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Information on EC 3.4.22.B65 - cathepsin P
for references in articles please use BRENDA:EC3.4.22.B65preliminary BRENDA-supplied EC number
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EC Tree
3.4.22.B65 cathepsin PSpecify your search results
Word Map
- 3.4.22.B65
- cathepsins
- papain
-
peptidyl
- rodent
- lysosomal
- proenzyme
- tubule
- phe
-
perimembranous
-
kupffer
-
cytred
-
giant
-
papain-like
- peptidases
- propeptide
-
pecs
-
rcho-1
- hepatocytes
- na2so4
-
immunolocalization
-
trophoblast
- choriocarcinoma
- preproprotein
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with restricted preference for substrates containing hydrophobic amino acids. Efficiently cleaves -Glu-Ile-Phe-/-Val-Phe-Lys-Gln-. Involved in the processing of endoplasmic proteins
Synonyms
cathepsin p, 
more
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with restricted preference for substrates containing hydrophobic amino acids. Efficiently cleaves -Glu-Ile-Phe-/-Val-Phe-Lys-Gln-. Involved in the processing of endoplasmic proteins
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
94716-08-02
-
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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
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2
calreticulin + H2O
?
endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins
protein is processed from the C-terminus, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with calreticulin in rat choriocarcinoma cell
-
?
Gp96 protein + H2O
?
endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins
protein is sequentially processed by cathepsin P at 2 sites towards the C-terminus of the protein, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with gp96 in rat choriocarcinoma cell
-
?
o-aminobenzoic acid-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-ALR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-EIF + VFKQ-N-(2,4-dinitrophenyl)ethylenediamine
ideal substrate constructed after analysis of substrate preferences. In contrast to most substrates, hydrolysis is not stimulated by addition of salts
-
-
?
o-aminobenzoic acid-ELRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-ELR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-FLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-FLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-HLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-HLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-ILRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-ILR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KARSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KAR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KFRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KFR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KIRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KIR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLASSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLA + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLFSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLF + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLISSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLI + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine + o-aminobenzoic acid-KLIS + SKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
preferential hydrolysis at the Ser-Ser bond
-
?
o-aminobenzoic acid-KLKSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLK + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLLSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLL + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLMSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLM + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLQSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLQ + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRESKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + ESKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRfSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + fSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRGSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + GSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRHSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + HSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRISKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + ISKQ-N-(2,4-dinitrophenyl)ethylenediamine + o-aminobenzoic acid-KLRIS + KQ-N-(2,4-dinitrophenyl)ethylenediamine
-
30% cleavage at Arg-Ile bond, 70% cleavage at Ser-Lys bond
-
?
o-aminobenzoic acid-KLRLSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + LSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRNSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + NSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRQSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + QSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRRSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + RSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLR + VSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLTSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLT + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KLYSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KLY + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KMRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KMR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KNLRSSKQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
?
o-aminobenzoic acid-KQRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KQR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KRRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KRR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KTRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KTR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KVRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KVR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-KYRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-KYR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-LLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-LLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-NLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-NLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-RLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-RLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
o-aminobenzoic acid-VLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoic acid-VLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
?
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2
-
-
-
?
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2
-
-
-
-
?
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-Dap(Dnp)-Ala-Arg-NH2
-
-
-
-
?
additional information
?
-
no substrates: Z-Phe-Arg-NHMec, Z-Arg-Arg-NHMec, Arg-NHMec, Bz-Phe-Val-Arg-NHMec, succinyl-Ala-Ala-Phe-NHMec, Z-Val-Ala-Asp-NHMec, bradykinin, somatostatin, Fmoc-Tyr-Ala-OH, Z-Gly-Gly-OH, Z-Leu-Tyr-OH, Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2, Mca-Pro-Leu-Ala-Gln-Ala-Val-Dpa-Arg-Ser-Ser-Ser-Arg-NH2 or Dnp-Pro-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(Nma)NH2
-
-
?
additional information
?
-
-
no substrates: Z-Phe-Arg-NHMec, Z-Arg-Arg-NHMec, Arg-NHMec, Bz-Phe-Val-Arg-NHMec, succinyl-Ala-Ala-Phe-NHMec, Z-Val-Ala-Asp-NHMec, bradykinin, somatostatin, Fmoc-Tyr-Ala-OH, Z-Gly-Gly-OH, Z-Leu-Tyr-OH, Dnp-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2, Mca-Pro-Leu-Ala-Gln-Ala-Val-Dpa-Arg-Ser-Ser-Ser-Arg-NH2 or Dnp-Pro-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(Nma)NH2
-
-
?
additional information
?
-
peptides with hydrophobic residues such as Phe, Met, and Leu in the P1 position are preferred substrates of cathepsin P. Substrates with negatively charged amino acids such as Glu, polar uncharged amino acids such as Asn, Gln, Ser, and Thr, and positively charged amino acids such as Arg, Lys, and His in this position are poorly hydrolyzed by cathepsin P due to either reduced kcat or increased Km, or both
-
-
?
additional information
?
-
-
peptides with hydrophobic residues such as Phe, Met, and Leu in the P1 position are preferred substrates of cathepsin P. Substrates with negatively charged amino acids such as Glu, polar uncharged amino acids such as Asn, Gln, Ser, and Thr, and positively charged amino acids such as Arg, Lys, and His in this position are poorly hydrolyzed by cathepsin P due to either reduced kcat or increased Km, or both
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CBZ-Trp-Trp-4-cyclohexanone-Trp-Phe-OMe
reversoble competitive inhibition. 10fold less inhibitory on mouse cathepsin L, 20fold less inhibitory on human cathpsin L, 50fold less inhibotry on human cathepsin B
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na2SO4
in presence of 2 M Na2SO4, activity of cathepsin P is almost 100fold higher than in the absence of the salt. Variation of the Na2SO4 concentration from 0 to 2.5 M does not affect the cathepsin P secondary structure, the salt effect is more likely restricted to effects on more subtle interactions between the substrate and surface amino acids of the enzyme
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Choriocarcinoma
Expression of cathepsin P mRNA, protein and activity in the rat choriocarcinoma cell line, Rcho-1, during giant cell transformation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
o-aminobenzoic acid-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0051
o-aminobenzoic acid-ELRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0094
o-aminobenzoic acid-FLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0048
o-aminobenzoic acid-HLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0085
o-aminobenzoic acid-ILRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0184
o-aminobenzoic acid-KARSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.004
o-aminobenzoic acid-KFRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0069
o-aminobenzoic acid-KIRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0034
o-aminobenzoic acid-KLASSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0015
o-aminobenzoic acid-KLFSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0015
o-aminobenzoic acid-KLLSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0014
o-aminobenzoic acid-KLMSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0053
o-aminobenzoic acid-KLRESKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0079
o-aminobenzoic acid-KLRFSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0058
o-aminobenzoic acid-KLRGSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0153
o-aminobenzoic acid-KLRHSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0046
o-aminobenzoic acid-KLRLSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0202
o-aminobenzoic acid-KLRNSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0084
o-aminobenzoic acid-KLRQSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0107
o-aminobenzoic acid-KLRRSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0014
o-aminobenzoic acid-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.002
o-aminobenzoic acid-KLTSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0038
o-aminobenzoic acid-KLYSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0084
o-aminobenzoic acid-KMRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0048
o-aminobenzoic acid-KNLRSSKQ-(N-(2,4-dinitrophenyl)ethylenediamine)
37°C, pH 6.5
0.0201
o-aminobenzoic acid-KQRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.018
o-aminobenzoic acid-KRRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0243
o-aminobenzoic acid-KTRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0055
o-aminobenzoic acid-KVRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.00044
o-aminobenzoic acid-KYRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.018
o-aminobenzoic acid-LLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0086
o-aminobenzoic acid-NLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-RLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.004
o-aminobenzoic acid-VLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.15
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 1 M Na2SO4
0.2
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.5
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 2.5 M Na2SO4
0.0029
o-aminobenzoic acid-KLQSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-KLQSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.004
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 2.5 M Na2SO4
0.0048
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0048
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 1 M Na2SO4
0.01
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
o-aminobenzoic acid-ALRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.021
o-aminobenzoic acid-ELRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.024
o-aminobenzoic acid-FLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-HLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.016
o-aminobenzoic acid-ILRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.008
o-aminobenzoic acid-KARSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.004
o-aminobenzoic acid-KFRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.05
o-aminobenzoic acid-KIRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.009
o-aminobenzoic acid-KLASSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.016
o-aminobenzoic acid-KLFSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.02
o-aminobenzoic acid-KLKSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.012
o-aminobenzoic acid-KLLSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-KLMSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.006
o-aminobenzoic acid-KLQSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.014
o-aminobenzoic acid-KLRESKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.01
o-aminobenzoic acid-KLRFSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.007
o-aminobenzoic acid-KLRGSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.009
o-aminobenzoic acid-KLRHSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.018
o-aminobenzoic acid-KLRLSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.044
o-aminobenzoic acid-KLRNSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.029
o-aminobenzoic acid-KLRQSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.018
o-aminobenzoic acid-KLRRSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.009
o-aminobenzoic acid-KLRVSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.007
o-aminobenzoic acid-KLTSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.015
o-aminobenzoic acid-KLYSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.02
o-aminobenzoic acid-KMRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.016
o-aminobenzoic acid-KNLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.006
o-aminobenzoic acid-KQRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.001
o-aminobenzoic acid-KRRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-KTRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.017
o-aminobenzoic acid-KVRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.005
o-aminobenzoic acid-KYRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.029
o-aminobenzoic acid-LLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.012
o-aminobenzoic acid-NLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.023
o-aminobenzoic acid-RLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.013
o-aminobenzoic acid-VLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.004
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 2.5 M Na2SO4
0.005
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 1 M Na2SO4
0.006
o-aminobenzoic acid-EIFVFKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.0014
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 2.5 M Na2SO4
0.0016
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5, presence of 1 M Na2SO4
0.004
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
0.016
o-aminobenzoic acid-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
37°C, pH 6.5
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
substrate 7-(methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-Dnp(Dpa)-Ala-Arg-NH2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Cathepsin P expression is induced during differentiation of Rcho-1 cells into a trophoblast giant cell phenotype
brenda
additional information
additional information
no expression in heart, kidney, liver, lung or spleen
brenda
additional information
-
no expression in heart, kidney, liver, lung or spleen
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cathepsin P co-localizes with cathepsin B and may function in an endosomal-lysosomal compartment
brenda
-
cathepsin P co-localizes with cathepsin B and may function in an endosomal-lysosomal compartment
brenda
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
27000
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
31000
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
35000
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
38000
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 31000, x * 35000, x * 38000, SDS-PAGE of recombinant zymogen, x * 24000, x * 27000, SDS-PAGE of mature protein
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
treatment of recombinant protein with PNGase F results in a single protein band of 29000 Da in SDS-PAGE for the zymogen and of 22000 Da for the autoactivated protein
proteolytic modification
the inactive zymogen can be activated by proteinase K, chymotrypsin or pancreatic elastase at neutral pH. Cathepsin P can be autoactivated at neutral pH, but not at acidic pH
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethyl sulfoxide
increased concentration of dimethyl sulfoxide reduces Vmax but does not affect Km for substrate MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)-Ala-Arg-NH2
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Puzer, L.; Barros, N.M.; Oliveira, V.; Juliano, M.A.; Lu, G.; Hassanein, M.; Juliano, L.; Mason, R.W.; Carmona, A.K.
Defining the substrate specificity of mouse cathepsin P
Arch. Biochem. Biophys.
435
190-196
2005
Mus musculus (Q9R014), Mus musculus
brenda
Hassanein, M.; Xue, F.; Seto, C.T.; Mason, R.W.
Development of a specific inhibitor for the placental protease, cathepsin P
Arch. Biochem. Biophys.
464
288-294
2007
Mus musculus (Q9R014), Mus musculus
brenda
Sol-Church, K.; Frenck, J.; Mason, R.W.
Cathepsin Q, a novel lysosomal cysteine protease highly expressed in placenta
Biochem. Biophys. Res. Commun.
267
791-795
2000
Mus musculus (Q9R014), Mus musculus
brenda
Mason, R.W.; Bergman, C.A.; Lu, G.; Frenck Holbrook, J.; Sol-Church, K.
Expression and characterization of cathepsin P
Biochem. J.
378
657-663
2004
Mus musculus (Q9R014), Mus musculus
brenda
Hassanein, M.; Bojja, A.S.; Glazewski, L.; Lu, G.; Mason, R.W.
Protein processing by the placental protease, cathepsin P
Mol. Hum. Reprod.
15
433-442
2009
Mus musculus (Q9R014)
brenda
Hassanein, M.; Korant, B.D.; Lu, G.; Mason, R.W.
Expression of cathepsin P mRNA, protein and activity in the rat choriocarcinoma cell line, Rcho-1, during giant cell transformation
Placenta
28
912-919
2007
Rattus norvegicus
brenda
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