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Information on EC 3.4.22.16 - cathepsin H and Organism(s) Rattus norvegicus and UniProt Accession P00786
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3.4.22.16 cathepsin HSpecify your search results
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
cathepsin h, aleurain, catb3, cat h, procathepsin h, cathepsin b3, cathepsin h-like cysteine proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aleurain
-
-
-
-
cathepsin B3
-
-
-
-
cathepsin Ba
-
-
-
-
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
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
number of possible subsites: three
-
CAS REGISTRY NUMBER
COMMENTARY
60748-73-4
-
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
alpha-N-benzoyl-DL-arginine-beta-naphthylamide + H2O
alpha-N-benzoyl-DL-arginine + beta-naphthylamine
-
-
-
ir
benzoyl-Arg-4-methylcoumaryl-7-amide + H2O
benzoyl-Arg + 7-amino-4-methylcoumarin
-
-
-
ir
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
citrulline-4-methylcoumaryl-7-amide + H2O
citrulline + 7-amino-4-methylcoumarin
-
-
-
ir
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
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
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
benzoyl-DL-Arg-2-naphthylamide + H2O
benzoyl-DL-Arg + 2-naphthylamine
-
-
-
ir
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
?
-
-
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
-
-
?
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
Proteins + H2O
?
-
involved in cell growth, protein degradation, synthesis of peptide hormones and tumor metastasis
-
-
?
Proteins + H2O
?
-
rather broad specificity of aminopeptidase activity
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzyloxycarbonyl-Gly-Leu-NH
-
inhibits processing of proenzyme to active form
Benzyloxycarbonyl-Leu-NH2
-
inhibits formation of active enzyme from procathepsin H
ethyl(2S,3S)-3-(S)-3-methyl-1-(3-methylbutylcarbamoyl)butylcarbamoyl oxirane-2-carboxylate
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
-
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
metalloendopeptidases involved in processing of procathepsin to active enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH and temperature dependence of kcat/Km
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH and temperature dependence of kcat/Km
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
6.5
-
substrates Arg-4-methylcoumaryl-7-amide and citrulline-4-methylcoumaryl-7-amide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
543 ng /mg protein, distribution in tissues and peripheral blood cells
-
683 ng /mg protein, distribution in tissues and peripheral blood cells
additional information
immunofluorescent and immunohistochemic analysis
-
1429 ng /mg protein, distribution in tissues and peripheral blood cells
-
556 ng /mg protein, distribution in tissues and peripheral blood cells
-
158-298 ng /1000000 cells, distribution in tissues and peripheral blood cells
-
480 ng /mg protein, distribution in tissues and peripheral blood cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
biosynthesis in endoplasmic reticulum, proteolytic cleavage of proenzyme during translocation to lysosomes
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
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
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). CATH_RAT
333
0
37104
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
additional information
-
comparison to other proteinases of the papain superfamily: high sequence homologies
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
side-chain modification
side-chain modification
-
structural studies of carbohydrate moieties: 1 Asn-115-linked high-mannose type oligosaccharide per molecule, structure reported
side-chain modification
-
glycosylated residues located on rather loose surface loop
side-chain modification
-
high-mannose oligosaccharide, one N-glycosylation site per molecule
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C, 50 mM Na-acetate buffer, pH 5.0, 0.2 M NaCl, 0. 5 mM HgCl2, 1 mM EDTA
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CTSH, real-time PCR enzyme expression analysis in skin and keratinocyte culture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barrett, A.J.; Kirschke, H.
Cathepsin B, Cathepsin H, and cathepsin L
Methods Enzymol.
80
535-561
1981
Homo sapiens, Rattus norvegicus
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
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
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
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
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
Brmme, 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
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
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
Bergmeyer, H.U.ed
Cathepsin B, cathepsin H, and cathepsin L
Methods Enzym. Anal. (3rd. ed. )
5
195-210
1984
Homo sapiens, Rattus norvegicus
-
Schwartz, W.N.; Barrett, A.J.
Human cathepsin H
Biochem. J.
191
487-497
1980
Homo sapiens, Rattus norvegicus
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
Rothe, M.; Doth, J.
Studies on the aminopeptidase activity of rat cathepsin H
Eur. J. Biochem.
210
759-764
1992
Rattus norvegicus
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
Kominami, E.; Katunuma, N.
Immunological studies on cathepsins B and H from rat liver
J. Biochem.
91
67-71
1982
Rattus norvegicus
Naeem, A.S.; Tommasi, C.; Cole, C.; Brown, S.J.; Zhu, Y.; Way, B.; Willis Owen, S.A.; Moffatt, M.; Cookson, W.O.; Harper, J.I.; Di, W.L.; Brown, S.J.; Reinheckel, T.; O'Shaughnessy, R.F.
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
J. Allergy Clin. Immunol.
139
1228-1241
2017
Homo sapiens (P09668), Homo sapiens, Mus musculus (P49935), Mus musculus, Mus musculus C57BL/6J (P49935), Rattus norvegicus (P00786)
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