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Information on EC 3.4.22.16 - cathepsin H
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3.4.22.16 cathepsin HSpecify your search results
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
Synonyms
aleurain, aleuron thiol protease, alpha-N-benzoyl-arginine 2-naphthylamide hydrolase, alpha-N-benzoylarginine-beta-naphthylamide hydrolase, Cat H, CatB3, CatH, cathepsin B3, cathepsin Ba, cathepsin H, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aleurain
-
-
-
-
cathepsin B3
cathepsin Ba
-
-
-
-
cathepsin H
CTSH
cathepsin B3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
mini-chain has definitive role in substrate-recognition, implications for enzyme function
-
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
mechanism: specific interactions of an anionic active site residue with the charged alpha-amino group of substrates cause transition state stabilization which proves the enzyme to act preferentially as an aminopeptidase
-
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
mechanism: interactive catalytic-site system in which the nucleophilic character of the sulphur atom is maintained in acidic media
-
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
number of possible subsites: three
-
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
same catalytic mechanism as in papain and actinidin
-
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
hydrolysis of peptide bond
-
-
peptides, endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
60748-73-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
-
-
ir
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
ir
alpha-N-benzoyl-DL-Arg-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-Arg + beta-naphthylamine
-
-
-
?
alpha-N-benzoyl-DL-arginine-2-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + 2-naphthylamine
-
-
-
-
?
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
alpha-neoendorphin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
Arg-7-amido-4-trifluoromethylcoumarin + H2O
Arg + 7-amino-4-trifluoromethylcoumarin
fluorogenic cathepsin H substrate
-
-
?
benzoyl-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-Arg + 7-amino-4-methylcoumarin
-
-
-
ir
benzoyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro + H2O
benzyloxycarbonyl-Pro-Ala-Ala-Ala + Pro
-
-
-
ir
benzyloxycarbonyl-Pro-Ala-Ala-Ala-Pro-NH2 + H2O
benzyloxycarbonyl-Pro-Ala-Ala-Ala + Pro-NH2
-
-
-
ir
bradykinin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
citrulline-4-methylcoumaryl-7-amide + H2O
citrulline + 7-amino-4-methylcoumarin
-
-
-
ir
demorphin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
dynorphin(1-13) + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
dynorphin(1-6) + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
Gly-beta-naphthylamide + H2O
Gly + beta-naphthylamine
-
very poor substrate
-
?
H2N-Arg-7-amido-4-methylcoumarin + H2O
H2N-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-beta-naphthylamide + H2O
L-Ala + beta-naphthylamine
-
-
-
?
L-Arg-4-methylcoumaryl-7-amide + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-beta-naphthylamide + H2O
L-Arg + beta-naphthylamine
-
-
-
?
L-Leu-beta-naphthylamide + H2O
L-Leu + beta-naphthylamine
-
-
-
?
L-Lys-beta-naphthylamide + H2O
L-Lys + beta-naphthylamine
-
-
-
?
L-Met-beta-naphthylamide + H2O
L-Met + beta-naphthylamine
-
-
-
?
L-Pro-beta-naphthylamide + H2O
L-Pro + beta-naphthylamine
-
very poor substrate
-
?
L-Ser-beta-naphthylamide + H2O
L-Ser + beta-naphthylamine
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
ir
Leu-enkephalin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
Lys-4-methylcoumaryl-7-amide + H2O
Lys + 7-amino-4-methylcoumarin
-
-
-
ir
Lys-bradykinin + H2O
?
-
preferentially aminopeptidase activity, endoeptidase activity after prolonged incubation
-
?
Met-2-naphthylamide + H2O
Met + 2-naphthylamine
-
189% activity of substrate Leu-2-N-naphthylamine
-
ir
neurotensin + H2O
?
-
no aminopeptidase activity, endopeptidase activity after prolonged incubation
-
?
pro-granzyme B + H2O
granzyme B + ?
-
cathepsin H has pro-granzyme B convertase activity in vitro
-
-
?
pro-surfactant protein B-EGFP fusion protein + H2O
?
-
cleavage 13 amino acids upstream of the NH2-terminus of mature surfactant protein B, and at the boundary between surfactant protein and C-terminal peptide
-
-
?
succinyl-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala + 4-nitroaniline
-
-
-
ir
succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
ir
succinyl-Ala-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala-Ala + 4-nitroaniline
-
-
-
ir
succinyl-Ala-Ala-Ala-Ala-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Ala-Ala-Ala + 4-nitroaniline
-
-
-
ir
succinyl-Ala-Ala-Pro-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro + 4-nitroaniline
-
-
-
ir
succinyl-Ala-Pro-Ala-4-nitroanilide + H2O
succinyl-Ala-Pro-Ala + 4-nitroaniline
-
-
-
ir
succinyl-Pro-Ala-Ala-4-nitroanilide + H2O
succinyl-Pro-Ala-Ala + 4-nitroaniline
-
-
-
ir
talin + H2O
?
-
cathepsin H cleaves the N-terminus of the talin F0 head domain
-
-
?
troponin I + H2O
?
-
degradation at pH 4.0, little degradation at pH 5.o-5.6
-
?
VALSLKISIGNVVKTMQFEPST + H2O
?
-
the peptide mimicks the N-terminus of the talin F0 head domain
-
-
?
Z-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
?
-
no substrate for wild type enzyme, endopeptidase activity of mutant T11_E18del-cathepsin H
-
?
Z-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
ir
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
-
?
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
ir
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
ir
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
-
?
Arg-2-naphthylamide + H2O
Arg + 2-naphthylamine
-
97% activity of substrate Leu-2-N-naphthylamine
-
ir
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
ir
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
?
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
conventional test substrate
-
ir
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
-
-
ir
Arg-4-methylcoumaryl-7-amide + H2O
Arg + 7-amino-4-methylcoumarin
-
conventional test substrate
-
ir
Arg-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
assay at pH 5.5, 37°C
-
-
?
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-L-Phe-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
specific substrate
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
-
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Lys-7-amido-4-methylcoumarin + H2O
L-Lys + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
Proteins + H2O
?
-
involved in human glioma, anaplastic astrocytoma, and glioblastoma progression and invasion
-
-
?
Proteins + H2O
?
-
involved in cell growth, protein degradation, synthesis of peptide hormones and tumor metastasis
-
-
?
Proteins + H2O
?
-
rather broad specificity of aminopeptidase activity
-
-
?
additional information
?
-
-
activity as endopeptidase and aminopeptidase on synthetic substrates
-
-
?
additional information
?
-
-
enzyme is involved in maturation of the biologically active surfactant protein B
-
-
?
additional information
?
-
-
does not cleave benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin, benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin, and benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
procathepsin H is not capable of autocleavage at pH 4.5-6.5
-
-
?
additional information
?
-
-
procathepsin H is not capable of autocleavage at pH 4.5-6.5
-
-
?
additional information
?
-
-
activity as endopeptidase and aminopeptidase on synthetic substrates
-
-
?
additional information
?
-
-
influence of Pro in position P1 to P3 on rate of peptide hydrolysis, P3 i.e. 3rd amino acid in N-terminal direction relative to point of cleavage, greatest increase in activity after substrate elongation to tetrapeptide
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is involved in maturation of the biologically active surfactant protein B
-
-
?
Proteins + H2O
?
-
involved in human glioma, anaplastic astrocytoma, and glioblastoma progression and invasion
-
-
?
Proteins + H2O
?
-
involved in cell growth, protein degradation, synthesis of peptide hormones and tumor metastasis
-
-
?
Proteins + H2O
?
-
rather broad specificity of aminopeptidase activity
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-2-[3-(2-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2E)-2-[3-(2-methoxyphenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2E)-2-[3-(3-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2E)-2-[3-(3-methoxyphenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2E)-2-[3-(4-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2E)-2-[3-(4-methylphenyl)-1-phenylpropylidene]hydrazinecarboxamide
-
(2Z)-2-(2-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
(2Z)-2-(2-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
(2Z)-2-(2-nitrobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 6.10% activity remaining
(2Z)-2-(3-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
(2Z)-2-(3-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
(2Z)-2-(4-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 20.80% activity remaining
(2Z)-2-(4-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 37.00% activity remaining
(2Z)-2-(4-nitrobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 25.40% activity remaining
(2Z)-2-benzylidenehydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 14.60% activity remaining
(2Z)-2-[(2E)-3-(2-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(2-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(3-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(3-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(3-nitrophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(4-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(4-methylphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
-
(2Z)-2-[(2E)-3-(4-nitrophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C, 1 mM, 13.5% activity remaining
1-[4-(2-methoxyphenyl)piperazin-1-yl]-3-[3-(5-methyl-1,3,4-oxadiazol-2-yl)phenoxy]propan-2-ol
-
1H-spiro(cyclohexane-1,2-quinazolin)-4(3H)-one
-
competitive inhibition, 94.86% residual activity at 0.1 mM
2-(2-chlorophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 25.12% activity remaining
2-(2-methoxyphenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 45.35% activity remaining
2-(2-nitrophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 92.07% activity remaining
2-(3-chlorophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 36.19% activity remaining
2-(3-methoxyphenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 48.08% activity remaining
2-(3-nitrophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 59.47% activity remaining
2-(4-(dimethylamino)phenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 88.37% residual activity at 0.1 mM
2-(4-bromophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 91.62% residual activity at 0.1 mM
2-(4-chlorophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 98.11% residual activity at 0.1 mM
2-(4-chlorophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 30.98% activity remaining
2-(4-fluorophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 94.05% residual activity at 0.1 mM
2-(4-methoxyphenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 95.94% residual activity at 0.1 mM
2-(4-methoxyphenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 43.49% activity remaining
2-(4-methylphenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 39.18% residual activity at 0.1 mM
2-(4-methylphenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 49.89% activity remaining
2-(4-nitrophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 81.89% residual activity at 0.1 mM
2-(4-nitrophenyl)-5-phenyl-1,3,4-oxadiazole
1 mM, 69.33% activity remaining
2-chlorobenzohydrazide
-
non-competitive inhibition; non-competitive inhibition, 89.46% residual activity at 0.01 mM
2-methoxybenzohydrazide
-
non-competitive inhibition; non-competitive inhibition, 97.83% residual activity at 0.01 mM
2-phenyl-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 79.73% residual activity at 0.1 mM
2-[[(2E)-2-(1,3-benzodioxol-5-ylmethylidene)hydrazinyl]carbonyl]-3-phenyl-1H-indole-5-sulfonamide
-
3,5-diphenyl-4-amino-1,2,4-triazole
-
non-competitive inhibition; non-competitive inhibition, 69.73% residual activity at 0.01 mM
3-(2'-hydroxy-3'-methylphenyl)-5-(2'-hydroxy-3'-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 88.11% residual activity at 0.01 mM
3-(2'-methylphenyl)-5-(2'-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 82.97% residual activity at 0.01 mM
3-(2-hydroxy-3-methylphenyl)-5-(2-hydroxy-3-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-(2-methylphenyl)-5-(2-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-(3'-aminophenyl)-5-(3'-aminophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 16.37% residual activity at 0.01 mM
3-(3'-methylphenyl)-5-(3'-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 79.45% residual activity at 0.01 mM
3-(3'-nitrophenyl)-5-(3'-nitrophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 45.13% residual activity at 0.01 mM
3-(3-aminophenyl)-5-(3-aminophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-(3-methylphenyl)-5-(3-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-(4'-chlorophenyl)-5-(4'-chlorophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 24.35% residual activity at 0.01 mM
3-(4'-methylphenyl)-5-(4'-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 89.46% residual activity at 0.01 mM
3-(4-chlorophenyl)-1-(4-(N'-4-nitrophenyl)methylene)aminophenyl)prop-2-en-1-one
-
3-(4-chlorophenyl)-5-(4-chlorophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-(4-methylphenyl)-5-(4-methylphenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition
3-phenyl-5-(4'-nitrophenyl)-4-amino-1,2,4-triazole
-
non-competitive inhibition, 78.11% residual activity at 0.01 mM
4-bromo-N-[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]benzenecarbohydrazonoyl chloride
-
4-hydroxybenzohydrazide
-
non-competitive inhibition; non-competitive inhibition, 91.62% residual activity at 0.01 mM
4-methoxybenzohydrazide
-
non-competitive inhibition; non-competitive inhibition, 45% residual activity at 0.01 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
95% inhibition at 0.1 mM, substrate Leu-2-N-naphthylamine
acetyl-(Ala)2-Pro-Ala-CH2Cl
-
100% inhibition at 0.1 mM, substrate Leu-2-N-naphthylamine
acetyl-(Ala)2-Pro-Val-CH2Cl
-
100% inhibition at 0.1 mM, substrate Leu-2-N-naphthylamine
benzyloxycarbonyl-Gly-Leu-NH
-
inhibits processing of proenzyme to active form
Benzyloxycarbonyl-Leu-NH2
-
inhibits formation of active enzyme from procathepsin H
CNWAAGYNCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CNWTLGGYKCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CPI-H
-
peptide inhibitor of 13 kDa from rabbit skeletal muscle, noncompetitive
-
CPI-L
-
peptide inhibitor of 23 kDa from rabbit skeletal muscle, noncompetitive
-
CWEWGGWHCGGSS-OH
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
CWSMMGFQCGGGS-NH2
-
cyclic peptide with intramolecular disulfide bond, comparison of inhibitory effect with cathepsin K, cathepsin L, cathepsin B and papain
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
N'-(4-[(E)-[2-(2-formylphenyl)hydrazinylidene]methyl]phenyl)-N-phenylimidoformamide
-
N-(3-methoxypyrazin-2-yl)-2-[4-(1,3,4-oxadiazol-2-yl)phenyl]pyridine-3-sulfonamide
-
N-benzoyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
55.13% residual activity at 0.01 mM
N-benzoyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
79.37% residual activity at 0.01 mM
N-benzoyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
34.77% residual activity at 0.01 mM
N-benzoyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
44.2% residual activity at 0.01 mM
N-benzoyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
76.06% residual activity at 0.01 mM
N-benzoyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
27.49% residual activity at 0.01 mM
N-benzoyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
62.47% residual activity at 0.01 mM
N-benzoyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
69.69% residual activity at 0.01 mM
N-benzoyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
28.77% residual activity at 0.01 mM
N-benzyl-5-hydroxy-1-methyl-2-[2-[(1,3,4-oxadiazol-2-ylcarbonyl)amino]propan-2-yl]-6-oxo-1,6-dihydropyrimidine-4-carboxamide
-
N-formyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
61.38% residual activity at 10 mM
N-formyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
92.97% residual activity at 0.001 mM
N-formyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
30.2% residual activity at 0.001 mM
N-formyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
49.57% residual activity at 0.001 mM
N-formyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
86.03% residual activity at 0.001 mM
N-formyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
14.15% residual activity at 0.001 mM
N-formyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
69.38% residual activity at 0.001 mM
N-formyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
80.06% residual activity at 0.001 mM
N-formyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
27.64% residual activity at 0.001 mM
N-[(1E,2S)-1-(2-benzoylhydrazinylidene)-4-phenylbutan-2-yl]-N2-(piperidin-1-ylcarbonyl)-L-leucinamide
-
N-[(5S,8S,11S,13Z,19S)-8-(4-fluorobenzyl)-5-formyl-2,7,10-trioxo-18-oxa-1,6,9-triazabicyclo[17.2.1]docos-13-en-11-yl]-5-methyl-1,2-oxazole-3-carboxamide
-
N-[(E)-[(2-chlorophenyl)imino]methyl]benzamide
1 mM, 25.66% activity remaining
N-[(E)-[(2-methoxyphenyl)imino]methyl]benzamide
1 mM, 41.11% activity remaining
N-[(E)-[(2-nitrophenyl)imino]methyl]benzamide
1 mM, 90.07% activity remaining
N-[(E)-[(3-chlorophenyl)imino]methyl]benzamide
1 mM, 39.45% activity remaining
N-[(E)-[(3-methoxyphenyl)imino]methyl]benzamide
1 mM, 49.59% activity remaining
N-[(E)-[(3-nitrophenyl)imino]methyl]benzamide
1 mM, 73.01% activity remaining
N-[(E)-[(4-chlorophenyl)imino]methyl]benzamide
1 mM, 24.75% activity remaining
N-[(E)-[(4-methoxyphenyl)imino]methyl]benzamide
1 mM, 40.2% activity remaining
N-[(E)-[(4-methylphenyl)imino]methyl]benzamide
1 mM, 39.93% activity remaining
N-[(E)-[(4-nitrophenyl)imino]methyl]benzamide
1 mM, 75.07% activity remaining
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
p-Hydroxymercuriphenylsulfonic acid
-
83% inhibition at 0.011 mM, substrate Leu-2-N-naphthylamine
phenylacetyl hydrazine
-
non-competitive inhibition; non-competitive inhibition, 81.08% residual activity at 0.01 mM
(2E)-1,3-diphenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 93.50% activity remaining
(2E)-3-(2-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 42.00% activity remaining
(2E)-3-(2-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 66.00% activity remaining
(2E)-3-(3-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 0.30% activity remaining
(2E)-3-(3-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 51.40% activity remaining
(2E)-3-(3-nitrophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 55.20% activity remaining
(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 73.30% activity remaining
(2E)-3-(4-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 55.60% activity remaining
(2E)-3-(4-methylphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 92.50% activity remaining
(2E)-3-(4-nitrophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 61.80% activity remaining
2,2'-dipyridyl disulfide
-
96% inhibition at 0.1 mM, substrate Leu-2-N-naphthylamine
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
90% inhibition at 0.001 mM, substrate Leu-2-N-naphthylamine
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
100% inhibition at 0.1 mM
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
E-64-d, inhibits processing of proenzyme to synthetic analogs
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
-
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
E-64-d, inhibits processing of proenzyme to active form
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
-
65-76% inhibition at 0.01 mg/ml, isoform-dependent
Thiol proteinase inhibitor
-
from human serum, human lung, molecular weights: 13000 and 80000, the latter including haptoglobin, 4-7% inhibition
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
Thiol proteinase inhibitor
-
proteinase inhibitor from rat, man, hog, Tetrahymena, tuna, chicken, toad, purified rat lung inhibitors have molecular weight of 14000, purified hog kidney inhibitors have molecular weight of 11000, also high molecular weight inhibitors in human and rat serum, tissue distributions in humans and rat: inhibitors widely distributed, probaly regulatory function
-
additional information
-
amastatin, arphamenine A, and bestatin have no effect on cathepsin H
-
additional information
2,5-diaryloxadiazoles and their precursors as inhibitors of cathepsins B, H and L, synthesis and inhibitory potencies, pharmacological evaluation, molecular docking, overview. Structure-activity relationship studies show that 2,5-diaryloxadiazoles are less inhibitory than their precursors, N-subsituted benzylidenebenzohydrazides. Cathepsin H activity is maximally inhibited by (2E)-3-(3-methoxyphenyl)-1-phenylprop-2-en-1-one and (2Z)-2-[(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide, assay with liver hommogenate. All compounds exhibited a competitive type of inhibition
-
additional information
chalcones, semicarbazones and pyrazolines as inhibitors of cathepsins H, synthesis and inhibitory potencies, pharmacological evaluation, molecular docking, overview. Structure-activity relationship analysis
-
additional information
semicarbazones and thiosemicarbazones as inhibitors of cathepsins H, active site docking study and structure-activity relationship analysis, comparison to cathepsin L, overview
-
additional information
synthesis of a small library of chalcones and study of their role as inhibitors of cathepsins, overview. The most potent inhibitors among all compounds are chloro-substituted compounds for cathepsin H. Docking analysis and modeling, overview
-
additional information
no significant inhibitory effect of enzyme propeptide fragments, detailed analysis using several different peptides. Recombinant enzyme lacking the mini-chain shows inhibitory interaction
-
additional information
molecular basis for the inhibition of the mature enzyme by the prodomain. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
-
additional information
-
molecular basis for the inhibition of the mature enzyme by the prodomain. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain
-
additional information
-
amastatin, arphamenine A, and bestatin have no effect on cathepsin H
-
additional information
-
not inhibitory: pepstatin, bestatin, puromycin, phenylmethylsulfonylfluoride, trypsin inhibitor
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
recombinant CatB3 shows enzymatic activity when autoprocessed at pH 4.5 in the presence of dithiothreitol and dextran sulfate
-
additional information
-
recombinant CatB3 shows enzymatic activity when autoprocessed at pH 4.5 in the presence of dithiothreitol and dextran sulfate
-
additional information
procathepsin H is not capable of autoactivation and requires other proteases such as cathepsin L for its activation
-
additional information
-
procathepsin H is not capable of autoactivation and requires other proteases such as cathepsin L for its activation
-
additional information
-
metalloendopeptidases involved in processing of procathepsin to active enzyme
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abortion, Habitual
Altered expression of genes involved in the production and degradation of endometrial extracellular matrix in patients with unexplained infertility and recurrent miscarriages.
Alveolitis, Extrinsic Allergic
The significance of cathepsins, thrombin and aminopeptidase in diffuse interstitial lung diseases.
Alzheimer Disease
Comparison of cathepsin protease activities in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease.
Arthritis
Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases.
Arthritis, Rheumatoid
Determination of cathepsins B and H in sera and synovial fluids of patients with different joint diseases.
Astrocytoma
Expression and the role of cathepsin H in human glioma progression and invasion.
Atherosclerosis
Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.
Carcinogenesis
Cathepsin H indirectly regulates morphogenetic protein-4 (BMP-4) in various human cell lines.
Carcinogenesis
[Changes in active cysteine cathepsins in lysosomes from tissues thyroid papillary carcinomas with various biological characteristics].
Carcinoma
Alterations in cathepsin H activity and protein patterns in human colorectal carcinomas.
Carcinoma
Prognostic value of cathepsins B, H, L, D and their endogenous inhibitors stefins A and B in head and neck carcinoma.
Carcinoma, Hepatocellular
Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells.
Carcinoma, Papillary
[Changes in active cysteine cathepsins in lysosomes from tissues thyroid papillary carcinomas with various biological characteristics].
Carcinoma, Renal Cell
Cathepsin H expression distinguishes oncocytomas from renal cell carcinomas.
Carcinosarcoma
Molecular cloning of rat precursor cathepsin H and the expression of five lysosomal cathepsins in normal tissues and in a rat carcinosarcoma.
cathepsin h deficiency
Cathepsin H deficiency decreases hypoxia-ischemia-induced hippocampal atrophy in neonatal mice through attenuated TLR3/IFN-? signaling.
cathepsin h deficiency
Cathepsin H deficiency in mice induces excess Th1 cell activation and early-onset of EAE though impairment of toll-like receptor 3 cascade.
Cholesteatoma
Gene expression analysis of human middle ear cholesteatoma using complementary DNA arrays.
Colorectal Neoplasms
Alterations in cathepsin H activity and protein patterns in human colorectal carcinomas.
Colorectal Neoplasms
Serum cathepsin H as a potential prognostic marker in patients with colorectal cancer.
Cryptogenic Organizing Pneumonia
The significance of cathepsins, thrombin and aminopeptidase in diffuse interstitial lung diseases.
Diabetes Mellitus, Type 1
Genetic and environmental factors regulate the type 1 diabetes gene CTSH via differential DNA methylation.
Encephalomyelitis
Cathepsin H deficiency in mice induces excess Th1 cell activation and early-onset of EAE though impairment of toll-like receptor 3 cascade.
Encephalomyelitis, Autoimmune, Experimental
Cathepsin H deficiency in mice induces excess Th1 cell activation and early-onset of EAE though impairment of toll-like receptor 3 cascade.
Epstein-Barr Virus Infections
Epstein-Barr virus-induced genes: first lymphocyte-specific G protein-coupled peptide receptors.
Gallbladder Neoplasms
Identification of prosaposin and transgelin as potential biomarkers for gallbladder cancer using quantitative proteomics.
Glioblastoma
Expression and the role of cathepsin H in human glioma progression and invasion.
Huntington Disease
Comparison of cathepsin protease activities in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease.
Idiopathic Pulmonary Fibrosis
The significance of cathepsins, thrombin and aminopeptidase in diffuse interstitial lung diseases.
Infections
Channel catfish, Ictalurus punctatus, cysteine proteinases: cloning, characterisation and expression of cathepsin H and L.
Infections
Diagnosis of Fasciola gigantica infection using a monoclonal antibody-based sandwich ELISA for detection of circulating cathepsin B3 protease.
Infections
The combined recombinant cathepsin L1H and cathepsin B3 vaccine against Fasciola gigantica infection.
Infertility
Altered expression of genes involved in the production and degradation of endometrial extracellular matrix in patients with unexplained infertility and recurrent miscarriages.
Inflammatory Breast Neoplasms
Cathepsin B, cathepsin H, cathepsin X and cystatin C in sera of patients with early-stage and inflammatory breast cancer.
Insulinoma
Immunocytochemical localization of cathepsins B and H in human pancreatic endocrine cells and insulinoma cells.
Lung Neoplasms
Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking.
Lung Neoplasms
[Serum activity of chitotriosidase, lysozyme and cathepsin H in patients with lung cancer and patients with inflammatory exudate (preliminary report)]
Melanoma
Cathepsins B, H, and L and their inhibitors stefin A and cystatin C in sera of melanoma patients.
Melanoma
Enzyme-linked immunosorbent assay for the detection of total cathepsin H in human tissue cytosols and sera.
Melanoma
Generation of a double binary transgenic zebrafish model to study myeloid gene regulation in response to oncogene activation in melanocytes.
Melanoma, Amelanotic
Cathepsin B-like activity in viable tumor cells isolated from rodent tumors.
Mouth Neoplasms
[Activity of cathepsin H in blood and biopsies of patients with precancerous conditions and mouth cancer]
Multiple Sclerosis
Cathepsin H deficiency in mice induces excess Th1 cell activation and early-onset of EAE though impairment of toll-like receptor 3 cascade.
Neoplasm Metastasis
Cathepsins B, H, and L and their inhibitors stefin A and cystatin C in sera of melanoma patients.
Neoplasms
Alterations in cathepsin H activity and protein patterns in human colorectal carcinomas.
Neoplasms
Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level.
Neoplasms
Cathepsin H indirectly regulates morphogenetic protein-4 (BMP-4) in various human cell lines.
Neoplasms
Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells.
Neoplasms
Cathepsins in basal cell carcinomas: activity, immunoreactivity and mRNA staining of cathepsins B, D, H and L.
Neoplasms
Cysteine proteases and cell differentiation: excystment of the ciliated protist Sterkiella histriomuscorum.
Neoplasms
Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking.
Neoplasms
Deletion of cathepsin H perturbs angiogenic switching, vascularization and growth of tumors in a mouse model of pancreatic islet cell cancer.
Neoplasms
Design, synthesis and docking studies of bischalcones based quinazoline-2(1H)-ones and quinazoline-2(1H)-thiones derivatives as novel inhibitors of cathepsin B and cathepsin H.
Neoplasms
Increased expression of cathepsins and obesity-induced proinflammatory cytokines in lacrimal glands of male NOD mouse.
Neoplasms
Lysosomal proteases cathepsins D, B, H, L and their inhibitors stefins A and B in head and neck cancer.
Neoplasms
Prognostic value of cathepsins B, H, L, D and their endogenous inhibitors stefins A and B in head and neck carcinoma.
Neoplasms
Serum cathepsin H as a potential prognostic marker in patients with colorectal cancer.
Neoplasms
[Activity of cathepsin H in blood and biopsies of patients with precancerous conditions and mouth cancer]
Neoplasms
[Changes in active cysteine cathepsins in lysosomes from tissues thyroid papillary carcinomas with various biological characteristics].
Osteosarcoma
Cathepsin H indirectly regulates morphogenetic protein-4 (BMP-4) in various human cell lines.
Pancreatic Neoplasms
Isolation of tissue-type plasminogen activator, cathepsin H, and non-specific cross-reacting antigen from SK-PC-1 pancreas cancer cells using subtractive hybridization.
Pneumonia
The significance of cathepsins, thrombin and aminopeptidase in diffuse interstitial lung diseases.
Polycystic Kidney, Autosomal Dominant
Functional defects in lysosomal enzymes in autosomal dominant polycystic kidney disease (ADPKD): abnormalities in synthesis, molecular processing, polarity, and secretion.
Polyradiculoneuropathy, Chronic Inflammatory Demyelinating
Cystatin C and cathepsin B in CSF from patients with inflammatory neurologic diseases.
Precancerous Conditions
[Activity of cathepsin H in blood and biopsies of patients with precancerous conditions and mouth cancer]
Prostatic Intraepithelial Neoplasia
Analysis of a truncated form of cathepsin H in human prostate tumor cells.
Prostatic Neoplasms
Cathepsin H indirectly regulates morphogenetic protein-4 (BMP-4) in various human cell lines.
Prostatic Neoplasms
Cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells.
Pulmonary Alveolar Proteinosis
Cathepsin H and napsin A are active in the alveoli and increased in alveolar proteinosis.
Pulmonary Eosinophilia
The significance of cathepsins, thrombin and aminopeptidase in diffuse interstitial lung diseases.
Thymoma
A mechanistic target of rapamycin complex 1/2 (mTORC1)/V-Akt murine thymoma viral oncogene homolog 1 (AKT1)/cathepsin H axis controls filaggrin expression and processing in skin, a novel mechanism for skin barrier disruption in patients with atopic dermatitis.
Thyroid Neoplasms
Favorable Prognostic Impact of Cathepsin H (CTSH) High Expression in Thyroid Carcinoma.
Tuberculosis
Investigating potential transmission of antimicrobial resistance in an open-plan hospital ward: a cross-sectional metagenomic study of resistome dispersion in a lower middle-income setting.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.082
benzoyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
pH 6.5, 25°C, mutant lacking the mini chain
-
0.092
Z-L-Phe-L-Arg-NH-4-methylcoumaryl-7-amide
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
additional information
additional information
-
pH and temperature dependence of kcat/Km
-
0.025
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, 25°C, native enzyme
0.038
benzoyl-L-Phe-L-Val-L-Arg-4-methylcoumaryl-7-amide
-
pH 6.5, 25°C, mutant lacking the mini chain
3.6
H-L-Arg-NH-4-methylcoumaryl-7-amide
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH and temperature dependence of kcat/Km
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.066
(2E)-2-(1,3-diphenylpropylidene)hydrazinecarboxamide
pH 6.0, 37°C
0.033
(2E)-2-[3-(2-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.054
(2E)-2-[3-(2-methoxyphenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.06
(2E)-2-[3-(3-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.066
(2E)-2-[3-(3-methoxyphenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.033
(2E)-2-[3-(3-nitrophenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.021
(2E)-2-[3-(4-chlorophenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.04
(2E)-2-[3-(4-methylphenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.032
(2E)-2-[3-(4-nitrophenyl)-1-phenylpropylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.208
(2Z)-2-(2-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
0.28
(2Z)-2-(2-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
0.009
(2Z)-2-(2-nitrobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 6.10% activity remaining
0.704
(2Z)-2-(3-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
0.016
(2Z)-2-(3-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, no activity remaining
0.17
(2Z)-2-(4-chlorobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 20.80% activity remaining
0.35
(2Z)-2-(4-methoxybenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 37.00% activity remaining
0.2
(2Z)-2-(4-nitrobenzylidene)hydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 25.40% activity remaining
0.06
(2Z)-2-benzylidenehydrazinecarbothioamide
pH 6.0, 37°C, 1 mM, 14.60% activity remaining
0.1
(2Z)-2-[(2E)-1,3-diphenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.043
(2Z)-2-[(2E)-3-(2-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.066
(2Z)-2-[(2E)-3-(2-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.096
(2Z)-2-[(2E)-3-(3-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.074
(2Z)-2-[(2E)-3-(3-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.023
(2Z)-2-[(2E)-3-(3-nitrophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.029
(2Z)-2-[(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.054
(2Z)-2-[(2E)-3-(4-methoxyphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.045
(2Z)-2-[(2E)-3-(4-methylphenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C
0.025
(2Z)-2-[(2E)-3-(4-nitrophenyl)-1-phenylprop-2-en-1-ylidene]hydrazinecarboxamide
pH 6.0, 37°C, 1 mM, 13.50% activity remaining
0.01858
2-(4-(dimethylamino)phenyl)-2,3-dihydroquinazolin-4(1H)-one
-
at pH 7.0 and 37°C
0.02325
2-(4-chlorophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
at pH 7.0 and 37°C
0.00818
2-(4-fluorophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
at pH 7.0 and 37°C
0.05682
2-(4-methoxyphenyl)-2,3-dihydroquinazolin-4(1H)-one
-
at pH 7.0 and 37°C
0.192
3,5-diphenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.0781
3-(2'-hydroxy-3'-methylphenyl)-5-(2'-hydroxy-3'-methylphenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0532
3-(2'-methylphenyl)-5-(2'-methylphenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0214
3-(2-chlorophenyl)-1-(4-bromophenyl)prop-2-en-1-one
pH 5.0, 37°C
0.0989
3-(2-chlorophenyl)-1-(napthalen-3-yl)prop-2-en-1-one
pH 5.0, 37°C
0.0472
3-(2-chlorophenyl)-1-(pyridin-2-yl)prop-2-en-1-one
pH 5.0, 37°C
0.0781
3-(2-hydroxy-3-methylphenyl)-5-(2-hydroxy-3-methylphenyl)-4-amino-1,2,4-triazole
-
pH 5, 37°C
0.0532
3-(2-methylphenyl)-5-(2-methylphenyl)-4-amino-1,2,4-triazole
-
pH 5, 37°C
0.002
3-(3'-aminophenyl)-5-(3'-aminophenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0387
3-(3'-methylphenyl)-5-(3'-methylphenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0086
3-(3'-nitrophenyl)-5-(3'-nitrophenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.128
3-(3-chlorophenyl)-1-(4-aminophenyl)prop-2-en-1-one
pH 5.0, 37°C
0.0317
3-(3-chlorophenyl)-1-(4-fluorophenyl)prop-2-en-1-one
pH 5.0, 37°C
0.163
3-(3-chlorophenyl)-1-(4-hydroxyphenyl)-prop-2-en-1-one
pH 5.0, 37°C
0.0387
3-(3-methylphenyl)-5-(3-methylphenyl)-4-amino-1,2,4-triazole
-
pH 5, 37°C
0.0033
3-(4'-chlorophenyl)-5-(4'-chlorophenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0901
3-(4'-methylphenyl)-5-(4'-methylphenyl)-4-amino-1,2,4-triazole
-
at pH 7.0 and 37°C
0.0133
3-(4-chlorophenyl)-1-(4-(N'-4-nitrophenyl)methylene)aminophenyl)prop-2-en-1-one
pH 5.0, 37°C
0.0416
3-(4-chlorophenyl)-1-(4-methylphenyl)prop-2-en-1-one
pH 5.0, 37°C
0.405
3-(4-chlorophenyl)-1-(4-nitrophenyl)prop-2-en-1-one
pH 5.0, 37°C
0.0033
3-(4-chlorophenyl)-5-(4-chlorophenyl)-4-amino-1,2,4-triazole
-
pH 5, 37°C
0.0901
3-(4-methylphenyl)-5-(4-methylphenyl)-4-amino-1,2,4-triazole
-
pH 5, 37°C
0.06
5-(2-chlorophenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.04
5-(2-methoxyphenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.025
5-(3-chlorophenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.043
5-(3-methoxyphenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.038
5-(3-nitrophenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.066
5-(4-chlorophenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.048
5-(4-methoxyphenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.048
5-(4-methylphenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.06
5-(4-nitrophenyl)-3-phenyl-4,5-dihydro-1H-pyrazole-1-carboxamide
pH 6.0, 37°C
0.00189
N-benzoyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00181
N-benzoyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00503
N-benzoyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00301
N-benzoyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.0041
N-benzoyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00014
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.00168
N-[(E)-[(3-methoxyphenyl)imino]methyl]benzamide
pH 5.0, 37°C
0.00133
N-[(E)-[(4-methoxyphenyl)imino]methyl]benzamide
pH 5.0, 37°C
0.0014
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
8.19
(2E)-1,3-diphenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 93.50% activity remaining
0.43
(2E)-3-(2-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 42.00% activity remaining
1.08
(2E)-3-(2-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 66.00% activity remaining
0.027
(2E)-3-(3-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 0.30% activity remaining
0.63
(2E)-3-(3-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 51.40% activity remaining
0.7
(2E)-3-(3-nitrophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 55.20% activity remaining
1.66
(2E)-3-(4-chlorophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 73.30% activity remaining
0.71
(2E)-3-(4-methoxyphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 55.60% activity remaining
7.04
(2E)-3-(4-methylphenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 92.50% activity remaining
1
(2E)-3-(4-nitrophenyl)-1-phenylprop-2-en-1-one
pH 6.0, 37°C, 1 mM, 61.80% activity remaining
0.000000095
chicken egg white cystatin
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
-
0.0032
N-benzoyl-3,5-diphenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00965
N-benzoyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00144
N-benzoyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00098
N-benzoyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00127
N-benzoyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000174
N-formyl-3,5-diphenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000135
N-formyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000387
N-formyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.0000963
N-formyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00013
N-formyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000272
N-formyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.0000519
N-formyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000137
N-formyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000221
N-formyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.000058
N-formyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02256
0.02291
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.5
6.5
6.5 - 7.2
6.8
6.5
-
substrates Arg-4-methylcoumaryl-7-amide and citrulline-4-methylcoumaryl-7-amide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
38
40
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
up-regulation of catfish cathepsin H and L transcripts during the early stage of Edwardsiella ictaluri infection
UniProt
brenda
-
30138, 36634, 36637, 638815, 638816, 638818, 638829, 638831, 638834, 638836, 638842, 650475, 653418, 667333, 667413
-
-
brenda
-
36634, 36637, 586915, 638817, 638819, 638820, 638821, 638823, 638827, 638829, 638831, 638834, 638837
-
-
brenda
immunological differentiation from rat liver cathepsin B, human and rabbit liver cathepsin H
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression level in intestine and gill, but barely in other tissues
brenda
high expression level in intestine and gill, but barely in other tissues
brenda
cathepsin B3 is detected in the whole body extract of metacercariae and newly excysted juveniles but not in 4-week-old juveniles or adult parasites
brenda
-
cathepsin H is highly expressed in the secretory organelles of alveolar type II pneumocytes
brenda
-
683 ng /mg protein, distribution in tissues and peripheral blood cells
brenda
additional information
-
1429 ng /mg protein, distribution in tissues and peripheral blood cells
brenda
-
556 ng /mg protein, distribution in tissues and peripheral blood cells
brenda
-
543 ng /mg protein, distribution in tissues and peripheral blood cells
brenda
-
158-298 ng /1000000 cells, distribution in tissues and peripheral blood cells
brenda
-
480 ng /mg protein, distribution in tissues and peripheral blood cells
brenda
additional information
immunofluorescent and immunohistochemic analysis
brenda
additional information
-
immunofluorescent and immunohistochemic analysis
brenda
additional information
high expression level in intestine and gill, but barely in other tissues
brenda
additional information
-
high expression level in intestine and gill, but barely in other tissues
brenda
additional information
immunofluorescent and immunohistochemic analysis
brenda
additional information
-
immunofluorescent and immunohistochemic analysis
brenda
additional information
-
immunofluorescent and immunohistochemic analysis
-
brenda
additional information
immunofluorescent and immunohistochemic analysis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
biosynthesis in endoplasmic reticulum, proteolytic cleavage of proenzyme during translocation to lysosomes
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases
malfunction
metabolism
physiological function
additional information
malfunction
-
lymphocytes deficient in CatH are still capable of generating active granzyme B. CatH-deficient mice do not show a gross morphological phenotype and no impairment of reproductive capacity or breeding behavior or nursing
malfunction
-
cathepsin H-deficient mice show no gross phenotype and their development is normal without growth retardation. Broncho-alveolar lavage from cathepsin H-deficient mice contain lower levels of pulmonary surfactant protein B
malfunction
-
knockout of the cathepsin H gene results in 50% reduction of (Met)enkephalin in mouse brain. Cathepsin H deficient mice also show a substantial 80% decrease in galanin peptide neurotransmitter levels in brain
malfunction
-
specific inhibition of cathepsin H increases the activation of alphabeta3-integrin on PC-3 cells
malfunction
loss of CTSH inhibits filaggrin processing, but not expression, and impairs epidermal barrier function, evidence for compensation in CTSH knockout
malfunction
loss of CTSH inhibits filaggrin processing, but not expression, and impairs epidermal barrier function, evidence for compensation in CTSH knockout
malfunction
reduced filaggrin processing and impaired epidermal barrier in CTSH-deficient mouse skin, histology of Ctsh-/-, Ctsh+/-, and wild-type mouse neonatal skin, overview. Loss of CTSH increases skin macrophage counts, mast cell degranulation, and proinflammatory molecule expression. Loss of CTSH inhibits filaggrin processing, but not expression, and impairs epidermal barrier function, evidence for compensation in CTSH knockout
malfunction
-
reduced filaggrin processing and impaired epidermal barrier in CTSH-deficient mouse skin, histology of Ctsh-/-, Ctsh+/-, and wild-type mouse neonatal skin, overview. Loss of CTSH increases skin macrophage counts, mast cell degranulation, and proinflammatory molecule expression. Loss of CTSH inhibits filaggrin processing, but not expression, and impairs epidermal barrier function, evidence for compensation in CTSH knockout
-
metabolism
phosphoinositide 3-kinase signaling through AKT1 is required for the proteolytic processing of filaggrin during late epidermal terminal differentiation
metabolism
phosphoinositide 3-kinase signaling through AKT1 is required for the proteolytic processing of filaggrin during late epidermal terminal differentiation
metabolism
phosphoinositide 3-kinase signaling through AKT1 is required for the proteolytic processing of filaggrin during late epidermal terminal differentiation
metabolism
-
phosphoinositide 3-kinase signaling through AKT1 is required for the proteolytic processing of filaggrin during late epidermal terminal differentiation
-
physiological function
CatB3 is a major protease antigen in Fasciola gigantica metacercariae and newly excysted juveniles
physiological function
-
cathepsin H is involved in the surfactant protein B production
physiological function
-
cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells
physiological function
-
cathepsin H plays a role in enkephalin and galanin peptide neurotransmitter production
physiological function
-
cathepsin H plays a role in enkephalin and galanin peptide neurotransmitter production
physiological function
profilaggrin to filaggrin processing is complex, requiring dephosphorylation and numerous proteolytic events, several proteases have been identified that cleave profilaggrin at specific sites, releasing the filaggrin monomers and both the N- and C-termini, including cathepsin H. CTSH is a differentiation-dependent protease coexpressed with filaggrin
physiological function
profilaggrin to filaggrin processing is complex, requiring dephosphorylation and numerous proteolytic events, several proteases have been identified that cleave profilaggrin at specific sites, releasing the filaggrin monomers and both the N- and C-termini, including cathepsin H. CTSH is a differentiation-dependent protease coexpressed with filaggrin
physiological function
profilaggrin to filaggrin processing is complex, requiring dephosphorylation and numerous proteolytic events, several proteases have been identified that cleave profilaggrin at specific sites, releasing the filaggrin monomers and both the N- and C-termini, including cathepsin H. CTSH is a differentiation-dependent protease coexpressed with filaggrin
physiological function
the mature enzyme is inhibited by its own prodomain after maturation cleavage. Upon activation, cathepsin H displays a distinct proteolytic activity among the papain superfamily, functioning predominantly as an aminopeptidase that cleaves a single N-terminal residue from a polypeptide chain. Cathepsin H has also been shown to act as an endopeptidase, although with much lower efficiency
physiological function
-
profilaggrin to filaggrin processing is complex, requiring dephosphorylation and numerous proteolytic events, several proteases have been identified that cleave profilaggrin at specific sites, releasing the filaggrin monomers and both the N- and C-termini, including cathepsin H. CTSH is a differentiation-dependent protease coexpressed with filaggrin
-
additional information
the catalytic triad residues Cys26, His166 and Asn186 of procathepsin H reside in the active site cleft
additional information
-
the catalytic triad residues Cys26, His166 and Asn186 of procathepsin H reside in the active site cleft
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATB_MEDTR
350
0
38752
Swiss-Prot
Secretory Pathway (Reliability: 2)
CATH_BOVIN
335
0
37351
Swiss-Prot
Secretory Pathway (Reliability: 1)
CATH_HUMAN
335
0
37394
Swiss-Prot
Secretory Pathway (Reliability: 1)
CATH_MOUSE
333
0
37170
Swiss-Prot
Secretory Pathway (Reliability: 1)
CATH_PIG
335
0
37455
Swiss-Prot
Secretory Pathway (Reliability: 2)
CATH_RAT
333
0
37104
Swiss-Prot
Secretory Pathway (Reliability: 1)
ALEUL_ARATH
358
0
39542
Swiss-Prot
Secretory Pathway (Reliability: 1)
ALEU_ARATH
358
1
38959
Swiss-Prot
Secretory Pathway (Reliability: 1)
ALEU_HORVU
362
1
39122
Swiss-Prot
Secretory Pathway (Reliability: 1)
B2CNZ8_PIG
297
0
33319
TrEMBL
other Location (Reliability: 3)
A0A0A1U9F9_ENTIV
306
0
33916
TrEMBL
Secretory Pathway (Reliability: 3)
B0ESM6_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
308
0
33760
TrEMBL
Secretory Pathway (Reliability: 3)
B6AJH9_CRYMR
Cryptosporidium muris (strain RN66)
400
1
45992
TrEMBL
other Location (Reliability: 3)
L7FKS0_ENTIV
1005
0
109902
TrEMBL
Secretory Pathway (Reliability: 4)
B2D1T3_PIG
251
0
27876
TrEMBL
other Location (Reliability: 1)
B0EIS2_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
311
0
33645
TrEMBL
Secretory Pathway (Reliability: 4)
B0ENK4_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
650
1
73714
TrEMBL
Secretory Pathway (Reliability: 1)
A0A061I4G4_CRIGR
373
0
41896
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6YLP1_DAVIN
163
1
18467
TrEMBL
Mitochondrion (Reliability: 3)
A0A0B2P9L6_GLYSO
296
0
32846
TrEMBL
Mitochondrion (Reliability: 5)
G0QSX6_ICHMG
Ichthyophthirius multifiliis (strain G5)
229
0
25446
TrEMBL
other Location