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Information on EC 3.4.22.35 - Histolysain
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3.4.22.35 HistolysainSpecify your search results
Word Map
- 3.4.22.35
- cathepsins
- lysosomal
- cystatins
- papain
- calpains
- trypanosoma
- plasmodium
- falciparum
-
papain-like
- cruzi
- resorption
- polyproteins
-
antimalarial
- allergen
- caspase-1
- pyogenes
- chagas
- mite
- propeptide
-
calcium-dependent
- osteoclast
- leupeptin
- trophozoite
- m-calpain
-
asparaginyl
- proenzyme
- cruzipain
-
warhead
- nsp2
-
calpain-mediated
-
hexakisphosphate
- pteronyssinus
-
pyrogenic
-
procathepsin
- cpp32
- streptococcal
-
metacercariae
- 3clpro
-
autoprocessing
- bromelain
- kininogens
- calpastatin
- pineapple
-
gingipains
-
l-like
- alln
-
osteoclast-mediated
- legumain
-
collagenolytic
- dermatophagoides
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec
Synonyms
cysteine protease, ehcp112, ehcp5, ehcp2, ehcp1, cysteine proteinase 1, cysteine proteinase 5, cysteine protease 2, histolysain, ppehcp-b9, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Amebapain
-
-
-
-
CP1
CP2
CP5
CP6
cysteine protease 1
cysteine protease 2
cysteine protease 5
cysteine protease 6
cysteine proteinase 1
cysteine proteinase 5
EhCP1
Entamoeba histolytica 112kDa adhesin
-
together with a protein with an adherence domain EhADH112
Entamoeba histolytica cysteine protease
Entamoeba histolytica cysteine proteinase
Entamoeba histolytica neutral thiol proteinase
-
-
-
-
Histolysin
PCP5
Proteinase, Entamoeba histolytica cysteine
-
-
-
-
additional information
Entamoeba histolytica cysteine protease
-
-
-
-
Entamoeba histolytica cysteine proteinase
-
-
-
-
Histolysin
-
-
-
-
additional information
enzyme is a member of the cysteine proteinase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec
-
-
-
-
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec
from the protozoan, Entamoeba histolytica. In peptidase family C1 (papain family)
-
-
-
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec
cleavage mechanism on mucin substrate, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
92228-52-9
-
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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
Arg-Gly-Phe-Phe + H2O
Arg-Gly + Phe-Phe
-
substrate of amoebapain
-
-
?
benzyloxycarbonyl-Ala-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Arg-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
benzyloxycarbonyl-L-arginyl-L-arginine 4-nitroanilide + H2O
benzyloxycarbonyl-L-arginyl-L-arginine + 4-nitroaniline
-
-
?
Benzyloxycarbonyl-Phe-L-citrullin 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Collagen type I + H2O
?
-
digestion with an initial attack at the alpha2-chain
-
-
?
complement factor C3 + H2O
peptides
-
product determination
?
complement factor C9 + H2O
peptides
-
product determination
?
immunoglobulin G + H2O
peptides derived from immunoglobulin G
-
product determination
?
mucin MUC2 polymer + H2O
?
-
enzyme is involved, together with other Entamoeba histolytica cysteine proteinases, in the degradation of mucin in the mucous layer of the colon epithelium, altering the protective function to facilitate parasite attachment
-
?
N-benzyloxycarbonyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginine + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
N-benzyloxycarbonyl-L-phenylalanyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-phenylalanyl-L-arginine + 7-amino-4-methylcoumarin
-
7% of the activity with N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin
-
?
Z-Arg-Arg-4-methoxy-2-nitroanilide + H2O
Z-Arg-Arg + 4-methoxy-2-nitroaniline
-
-
-
-
?
Z-Arg-Arg-4-nitroanilide + H2O
Z-Arg-Arg + 4-nitroaniline
-
-
-
-
?
Z-Arg-Arg-7-amido-4-trifluoromethylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
-
-
-
?
chemokine CCL13 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
chemokine CCL2 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
chemokine CXCL8 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
immunoglobulin G + H2O
?
-
heavy chain, protein from human
-
-
?
MUC2 mucin + H2O
?
-
disruption of the protective mucin layer of targeted host cells, entry mechanism of the pathogen, overview
-
-
?
MUC2 mucin + H2O
?
-
the enzyme targets two site at the C-terminal cysteine-rich domain, which is less glycosylated and exposes its peptide chain, overview
-
-
?
N-benzyloxycarbonyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginine + 7-amino-4-methylcoumarin
-
17% of the activity with N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin
-
?
N-benzyloxycarbonyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginine + 7-amino-4-methylcoumarin
-
17% of the activity with N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin
-
?
N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-L-arginyl-L-arginyl-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
protein + H2O
peptides
enzyme is involved in pathogenic destruction of host tissue by degradation of extracellular matrix proteins
-
?
Z-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Ala-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Insulin B-chain + H2O
additional information
-
-
-
the Gly-Phe bond in the insulin B-chain is the major hydrolysis site
?
additional information
?
-
-
with unblocked tetrapeptides as substrates, peptidyl dipeptidase activity of the amoeba enzyme requires an arginine at the P2 position. Lysine cannot substitute for arginine
-
-
?
additional information
?
-
-
the enzyme causes a loss of adhesion of mammalian cells in culture
-
-
?
additional information
?
-
-
inactivates aldolase and glyceraldehyde 3-phosphate dehydrogenase from rabbit muscle and glucose 6-phosphate dehydrogenase from yeast, limited proteolysis yielding major cleavage products
-
-
?
additional information
?
-
-
splits blocked and unblocked peptide analogs with 2-naphthylamide moieties, cleavability is enhanced by the presence of basic residues, such as arginine or lysine, near the acyl end of the substrate
-
-
?
additional information
?
-
-
enzyme permits adhesion of trophozoites to cells via fibronectin binding, which can be inhibited by Zn2+
-
?
additional information
?
-
-
no activity with benzyloxycarbonyl-Phe-Arg-4-nitroanilide
-
?
additional information
?
-
-
no activity with N-benzyloxycarbonyl-Val-Lys-Met-7-amido-4-methylcoumarin and succinyl-LLVY-7-amido-4-methylcoumarin
-
?
additional information
?
-
no activity with peptide substrates containing phenylalanine at P2 position instead of arginine
-
?
additional information
?
-
-
the enzyme is covalently connected to an adhesin by electrostatic forces which are not broken during phagocytosis
-
?
additional information
?
-
-
appears to be important both for digestion and as a cytotoxic factor
-
-
?
additional information
?
-
-
the enzyme can degrade colon cell mucin and destroy epithelial cell layers
-
-
?
additional information
?
-
-
the enzyme degrades a number of proteins, including those of the extracellular matrix
-
-
?
additional information
?
-
-
the enzyme is involved in host tissue invasion by trophozoites and destroys cell monolayers
-
-
?
additional information
?
-
-
the enzyme shows cytopathic effects and destroys cell monolayers
-
-
?
additional information
?
-
-
the enzyme degrades a number of proteins, including those of the extracellular matrix, but also acts on small molecule substrates showing endopeptidase and exopeptidase-like activities, amoebapain hydrolyzes unblocked tetrapeptides with basic residues at P2
-
-
?
additional information
?
-
-
cysteine proteinases play a central role in tissue invasion and disruption of host defenses by digesting components of the extracellular matrix, immunoglobulins, complement, and cytokines
-
-
?
additional information
?
-
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
-
no activity with Z-Phe-Arg-4-amido-7-methylcoumarin
-
-
?
additional information
?
-
-
the cysteine proteinase EhCP112 and the adhesin EhADH112 assemble to form the EhCPADH complex involved in Entamoeba histolytica virulence
-
-
?
additional information
?
-
-
cysteine proteinases play a central role in tissue invasion and disruption of host defenses by digesting components of the extracellular matrix, immunoglobulins, complement, and cytokines
-
-
?
additional information
?
-
-
no activity with Z-Phe-Arg-4-amido-7-methylcoumarin
-
-
?
additional information
?
-
-
no activity with N-benzyloxycarbonyl-Val-Lys-Met-7-amido-4-methylcoumarin and succinyl-LLVY-7-amido-4-methylcoumarin
-
?
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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
chemokine CCL13 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
chemokine CCL2 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
chemokine CXCL8 + H2O
?
-
Entamoeba histolytica is a human pathogen causing amoebic colitis, the enzyme is involved in the inflammation process modulating human host leucocyte migration by proteolytic cleavage of chemokines CCL2, CCL13, and CXCL8, a mechanism to circumvent host immune response
-
-
?
MUC2 mucin + H2O
?
-
disruption of the protective mucin layer of targeted host cells, entry mechanism of the pathogen, overview
-
-
?
mucin MUC2 polymer + H2O
?
-
enzyme is involved, together with other Entamoeba histolytica cysteine proteinases, in the degradation of mucin in the mucous layer of the colon epithelium, altering the protective function to facilitate parasite attachment
-
?
protein + H2O
peptides
enzyme is involved in pathogenic destruction of host tissue by degradation of extracellular matrix proteins
-
?
additional information
?
-
-
appears to be important both for digestion and as a cytotoxic factor
-
-
?
additional information
?
-
-
the enzyme can degrade colon cell mucin and destroy epithelial cell layers
-
-
?
additional information
?
-
-
the enzyme degrades a number of proteins, including those of the extracellular matrix
-
-
?
additional information
?
-
-
the enzyme is involved in host tissue invasion by trophozoites and destroys cell monolayers
-
-
?
additional information
?
-
-
the enzyme shows cytopathic effects and destroys cell monolayers
-
-
?
additional information
?
-
-
cysteine proteinases play a central role in tissue invasion and disruption of host defenses by digesting components of the extracellular matrix, immunoglobulins, complement, and cytokines
-
-
?
additional information
?
-
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
essential for pathogenicity of Entamoeba histolytica
-
-
?
additional information
?
-
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
secreted cysteine proteases play an indispensable role in amoebic invasion and tissue destruction due to their hydrolytic and degradative activities towards extracellular matrix proteins
-
-
?
additional information
?
-
-
the cysteine proteinase EhCP112 and the adhesin EhADH112 assemble to form the EhCPADH complex involved in Entamoeba histolytica virulence
-
-
?
additional information
?
-
-
cysteine proteinases play a central role in tissue invasion and disruption of host defenses by digesting components of the extracellular matrix, immunoglobulins, complement, and cytokines
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-hydroxymercuribenzoate
-
E64 inhibits cell growth and is cytopathic/lethal for E64-sensitive and E64-resistant amoebae
4-[(2S,3S)-carboxyoxiran-2-ylcarbonyl-L-leucylamido]butylguanidine
-
i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane or E64
cysteine protease inhibitor 2
-
inhibits isoform CP5 approximately 20times more efficient than isoform CP2
-
EhICP1
Entamoeba histolytica inhibitor for cysteine protease type 1; Entamoeba histolytica inhibitor for cysteine protease type 1; Entamoeba histolytica inhibitor for cysteine protease type 1, inhibition also by regulation of CP5 processing
-
EhICP2
Entamoeba histolytica inhibitor for cysteine protease type 2; Entamoeba histolytica inhibitor for cysteine protease type 2; Entamoeba histolytica inhibitor for cysteine protease type 2, inhibition also by regulation of CP5 processing
-
L-3-carboxy-2,3-trans-epoxypropionyl-leucyl-amido(4-guanidino)butane
-
i.e. E-64
L-trans-epoxysuccinyl-(ethoxy)-Leu-3-methylbutylamide ethyl ester
-
i.e. E64d, inhibits cell growth and is cytopathic/lethal for E64-sensitive and E64-resistant amoebae
L-trans-epoxysuccinyl-Leu-4-guanidinobutylamide
-
i.e. E64, inhibits cell growth in E64-resistant by about 80% and is cytopathic/lethal for E64-sensitive amoebae
N-methylpiperazine-urea-phenylalanylhomoarginylvinylsulfone-benzene
-
WRR483, inhibitor addition to medium fully prevents invasion of parasite
N-methylpiperazine-urea-phenylalanylhomophenylalanylvinylsulfone-benzene
-
K11777, inhibitor addition to medium partially prevents invasion of parasite
Z-Phe-Ala-diazomethylketone
-
E64 inhibits cell growth and is cytopathic/lethal for E64-sensitive and E64-resistant amoebae
Z-Phe-Phe-diazomethylketone
-
25% inhibition of E64-sensitive and E64-resistant amoba growth
Zn2+
-
77% inhibition of proteolytic activity at 2.5 mM, completely reversible by L-cystein, phenanthroline, and L-histidine, Zn2+ interferes with the fibronectin binding of the amoeba
E64
activity was completely abolished when trophozoites are pretreated with 200 mM of E64, a potent, irreversible and highly selective cysteine protease inhibitor; activity was completely abolished when trophozoites are pretreated with 200 mM of E64, a potent, irreversible and highly selective cysteine protease inhibitor; activity was completely abolished when trophozoites are pretreated with 200 mM of E64, a potent, irreversible and highly selective cysteine protease inhibitor
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
ie.e. E-64, irreversible
additional information
-
no inhibition by pepstatin and phenylmethylsulfonyl fluoride
-
additional information
-
no inhibition by aprotinin, pepstatin, phosphoramidon, and pefabloc SC
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of ehpc1 and ehpc2 is increased in presence of E64 in E64-sensitive and E64-resistant amoebae, overview
-
dithiothreitol
-
2-5 mM activate refolded protein in a Tris, phosphate or citrate buffer containing EDTA, pH 7.0-7.5
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.132
cysteine protease inhibitor 1
-
isoform CP1, pH and temperature not specified in the publication
-
0.59
cysteine protease inhibitor 1
-
isoform CP5, pH and temperature not specified in the publication
-
0.809
cysteine protease inhibitor 1
-
isoform CP2, pH and temperature not specified in the publication
-
0.05
cysteine protease inhibitor 2
-
isoform CP5, pH and temperature not specified in the publication
-
0.166
cysteine protease inhibitor 2
-
isoform CP1, pH and temperature not specified in the publication
-
0.95
cysteine protease inhibitor 2
-
isoform CP2, pH and temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cytopathic activity of wild-type and recombinant amoebae
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
benzyloxycarbonyl-Phe-L-citrullin 4-methylcoumarin 7-amide, azocoll
9.5
-
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide, benzyloxycarbonyl-Arg-Arg 4-methylcoumarin 7-amide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
at optimal pH, the turnover increases with increasing temperature up to 85°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
30316, 30318, 30319, 30321, 30322, 30323, 30324, 30325, 649500, 651493, 653742, 669261, 670707, 683417, 683468
-
-
brenda
control strain and strains overexpressing EhRab7B and EhRab7B-GTP, activity secreted to the medium by the EhRab7B-GTP transformant is 4.3fold higher than the control transformant and has a 38% less total intracellular CP activity than the control transformant
-
-
brenda
gene ehcp2 or acp2 encodes histolysain, gene ehcp1 or acp1 encodes amoebapain
-
-
brenda
low-virulence HMI strain and highly virulent 1659 clone, derived from HMI by hamster liver passages
-
-
brenda
overexpression of EhRab11B protein results in a 15fold increase in both, intracellular and secreted cysteine protease activity, suggesting that the three major cysteine proteases are trafficked via an EhRab11B-associated secretory pathway
-
-
brenda
overexpression of EhRab11B protein results in a 15fold increase in both, intracellular and secreted cysteine protease activity, suggesting that the three major cysteine proteases are trafficked via an EhRab11B-associated secretory pathway
UniProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
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additional information
-
the enzyme is translocated to the amoebic surface upon the interaction of trophozoites with red blood cells, the enzyme participates thus in erythrophagocytosis
brenda
additional information
-
the enzyme is expressed and active in different life cycle stages
brenda
additional information
-
the enzyme is translocated to the amoebic surface upon the interaction of trophozoites with red blood cells, the enzyme participates thus in erythrophagocytosis
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted and localized on the cell surface
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additional information
-
bound to matrix-like structures both on the cell surface and within subcellular vesicles. The enzyme recycles between plasma membrane and pinocytic vesicles
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
cysteine proteinase 5 is a major virulent factor that binds integrin on colonic cells and stimulates nuclear factor kappaB-mediated pro-inflammatory responses. Cysteine proteinase 5 is the critical proteinase involved in activating nuclear factor kappaB, phosphorylating Akt and inducing the ubiquitination of nuclear factor-kappaB essential modulator
physiological function
-
Entamoeba histolytica-secreted cysteine proteases induce interleukin-8 production in human mast cells via a protease-activated receptor 2-independent mechanism which contributes to interleukin-8-mediated tissue inflammatory responses during the early phase of human amoebiasis
physiological function
-
the enzyme is highly involved in the virulence of Entamoeba histolytica
physiological function
-
cysteine proteinase 5 is a major virulent factor that binds integrin on colonic cells and stimulates nuclear factor kappaB-mediated pro-inflammatory responses. Cysteine proteinase 5 is the critical proteinase involved in activating nuclear factor kappaB, phosphorylating Akt and inducing the ubiquitination of nuclear factor-kappaB essential modulator
-
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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). CPP2_ENTHI
315
0
34688
Swiss-Prot
Secretory Pathway (Reliability: 3)
Q27643_ENTHI
311
0
33745
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1Y0Y5A0_ACEPA
273
0
29527
TrEMBL
-
Q27641_ENTDI
305
0
32985
TrEMBL
Mitochondrion (Reliability: 5)
Q95030_ENTHI
318
0
34759
TrEMBL
Secretory Pathway (Reliability: 2)
Q27645_ENTHI
320
0
35347
TrEMBL
Secretory Pathway (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
112000
-
x * 112000, enzyme attached to adhesin, reducing and nonreducing SDS-PAGE, x * 75000, about, enzyme without adhesin, SDS-PAGE
27000
35500
-
x * 52000, recombinant and refolded enzyme, SDS-PAGE, x * 35500, recombinant, refolded, and processed enzyme, SDS-PAGE
50000
-
x * 50000, SDS-PAGE, predicted molecular mass for thio-pro-EhCP1 of 50300 Da (36300 Da for the zymogen form of EhCP1, 13000 Da for the thioredoxin peptide, and 9000 Da for the six-His tag)
52000
75000
-
x * 112000, enzyme attached to adhesin, reducing and nonreducing SDS-PAGE, x * 75000, about, enzyme without adhesin, SDS-PAGE
52000
-
x * 52000, recombinant His-tagged full-length EhCP112 zymogen, containing the signal peptide and the pro-peptide, SDS-PAGE
52000
-
x * 52000, recombinant and refolded enzyme, SDS-PAGE, x * 35500, recombinant, refolded, and processed enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 112000, enzyme attached to adhesin, reducing and nonreducing SDS-PAGE, x * 75000, about, enzyme without adhesin, SDS-PAGE
?
-
x * 27000-29000, recombinant and native enzyme, reducing and nonreducing SDS-PAGE
?
-
x * 52000, recombinant His-tagged full-length EhCP112 zymogen, containing the signal peptide and the pro-peptide, SDS-PAGE
?
-
x * 50000, SDS-PAGE, predicted molecular mass for thio-pro-EhCP1 of 50300 Da (36300 Da for the zymogen form of EhCP1, 13000 Da for the thioredoxin peptide, and 9000 Da for the six-His tag)
?
-
x * 52000, recombinant and refolded enzyme, SDS-PAGE, x * 35500, recombinant, refolded, and processed enzyme, SDS-PAGE
?
-
x * 50000, SDS-PAGE, predicted molecular mass for thio-pro-EhCP1 of 50300 Da (36300 Da for the zymogen form of EhCP1, 13000 Da for the thioredoxin peptide, and 9000 Da for the six-His tag)
-
additional information
-
enzyme contains a transmembranal segment, amino acid residues 259-280, and an RGD motif
additional information
-
the enzyme contains an RGD integrin attachment motif, structure-function overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the recombinant enzyme needs to be refolded and processed from the inactive precursor, ppEhCP112, to a 35.5 kDa mature and active enzyme, EhCP112. The thiol specific inhibitor E-64, but not serine or aspartic proteinase inhibitors arrests this activation process
additional information
-
processing of the inactive pro-enzyme to the mature active form by treatment with 10 mM DTT and 0.04% SDS at 37°C and pH 8.8, SDS can be substituted by Triton X-100 and octylglucoside but these are 3fold less efficient
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of EhCP5-deficient amoeba by antisense inhibition showing no activity on mucin from cells LS174T and HT-29F Cl.16E or against CHO cell layers, enzyme-deficient amoeba cannot overcome the mucus barrier to disrupt CHO cell monolayers, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Hg2+, at low concentration causes a delay in heat denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length EhCP112 zymogen, containing the signal peptide and the pro-peptide, from Escherichia coli strain BL21 by nickel affinity chromatography
-
recombinant protein using His-tag under denaturating conditions
recombinant refolded His-tagged enzyme by nickel affinity chromatography
-
to homogeneity
recombinant protein using His-tag under denaturating conditions
-
recombinant protein using His-tag under denaturating conditions
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag and thioredoxin fusin protein in Escherichia coli
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3), formation of inclusion bodies
expression of partial gene ehcp1 in Escherichia coli as GST-fusion protein, expression of functional EhCP2 in insect cells using the baculovirus transfection system
-
expression of the His-tagged inactive pro-enzyme in Escherichia coli BL21(DE3)
-
gene ehcp112, functional expression of the His-tagged full-length EhCP112 zymogen, containing the signal peptide and the pro-peptide, in Escherichia coli strain BL21
-
gene Ehcp112, gene is encoded adjacent to Ehadh112, the latter encoding an adhesin that is covalently connected to the enzyme by electrostatic forces, DNA sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli BL21(DE3)
-
genes ehcp1, ehcp2, and ehcp5, stable episomal transfection, overexpression of EhCP5 highly increases activity of EhCP1, EhCP2, and EhCP5 in recombinant amoeba and cytopathic activity, while overexpression of EhCP1 or 2 enhances only the single activity and moderately enhances cytopathic activity, overview
-
recombinant expression of the His-tagged enzyme in Escherichia coli inclusion bodies
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CP5 expression is significantly higher in the Entamoeba histolytica strain EGG isolated from liver than in the other strains maintained in culture (5.6fold higher than strain 32, 4.1fold higher than strain HM1 and 3.0fold higher than cultured strain EGG)
-
cysteine protease 6 is upregulated in response to heat shock and during pathogen invasion of the host tissue
when Entamoeba histolytica is grown in the presence of E-64, PCP5 levels are significantly increased
cysteine protease 6 is upregulated in response to heat shock and during pathogen invasion of the host tissue
cysteine protease 6 is upregulated in response to heat shock and during pathogen invasion of the host tissue
-
-
when Entamoeba histolytica is grown in the presence of E-64, PCP5 levels are significantly increased
-
when Entamoeba histolytica is grown in the presence of E-64, PCP5 levels are significantly increased
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
2 mM SDS is the only surfactant that is effective at promoting the refolding and activation of the enzyme
-
recombinant His-tagged enzyme, solvation in 20 mM sodium phosphate, pH 7.4, 0.5 M NaCl, 10 mM imidazole, and 8 M urea, refolding and processing of the inactive precursor, ppEhCP112, to a 35.5 kDa mature and active enzyme, EhCP112
-
renaturation of purified inactive pro-enzyme by a 100fold dilution in a buffer containing reduced and oxidized thiols leading to a soluble inactive pro-enzyme
-
using 50 mM Tris pH 6.8,150 mM NaCl, 5% (v/v) glycerol, 0.5 mM oxidised glutathione, 3 mM reduced glutathione, at 4°C
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luaces, A.L.; Barrett, A.J.
Affinity purification and biochemical characterization of histolysin, the major cysteine proteinase of Entamoeba histolytica
Biochem. J.
250
903-909
1988
Entamoeba histolytica
brenda
Navarro-Garcia, F.; Chavez-Duenas, L.; Tsutsumi, V.; Posadas del Rio, F.; Lopez-Revilla, R.
Entamoeba histolytica: increase of enterotoxicity and of 53- and 75-kDa cysteine proteinases in a clone of higher virulence
Exp. Parasitol.
80
361-372
1995
Entamoeba histolytica
brenda
Scholze, H.; Loehden-Bendinger, U.; Mueller, G.; Bakker-Grunwald, T.
Subcellular distribution of amebapain, the major cysteine proteinase of Entamoeba histolytica
Arch. Med. Res.
23(3)
105-108
1992
Entamoeba histolytica
brenda
Scholze, H.; Werries, E.
A weakly acidic protease has a powerful proteolytic activity in Entamoeba histolytica
Mol. Biochem. Parasitol.
11
293-300
1984
Entamoeba histolytica
brenda
Scholze, H.; Schulte, W.
On the specificity of a cysteine proteinase from Entamoeba histolytica
Biomed. Biochim. Acta
47
115-123
1988
Entamoeba histolytica
brenda
Perez-Montfort, R.; Ostoa-Saloma, P.; Velazquez-Medina, L.; Montfort, I.; Becker, I.
Catalytic classes of proteinases of Entamoeba histolytica
Mol. Biochem. Parasitol.
26
87-97
1987
Entamoeba histolytica, Entamoeba histolytica HM 1:IMSS
brenda
Schulte, W.; Sholze, H.; Werries, E.
Specificity of a cysteine proteinase of Entamoeba histolytica towards the alpha 1-CB2 peptide of bovine collagen type I
Mol. Biochem. Parasitol.
25
39-43
1987
Entamoeba histolytica
brenda
Keene, W.E.; Petitt, M.G.; Allen, S.; McKerrow, J.H.
The major neutral proteinase of Entamoeba histolytica
J. Exp. Med.
163
536-549
1986
Entamoeba histolytica
brenda
Scholze, H.; Otte, J.; Werries, E.
Cysteine proteinase of Entamoeba histolytica. II. Identification of the major split position in bovine insulin B-chain
Mol. Biochem. Parasitol.
18
113-121
1986
Entamoeba histolytica
brenda
Scholze, H.; Werries, E.
Cysteine proteinase of Entamoeba histolytica. I. Partial purification and action on different enzymes
Mol. Biochem. Parasitol.
18
103-112
1986
Entamoeba histolytica
brenda
Franco, E.; de Araujo Soares, R.M.; Meza, I.
Specific and reversible inhibition of Entamoeba histolytica cysteine-proteinase activities by Zn2+: implications for adhesion and cell damage
Arch. Med. Res.
30
82-88
1999
Entamoeba histolytica
brenda
Spinella, S.; Levavasseur, E.; Petek, F.; Rigothier, M.C.
Purification and biochemical characterization of a novel cysteine protease of Entamoeba histolytica
Eur. J. Biochem.
266
170-180
1999
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
brenda
Moncada, D.; Keller, K.; Chadee, K.
Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function
Infect. Immun.
71
838-844
2003
Entamoeba histolytica
brenda
Jacobs, T.; Bruchhaus, I.; Dankebar, T.; Tannich, E.; Leippe, M.
Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
Mol. Microbiol.
27
169-276
1998
Entamoeba histolytica (Q95030)
-
brenda
Garcia-Rivera, G.; Rodriguez, M.A.; Ocadiz, R.; Martinez-Lopez, M.C.; Arroyo, R.; Gonzalez-Robles, A.; Orozco, E.
Entamoeba histolytica: a novel cysteine protease and an adhesin form the 112kDa surface protein
Mol. Microbiol.
33
556-568
1999
Entamoeba histolytica
brenda
Hellberg, A.; Nowak, N.; Leippe, M.; Tannich, E.; Bruchhaus, I.
Recombinant expression and purification of an enzymatically active cysteine proteinase of the protozoan parasite Entamoeba histolytica
Protein Expr. Purif.
24
131-137
2002
Entamoeba histolytica
brenda
Ocadiz, R.; Orozco, E.; Carrillo, E.; Quintas, L.I.; Ortega-Lopez, J.; Garcia-Perez, R.M.; Sanchez, T.; Castillo-Juarez, B.A.; Garcia-Rivera, G.; Rodriguez, M.A.
EhCP112 is an Entamoeba histolytica secreted cysteine protease that may be involved in the parasite-virulence
Cell. Microbiol.
7
221-232
2005
Entamoeba histolytica
brenda
Moncada, D.; Keller, K.; Ankri, S.; Mirelman, D.; Chadee, K.
Antisense inhibition of Entamoeba histolytica cysteine proteases inhibits colonic mucus degradation
Gastroenterology
130
721-730
2006
Entamoeba histolytica
brenda
Scholze, H.; Tannich, E.
Histolysain and other Entamoeba cysteine endopeptidases
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2
1164-1166
2004
Entamoeba dispar, Entamoeba histolytica
-
brenda
Nowak, N.; Lotter, H.; Tannich, E.; Bruchhaus, I.
Resistance of Entamoeba histolytica to the cysteine proteinase inhibitor E64 is associated with secretion of pro-enzymes and reduced pathogenicity
J. Biol. Chem.
279
38260-38266
2004
Entamoeba histolytica
brenda
Tillack, M.; Nowak, N.; Lotter, H.; Bracha, R.; Mirelman, D.; Tannich, E.; Bruchhaus, I.
Increased expression of the major cysteine proteinases by stable episomal transfection underlines the important role of EhCP5 for the pathogenicity of Entamoeba histolytica
Mol. Biochem. Parasitol.
149
58-64
2006
Entamoeba histolytica
brenda
Pertuz Belloso, S.; Ostoa Saloma, P.; Benitez, I.; Soldevila, G.; Olivos, A.; Garcia-Zepeda, E.
Entamoeba histolytica cysteine protease 2 (EhCP2) modulates leucocyte migration by proteolytic cleavage of chemokines
Parasite Immunol.
26
237-241
2004
Entamoeba histolytica
brenda
Lidell, M.E.; Moncada, D.M.; Chadee, K.; Hansson, G.C.
Entamoeba histolytica cysteine proteases cleave the MUC2 mucin in its C-terminal domain and dissolve the protective colonic mucus gel
Proc. Natl. Acad. Sci. USA
103
9298-9303
2006
Entamoeba histolytica
brenda
Saito-Nakano, Y.; Mitra, B.N.; Nakada-Tsukui, K.; Sato, D.; Nozaki, T.
Two Rab7 isotypes, EhRab7A and EhRab7B, play distinct roles in biogenesis of lysosomes and phagosomes in the enteric protozoan parasite Entamoeba histolytica
Cell. Microbiol.
9
1796-1808
2007
Entamoeba histolytica
brenda
Mitra, B.N.; Saito-Nakano, Y.; Nakada-Tsukui, K.; Sato, D.; Nozaki, T.
Rab11B small GTPase regulates secretion of cysteine proteases in the enteric protozoan parasite Entamoeba histolytica
Cell. Microbiol.
9
2112-2125
2007
Entamoeba histolytica, Entamoeba histolytica (Q01957), Entamoeba histolytica (Q01958)
brenda
Melendez-Lopez, S.G.; Herdman, S.; Hirata, K.; Choi, M.H.; Choe, Y.; Craik, C.; Caffrey, C.R.; Hansell, E.; Chavez-Munguia, B.; Chen, Y.T.; Roush, W.R.; McKerrow, J.; Eckmann, L.; Guo, J.; Stanley, S.L.; Reed, S.L.
Use of recombinant Entamoeba histolytica cysteine proteinase 1 to identify a potent inhibitor of amebic invasion in a human colonic model
Eukaryot. Cell
6
1130-1136
2007
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
brenda
Sato, D.; Nakada-Tsukui, K.; Okada, M.; Nozaki, T.
Two cysteine protease inhibitors, EhICP1 and 2, localized in distinct compartments, negatively regulate secretion in Entamoeba histolytica
FEBS Lett.
580
5306-5312
2006
Entamoeba histolytica, Entamoeba histolytica (Q01957), Entamoeba histolytica (Q01958)
brenda
Quintas-Granados, L.I.; Orozco, E.; Brieba, L.G.; Arroyo, R.; Ortega-Lopez, J.
Purification, refolding and autoactivation of the recombinant cysteine proteinase EhCP112 from Entamoeba histolytica
Protein Expr. Purif.
63
26-32
2009
Entamoeba histolytica
brenda
Freitas, M.A.; Fernandes, H.C.; Calixto, V.C.; Martins, A.S.; Silva, E.F.; Pesquero, J.L.; Gomes, M.A.
Entamoeba histolytica: cysteine proteinase activity and virulence. Focus on cysteine proteinase 5 expression levels
Exp. Parasitol.
122
306-309
2009
Entamoeba histolytica
brenda
Casados-Vazquez, L.E.; Lara-Gonzalez, S.; Brieba, L.G.
Crystal structure of the cysteine protease inhibitor 2 from Entamoeba histolytica: functional convergence of a common protein fold
Gene
471
45-52
2011
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
brenda
Hou, Y.; Mortimer, L.; Chadee, K.
Entamoeba histolytica cysteine proteinase 5 binds integrin on colonic cells and stimulates NFkappaB-mediated pro-inflammatory responses
J. Biol. Chem.
285
35497-35504
2010
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
brenda
Zamudio-Prieto, O.; Benitez-Cardoza, C.; Arroyo, R.; Ortega-Lopez, J.
Conformational changes induced by detergents during the refolding of chemically denatured cysteine protease ppEhCP-B9 from Entamoeba histolytica
Biochim. Biophys. Acta
1844
1299-1306
2014
Entamoeba histolytica
brenda
Lee, Y.A.; Nam, Y.H.; Min, A.; Kim, K.A.; Nozaki, T.; Saito-Nakano, Y.; Mirelman, D.; Shin, M.H.
Entamoeba histolytica-secreted cysteine proteases induce IL-8 production in human mast cells via a PAR2-independent mechanism
Parasite
21
1-1
2014
Entamoeba histolytica
brenda
Ghosh, A.; Raha, S.
Molecular and functional characterisation of a stress responsive cysteine protease, EhCP6 from Entamoeba histolytica
Protein Expr. Purif.
109
55-61
2015
Entamoeba histolytica (C4LSI6), Entamoeba histolytica, Entamoeba histolytica HM1:IMSS (C4LSI6)
brenda
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