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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 enzyme appears in viruses and cellular organisms
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
number of possible subsites: three
-
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
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
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
-
-
endopeptidase; 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
-
?
benzoyl-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-Arg + 7-amino-4-methylcoumarin
-
-
-
ir
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-2-naphthylamide + H2O
L-Leu + 2-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-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-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
?
-
-
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
1H-spiro(cyclohexane-1,2-quinazolin)-4(3H)-one
-
competitive inhibition, 94.86% residual activity at 0.1 mM
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-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-methylphenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 39.18% residual activity at 0.1 mM
2-(4-nitrophenyl)-2,3-dihydroquinazolin-4(1H)-one
-
competitive inhibition, 81.89% residual activity at 0.1 mM
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
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)-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-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-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-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
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
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
-
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
-
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
-
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 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.
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.
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.082
benzoyl-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
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
0.01858
2-(4-(dimethylamino)phenyl)-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
0.0781
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
0.0781
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
0.0387
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
0.0033
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
0.0032
N-benzoyl-3,5-diphenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.00189
N-benzoyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C
0.00965
N-benzoyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.00144
N-benzoyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 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
0.00098
N-benzoyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 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
0.00127
N-benzoyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000174
N-formyl-3,5-diphenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000135
N-formyl-5-(2-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000387
N-formyl-5-(2-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.0000963
N-formyl-5-(2-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.00013
N-formyl-5-(3-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000272
N-formyl-5-(3-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.0000519
N-formyl-5-(3-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000137
N-formyl-5-(4-chlorophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000221
N-formyl-5-(4-methoxyphenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.000058
N-formyl-5-(4-nitrophenyl)-3-phenylpyrazoline
-
in 0.1 M acetate buffer, at pH 5.0 and 37°C; pH 7, 37°C
0.00014
N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-norvalinamide
-
-
0.0014
N2-(morpholin-4-ylcarbonyl)-N-[(1E,3S)-5-phenyl-1-(phenylsulfonyl)pent-1-en-3-yl]-L-leucinamide
-
-
0.000000095
chicken egg white cystatin
-
mutant T11_E18del-cathepsin H, pH 6.8, 30°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02256
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
5.5
6.5 - 7.2
6.5
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, 668521, 669215, 678509, 707715, 732111
-
-
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
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
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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
malfunction
physiological function
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
-
specific inhibition of cathepsin H increases the activation of alphabeta3-integrin on PC-3 cells
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
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
B0EIS2_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
311
0
33645
TrEMBL
G0QSX6_ICHMG
Ichthyophthirius multifiliis (strain G5)
229
0
25446
TrEMBL
B0EQC1_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
317
0
37084
TrEMBL
G0QLT6_ICHMG
Ichthyophthirius multifiliis (strain G5)
334
1
37615
TrEMBL
B0E6S6_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
435
0
48521
TrEMBL
B0ED64_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
327
0
37768
TrEMBL
B0ENK4_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
650
1
73714
TrEMBL
B0ESD9_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
470
1
53201
TrEMBL
B0E7Y2_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
300
0
34314
TrEMBL
G0QKX5_ICHMG
Ichthyophthirius multifiliis (strain G5)
331
0
38062
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
25000
26000
28000
30000
37000
38000 - 39000
deglycosylation of recombinant CatB3 with endoglycosidase H under denaturing and native conditions produces protein migrating at 38000-39000 Da
55000 - 75000
purified recombinant glycosylated proCatB3 forms migrate at approximately 55000-75000Da
22000
-
SDS-PAGE, mature (active) Ctsh typically migrates as two bands: a 28000 Da single-chain form and a 22000 Da heavy chain of the two-chain form
28000
-
SDS-PAGE, mature (active) Ctsh typically migrates as two bands: a 28000 Da single-chain form and a 22000 Da heavy chain of the two-chain form
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
additional information
-
two bands in SDS-PAGE of 23000 and 27000, respectively, interpreted as different stages of enzyme processing
additional information
-
230 residues, 8 of which belong to SS-linked minichain, high sequnece homologies to cathepsin B and other cysteine proteinases of the papain superfamily; amino acid analysis
additional information
-
protein predicted from cDNA contains 361 amino acids
additional information
-
amino acid analysis; comparison to other proteinases of the papain superfamily: high sequence homologies
additional information
-
comparison of amino acid sequence to those of cathepsin B and papain reveals high degree of homology, equal contributions of monomeric and dimeric forms, model of tertiary structure, 2 free SH-groups postulated
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
glycoprotein
the deduced amino acid sequence has three potential N-glycosylation sites at the Asn96, Asn223 and Asn267 residues
proteolytic modification
-
mutant lacking the mini chain, autocatalytic processing at pH 5.0, 37°C, processing is accelerated in presence of 0.025 mg/ml of dextran, prolonged activation results in both cases in decrease of enzyme acivtiy
proteolytic modification
-
propeptide-binding region of enzyme is structurally rearranged during maturation processing and mini-chain formation, which impairs the effective recognition of mature enzyme by its propeptide
proteolytic modification
-
time-course of synthesis and posttranslational processing: proforms of MW 41000 are converted to single-chain cathepsin of MW 28000 within 1 h of translation
proteolytic modification
-
processing in three steps from proenzyme to endopeptidase intermediate to aminopeptidase, mini-chain formed from part of propeptide that is cleaved off
side-chain modification
-
structural studies of carbohydrate moieties: 1 Asn-115-linked high-mannose type oligosaccharide per molecule, structure reported
side-chain modification
-
high-mannose oligosaccharide, one N-glycosylation site per molecule
side-chain modification
-
glycosylated residues located on rather loose surface loop
side-chain modification
-
2 mol of glucosamine and 5 mol of mannose per mol enzyme
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
comparison of structure and primary sequences of 5 papain, actinidin, cathepsins B and H and stem bromelain yields high degree of similarity
-
general and secondary structure, structure of active-site cleft, mechanistic conclusions drawn from crystallographic study, mini-chain attached to active-site cleft of enzyme body via disulfide bond, structural comparison reveals high similarity to actinidin
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutant lacking the mini chain, loss of aminopeptidase activity, increase in endopeptidase activity
additional information
-
mutant lacking the mini-chain, T11_E18del-cathepsin H, minimal aminopeptidase activity against good wild type substrates, endopeptidase activity against Z-L-Phe-L-Arg-NH-4-methylcoumaryl-7-amide, which is not cleaved by wild type
additional information
-
mutant lacking the mini chain, loss of aminopeptidase activity, increase in endopeptidase activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 M sodium acetate buffer, pH 5.2, 1 mM EDTA, several months without loss of activity
-
4°C or -20°C, 50 mM Na-acetate buffer, pH 5.0, 0.2 M NaCl, 0. 5 mM HgCl2, 1 mM EDTA
4°C or -20°C, 50-100 mM Na-acetate buffer, pH 5.5, 1 mM Na2-EDTA, 0.1% Brij 35, 5 mM Na-tetrathionate, 1 month, 0-10% loss of activity
-
4°C, 50 mM Na acetate buffer, pH 4.6, 1 mM EDTA, 1 month, concentrated preparations, no loss of activity
-
4°C or -20°C, 50 mM Na-acetate buffer, pH 5.0, 0.2 M NaCl, 0. 5 mM HgCl2, 1 mM EDTA
-
4°C or -20°C, 50 mM Na-acetate buffer, pH 5.0, 0.2 M NaCl, 0. 5 mM HgCl2, 1 mM EDTA
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, CM Sephadex column chromatography, C-5 column chromatography, DEAE Sephadex A-5 column chromatography, and Sephadex G-1 and gel filtration
-
ammonium sulfate precipitation, CM-Sephadex column chromatography, C-50 column chromatography, DEAE-Sephadex A-50., and Sephadex G-100, and gel filtration
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
tumor specific increase in cathepsin H antigen may be useful marker of tumor progression in central nervous system neoplasms
medicine
-
enzyme activity, immunoreactivity, and mRNA in most basal cell carcinomas are higher than in normal skin. Reactive cells are located between and around tumor nodules, but not in tumor nests. Enzyme in peritumoral cells may either promote invasion of the tumor cells by degradation of the extracellular matrix or may reflect an elevated activity of the surrounding immunological cells
medicine
-
enzyme from meningogioma shows a 3.5fold increased vmax-value compared to normal tissue, and a 1.3fold decrease in KM-value. Molecular weight of tumor enzyme is decreased
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lenney, J.F.; Liao, J.R.; Sugg, S.L.; Gopalakrishnan, V.; Wong, H.C.H.; Ouye, K.H.; Chan, P.W.H.
Low molecular weight inhibitors of cathepsins B, H and T in human serum, synovial fluid and CSF
Biochem. Biophys. Res. Commun.
108
1581-1587
1982
Homo sapiens
brenda
Barrett, A.J.; Kirschke, H.
Cathepsin B, Cathepsin H, and cathepsin L
Methods Enzymol.
80
535-561
1981
Homo sapiens, Rattus norvegicus
brenda
Lenney, J.F.; Tolan, J.R.; Sugai, W.J.; Lee, A.G.
Thermostable endogenous inhibitors of cathepsins B and H
Eur. J. Biochem.
101
153-161
1979
Homo sapiens, Paramecium caudatum, Rattus norvegicus, Sus scrofa, Tetrahymena pyriformis
brenda
Taniguchi, T.; Mizuochi, T.; Towatari, T.; Katunuma, N.; Kobata, A.
Structural studies on the carbohydrate moieties of rat liver cathepsins B and H
J. Biochem.
97
973-976
1985
Rattus norvegicus
brenda
Fuchs, R.; Machleidt, W.; Gassen, H.G.
Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H
Biol. Chem. Hoppe-Seyler
369
469-475
1988
Homo sapiens
brenda
Popovic, T.; Brzin, J.; Kos, J.; Lenarcic, B.; Machleidt, W.; Ritonja, A.; Hanada, K.; Turk, V.
A new purification procedure of human kidney cathepsin H, its properties ans kinetic data
Biol. Chem. Hoppe-Seyler
369
175-183
1988
Homo sapiens
-
brenda
Hara, K.; Kominami, E.; Katunuma, N.
Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages
FEBS Lett.
231
229-231
1988
Rattus norvegicus
brenda
Ritonja, A.; Popovic, T.; Kotnik, M.; Machleidt, W.; Turk, V.
Amino acid sequences of the human kidney cathepsins H and L
FEBS Lett.
228
341-345
1988
Homo sapiens
brenda
Nishimura, Y.; Amano, J.; Sato, H.; Tsuji, H.; Kato, K.
Biosynthesis of lysosomal cathepsins B and H in cultures rat hepatocytes
Arch. Biochem. Biophys.
262
159-170
1988
Rattus norvegicus
brenda
Ishidoh, K.; Imajoh, S.; Emori, Y.; Ohno, S.; Kawasaki, H.; Minami, Y.; Kominami, E.; Katunuma, N.; Suzuki, K.
Molecular cloning and sequencing of cDNA for rat cathepsin H
FEBS Lett.
226
33-37
1987
Rattus norvegicus
brenda
Brümme, D.; Bescherer, K.; Kirschke, H.; Fittkau, S.
Enzyme-substrate interactions in the hydrolysis of peptides by cathepsins B and H from rat liver
Biochem. J.
245
381-385
1987
Rattus norvegicus
brenda
Rogers, J.C.; Dean, D.; Heck, G.R.
Aleurain: a barley thiol protease closely related to mammalian cathepsin H
Proc. Natl. Acad. Sci. USA
82
6512-6516
1985
Hordeum vulgare
brenda
Kominami, E.; Tsukahara, T.; Bando, Y.; Katunuma, N.
Distribution of cathepsins B and H in rat tissues and peripheral blood cells
J. Biochem.
98
87-93
1985
Rattus norvegicus
brenda
Willenbrock, F.; Brocklehurst, K.
Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe
Biochem. J.
85
511-519
1985
Bos taurus
-
brenda
Takahashi, T.; Dehdarani, A.H.; Schmidt, P.G.; Tang, J.
Cathepsins B and H from porcine spleen
J. Biol. Chem.
259
9874-9882
1984
Sus scrofa
brenda
Takio, K.; Towatari, T.; Katunuma, N.; Teller, D.C.; Titani, K.
Homology of amino acid sequences of rat liver cathepsins B and H with that of papain
Proc. Natl. Acad. Sci. USA
80
3666-3670
1983
Rattus norvegicus
brenda
Bergmeyer, H.U.ed
Cathepsin B, cathepsin H, and cathepsin L
Methods Enzym. Anal. (3rd. ed. )
5
195-210
1984
Homo sapiens, Rattus norvegicus
-
brenda
Schwartz, W.N.; Barrett, A.J.
Human cathepsin H
Biochem. J.
191
487-497
1980
Homo sapiens, Rattus norvegicus
brenda
Singh, H.; Kalnitsky, G.
Separation of a new alpha-N-benzoylarginine-beta-naphthylamide hydrolase from cathepsin B1
J. Biol. Chem.
253
4319-4326
1978
Oryctolagus cuniculus
brenda
Sivaparvathi, M.; Sawaya, R.; Gokaslan, Z.L.; Chintala, K.S.; Rao, J.S.
Expression and the role of cathepsin H in human glioma progression and invasion
Cancer Lett.
104
121-126
1996
Homo sapiens, Rattus norvegicus
brenda
Aranishi, F.; Hara, K.; Osatomi, K.; Ishihara, T.
Substrate specificity of carp Cyprinus carpio cathepsin H with methylcoumarylamide substrates
Comp. Biochem. Physiol. B
116B
203-208
1997
Cyprinus carpio
brenda
Guncar, G.; Podobnik, M.; Pungercar, J.; Strukelj, B.; Turk, V.; Turk, D.
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function
Structure
6
51-61
1998
Homo sapiens, Sus scrofa
brenda
Rothe, M.; Doth, J.
Studies on the aminopeptidase activity of rat cathepsin H
Eur. J. Biochem.
210
759-764
1992
Rattus norvegicus
brenda
Raghav, N.; Kamboj, R.C.; Parnami, S.; Singh, H.
Physico-chemical properties of brain cathepsin H
Indian J. Biochem. Biophys.
32
279-285
1995
Bos taurus
brenda
Aranishi, F.; Hara, K.; Ishinara, T.
Purification and characterization of cathepsin H from hepatopancreas of carp Cyprinus carpio
Comp. Biochem. Physiol. B
102B
499-505
1992
Cyprinus carpio
brenda
Yamamoto, K.; Kamata, O.; Kato, Y.
Separation and properties of three forms of cathepsin H-like cysteine proteinase from rat spleen
J. Biochem.
95
477-484
1984
Rattus norvegicus
brenda
Kominami, E.; Katunuma, N.
Immunological studies on cathepsins B and H from rat liver
J. Biochem.
91
67-71
1982
Rattus norvegicus
brenda
Kamphuis, I.G.; Drenth, J.; Baker, E.N.
Thiol proteases: comparative studies on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
J. Mol. Biol.
182
317-329
1985
Homo sapiens
brenda
Vasiljeva, O.; Dolinar, M.; Turk, V.; Turk, B.
Recombinant human cathepsin H lacking the mini chain is an endopeptidase
Biochemistry
42
13522-13528
2003
Homo sapiens, Sus scrofa
brenda
Dodt, J.; Reichwein, J.
Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase
Biol. Chem.
384
1327-1332
2003
Homo sapiens
brenda
Matsuishi, M.; Saito, G.; Okitani, A.; Kato, H.
Purification and some properties of cathepsin H from rabbit skeletal muscle
Int. J. Biochem. Cell Biol.
35
474-485
2003
Oryctolagus cuniculus
brenda
Jenko, S.; Dolenc, I.; Guncar, G.; Dobersek, A.; Podobnik, M.; Turk, D.
Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
J. Mol. Biol.
326
875-885
2003
Sus scrofa
brenda
Brguljan, P.M.; Turk, V.; Nina, C.; Brzin, J.; Krizaj, I.; Popovic, T.
Human brain cathepsin H as a neuropeptide and bradykinin metabolizing enzyme
Peptides
24
1977-1984
2003
Homo sapiens
brenda
Froehlich, E.; Moehrle, M.; Klessen, C.
Cathepsins in basal cell carcinomas: activity, immunoreactivity and mRNA staining of cathepsins B, D, H and L. [Erratum to document cited in CA141:021292]
Arch. Dermatol. Res.
296
94
2004
Homo sapiens
-
brenda
Bratkovic, T.; Lunder, M.; Popovic, T.; Kreft, S.; Turk, B.; Strukelj, B.; Urleb, U.
Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K
Biochem. Biophys. Res. Commun.
332
897-903
2005
Homo sapiens
brenda
Horn, M.; Doleckova-Maresova, L.; Rulisek, L.; Masa, M.; Vasiljeva, O.; Turk, B.; Gan-Erdene, T.; Baudys, M.; Mares, M.
Activation processing of cathepsin H impairs recognition by its propeptide
Biol. Chem.
386
941-947
2005
Homo sapiens (P09668)
brenda
Chornaya, V.; Lyannaya, O.
Some physicochemical properties of cathepsin H from human meningioma
Exp. Oncol.
26
278-281
2004
Homo sapiens
brenda
Ueno, T.; Linder, S.; Na, C.L.; Rice, W.R.; Johansson, J.; Weaver, T.E.
Processing of pulmonary surfactant protein B by napsin and cathepsin H
J. Biol. Chem.
279
16178-16184
2004
Homo sapiens
brenda
Serveau-Avesque, C.; Ferrer-Di Martino, M.; Herve-Grepinet, V.; Hazouard, E.; Gauthier, F.; Diot, E.; Lalmanach, G.
Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids
Biol. Cell.
98
15-22
2006
Homo sapiens
brenda
Torikai, H.; Akatsuka, Y.; Miyazaki, M.; Tsujimura, A.; Yatabe, Y.; Kawase, T.; Nakao, Y.; Tsujimura, K.; Motoyoshi, K.; Morishima, Y.; Kodera, Y.; Kuzushima, K.; Takahashi, T.
The human cathepsin H gene encodes two novel minor histocompatibility antigen epitopes restricted by HLA-A*3101 and -A*3303
Br. J. Haematol.
134
406-416
2006
Homo sapiens, Homo sapiens (P09668)
brenda
Woischnik, M.; Bauer, A.; Aboutaam, R.; Pamir, A.; Stanzel, F.; de Blic, J.; Griese, M.
Cathepsin H and napsin A are active in the alveoli and increased in alveolar proteinosis
Eur. Respir. J.
31
1197-1204
2008
Homo sapiens, Homo sapiens (P09668)
brenda
Lue, J.; Qian, J.; Keppler, D.; Cardoso, W.V.
Cathepsin H is an Fgf10 target involved in Bmp4 degradation during lung branching morphogenesis
J. Biol. Chem.
282
22176-22184
2007
Mus musculus
brenda
Nagaraj, N.S.; Santhanam, K.
Effect of frozen temperature and storage time on calpains, cathepsins (B, B + L, H and D) and their endogenous inhibitors in goat muscles
J. Food Biochem.
30
155-173
2006
Capra aegagrus
-
brenda
Yeh, H.Y.; Klesius, P.H.
Channel catfish, Ictalurus punctatus, cysteine proteinases: cloning, characterisation and expression of cathepsin H and L
Fish Shellfish Immunol.
26
332-338
2009
Ictalurus punctatus (B5LVX3), Ictalurus punctatus
brenda
Sethadavit, M.; Meemon, K.; Jardim, A.; Spithill, T.W.; Sobhon, P.
Identification, expression and immunolocalization of cathepsin B3, a stage-specific antigen expressed by juvenile Fasciola gigantica
Acta Trop.
112
164-173
2009
Fasciola gigantica, Fasciola gigantica (Q86MW6)
brenda
Li, J.; Petrassi, H.; Tumanut, C.; Masick, B.; Trussell, C.; Harris, J.
Substrate optimization for monitoring cathepsin C activity in live cells
Bioorg. Med. Chem.
17
1064-1070
2009
Homo sapiens
brenda
D'Angelo, M.E.; Bird, P.I.; Peters, C.; Reinheckel, T.; Trapani, J.A.; Sutton, V.R.
Cathepsin H is an additional convertase of pro-granzyme B
J. Biol. Chem.
285
20514-20519
2010
Mus musculus
brenda
Buehling, F.; Kouadio, M.; Chwieralski, C.E.; Kern, U.; Hohlfeld, J.M.; Klemm, N.; Friedrichs, N.; Roth, W.; Deussing, J.M.; Peters, C.; Reinheckel, T.
Gene targeting of the cysteine peptidase cathepsin H impairs lung surfactant in mice
PLoS ONE
6
e26247
2011
Mus musculus
brenda
Raghav, N.; Garg, S.
N-formylpyrazolines and N-benzoylpyrazolines as novel inhibitors of mammalian cathepsin B and cathepsin H
Bioorg. Chem.
57
43-50
2014
Capra hircus
brenda
Singh, M.; Raghav, N.
2,3-Dihydroquinazolin-4(1H)-one derivatives as potential non-peptidyl inhibitors of cathepsins B and H
Bioorg. Chem.
59
12-22
2015
Capra hircus
brenda
Raghav, N.; Singh, M.
Acyl hydrazides and triazoles as novel inhibitors of mammalian cathepsin B and cathepsin H
Eur. J. Med. Chem.
77
231-242
2014
Capra hircus
brenda
Jevnikar, Z.; Rojnik, M.; Jamnik, P.; Doljak, B.; Fonovic, U.P.; Kos, J.
Cathepsin H mediates the processing of talin and regulates migration of prostate cancer cells
J. Biol. Chem.
288
2201-2209
2013
Homo sapiens
brenda
Lu, W.D.; Funkelstein, L.; Toneff, T.; Reinheckel, T.; Peters, C.; Hook, V.
Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide neurotransmitters
J. Neurochem.
122
512-522
2012
Bos taurus, Mus musculus
brenda
Raghav, N.; Singh, M.
SAR studies of differently functionalized chalcones based hydrazones and their cyclized derivatives as inhibitors of mammalian cathepsin B and cathepsin H
Bioorg. Med. Chem.
22
4233-4245
2014
Capra hircus
brenda
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