
-
hDPPI
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polymerization of dipeptide amides
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-68-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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, 37°C
-
-
?
(H2N-fulleroproline-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Leu-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Leu-Leu)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Nva-(4-phenyl)Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Nva-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
(H2N-Pro-Homo-Phe)2-rhodamine + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly L-Pro-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
?
beta-(2-thienyl)Ala-Phe-7-amido-4-methylcoumarin + H2O
beta-(2-thienyl)Ala-Phe + 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-L-Arg-7-amido-4-methylcoumarin + H2O
Gly-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
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
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
-
-
-
-
?
H2N-Abu-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
H2N-Abu-Homo-Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
H2N-fulleroproline-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
H2N-fulleroproline-(4-phenyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
H2N-Leu-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
H2N-Nva-(3-methyl)Phe-rhodamine-morpholine-4-carboxamide + H2O
?
show the reaction diagram
-
assay at pH 5.5, 37°C
-
-
?
L-Ser-L-Tyr-7-amido-4-methylcoumarin + H2O
L-Ser-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-NH2 + H2O
Pro-Phe + NH3
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
optimal activity between 50 and 200mM NaCl for recombinant truncated cathepsin C. Variant's enzyme activity in the presence of 0.15 mM NaCl is about 55% of optimal activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
Boc-Gly-DELTA(Z)Phe-AbuPO(OMe)2
-
-
fluoride
-
fluoride preparations inhibit activity of cathepsin C in saliva
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
-
-
Guanidinium chloride
-
reversible, significantly decreases the Km-value of substrate hydrolysis, without changing the maximal velocity
leupeptin
-
-
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
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
0.0023
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
0.0065
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
0.0034 - 0.0052
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gln-Tyr(3-NO2)-NH2
0.0022 - 0.0032
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2)-NH2
0.0032 - 0.0052
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Tyr(3-NO2)-NH2
0.003 - 0.0036
beta-(2-thienyl)Ala-Phe-7-amido-4-methylcoumarin
6.4 - 17
L-Ser-L-Tyr-7-amido-4-methylcoumarin
0.0028
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
0.18
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
0.23
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
5.45 - 6.19
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gln-Tyr(3-NO2)-NH2
3.45 - 4.29
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2)-NH2
1.83 - 2.51
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Tyr(3-NO2)-NH2
2.07 - 3.5
beta-(2-thienyl)Ala-Phe-7-amido-4-methylcoumarin
0.16
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
benzyloxyarbonyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
78
benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
35
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
1180 - 1660
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gln-Tyr(3-NO2)-NH2
1340 - 1560
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2)-NH2
491 - 560
beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Tyr(3-NO2)-NH2
684 - 964
beta-(2-thienyl)Ala-Phe-7-amido-4-methylcoumarin
57
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
recombinant truncated cathepsin C, pH 5.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 37°C in acetate buffer (pH 5) containing NaCl (10 mM)
0.05
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly
-
at 37°C in acetate buffer (pH 5) containing NaCl (10 mM)
0.173
Gly-DELTAZPhe-Gly-DELTAEPhe-Gly-OMe
-
at 37°C in acetate buffer (pH 5) containing NaCl (10 mM)
0.122
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe
-
at 37°C in acetate buffer (pH 5) containing NaCl (10 mM)
0.324
Gly-DELTAZPhe-Gly-DELTAEPhe-Phe-OMe
-
at 37°C 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 37°C in acetate buffer (pH 5) containing NaCl (10 mM)
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.000063
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7.5
-
50% of maximal activity at pH 4.0 and at pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
-
high 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
-
activity of dipeptidyl-peptidase I increases significantly as compared to the normal esophageal 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
-
activity of dipeptidyl-peptidase I increases significantly as compared to the normal gastric mucosa
Manually annotated by BRENDA team
-
decrease in enzyme activity compared to normal kidney
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
of peripheral blood. DPPI deficiency in patients with Papillon-Lefevre syndrome
Manually annotated by BRENDA team
-
cytotoxic
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
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
HL-60 cells and differentiated neutrophil-like cells show active CatC in cytoplasmic granules
Manually annotated by BRENDA team
-
in B-lymphoblastoid cells cathepsin is distrubuted between late endosomes and lysosomes
Manually annotated by BRENDA team
mainly located in the Golgi of granule-free undifferentiated PLB-985 cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
mutations in the cathepsin C gene result in an autosomal recessive disorder, Papillon-Lefevre syndrome
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATC_HUMAN
463
0
51854
Swiss-Prot
Secretory Pathway (Reliability: 1)
I3V9S3_HUMAN
48
0
5748
TrEMBL
other Location (Reliability: 1)
A0A7I2V6E3_HUMAN
419
0
47128
TrEMBL
Secretory Pathway (Reliability: 1)
B4DJQ8_HUMAN
446
0
50152
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7I2V466_HUMAN
450
0
50328
TrEMBL
Secretory Pathway (Reliability: 1)
I3V9T0_HUMAN
48
0
5704
TrEMBL
other Location (Reliability: 1)
I3V9T1_HUMAN
48
0
5703
TrEMBL
other Location (Reliability: 1)
A0A7I2V2Q8_HUMAN
452
0
50746
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
210000
-
-
24000
-
x * 24000, SDS-PAGE
55000
-
x * 55000, SDS-PAGE with prior reduction
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking of substrate beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2). The interactions between the amino-terminal group of the substrate and the Asp1 and Gly277 of Cat C are responsible for the substrate N-terminus docking and are crucial for proteolytic activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R272P
-
missense mutation found in patients affected with classical features of Papillon-Lefevre syndrome
additional information
a recombinant form of cathepsin C lacking its exclusion domain is a monomer with endoprotease activity and affinity for hydrophobic residues such as Phe, Leu or Pro, but not Val, in the P2 position
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein A affinity chromatography and Superdex 200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells
-
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
application of substrate beta-(2-thienyl)Ala-beta-(7-methoxycoumarin-4-yl)Ala-Ser-Gly-Tyr(3-NO2) for detection of cathepsin C activity in various cell lysates, urine and bronchoalveolar lavage fluid samples
medicine
assay for enzymic activity in urinary samples to diagnose for Papillon-Lefevre syndrome PLS, which is caused by mutations in both alleles of the cathepsin C. The absence of active CatC and its proform in the urine is a strong and reliable indicator for PLS and useful in the early diagnosis of PLS. In contrast, 100% of urine samples from control subjects of any age and gender contained measurable amounts of active CatC. Nonsense, frameshift and missense mutations all result in a total absence of CatC or CatC fragments in the urine of PLS patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mantle, D.
Characterization of dipeptidyl and tripeptidyl aminopeptidases in human kidney soluble fraction
Clin. Chim. Acta
196
135-142
1991
Homo sapiens
Manually annotated by BRENDA team
Popovic, T.; Puizdar, V.; Ritonja, A.; Brzin, J.
Simultaneous isolation of human kidney cathepsins B, H, L and C and their characterisation
J. Chromatogr.
681
251-262
1996
Homo sapiens
Manually annotated by BRENDA team
Rao, N.V.; Rao, G.V.; Hoidal, J.R.
Human dipeptidyl-peptidase I. Gene characterization, localization, and expression
J. Biol. Chem.
272
10260-10265
1997
Homo sapiens (P53634), Homo sapiens
Manually annotated by BRENDA team
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
432-434
1974
Homo sapiens
-
Manually annotated by BRENDA team
Cigic, B.; Pain, R.H.
Competitive inhibition of cathepsin C by guanidinium ions and reexamination of substrate inhibition
Biochem. Biophys. Res. Commun.
258
6-10
1999
Homo sapiens
Manually annotated by BRENDA team
McGuire, M.J.; Lipsky, P.E.; Thiele, D.L.
Purification and characterization of dipeptidyl peptidase I from human spleen
Arch. Biochem. Biophys.
295
280-288
1992
Homo sapiens
Manually annotated by BRENDA team
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
2458-2567
1993
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Murakami, M.; Karnik, S.S.; Husain, A.
Human prochymase activation. A novel role for heparin in zymogen processing
J. Biol. Chem.
270
2218-2223
1995
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Berdowska, I.
Cysteine proteases as disease markers
Clin. Chim. Acta
342
41-69
2004
Homo sapiens
Manually annotated by BRENDA team
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
515-524
2004
Homo sapiens
Manually annotated by BRENDA team
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
171-173
2006
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
J. Immunol.
173
7277-7281
2004
Homo sapiens (P53634), Homo sapiens
Manually annotated by BRENDA team
Lautwein, A.; Kraus, M.; Reich, M.; Burster, T.; Brandenburg, J.; Overkleeft, H.S.; Schwarz, G.; Kammer, W.; Weber, E.; Kalbacher, H.; Nordheim, A.; Driessen, C.
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team