3.4.22.35: Histolysain
This is an abbreviated version!
For detailed information about Histolysain, go to the full flat file.
Word Map on EC 3.4.22.35
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3.4.22.35
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cathepsins
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lysosomal
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cystatins
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papain
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calpains
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trypanosoma
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plasmodium
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falciparum
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papain-like
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cruzi
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resorption
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polyproteins
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antimalarial
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allergen
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caspase-1
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pyogenes
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chagas
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mite
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propeptide
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calcium-dependent
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osteoclast
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leupeptin
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trophozoite
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m-calpain
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asparaginyl
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proenzyme
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cruzipain
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warhead
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nsp2
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calpain-mediated
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hexakisphosphate
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pteronyssinus
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pyrogenic
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procathepsin
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cpp32
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streptococcal
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metacercariae
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3clpro
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autoprocessing
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bromelain
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kininogens
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calpastatin
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pineapple
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gingipains
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l-like
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alln
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osteoclast-mediated
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legumain
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collagenolytic
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dermatophagoides
- 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
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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
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collagenolytic
- dermatophagoides
Reaction
hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-/- in small molecule substrates including Z-Arg-Arg-/-NHMec =
Synonyms
Amebapain, amoebapain, CP1, CP2, CP5, CP6, cysteine protease, cysteine protease 1, cysteine protease 2, cysteine protease 5, cysteine protease 6, cysteine proteinase 1, cysteine proteinase 5, EhCP1, EhCP112, EhCP2, EhCP5, Entamoeba histolytica 112kDa adhesin, Entamoeba histolytica cysteine protease, Entamoeba histolytica cysteine proteinase, Entamoeba histolytica cysteine proteinase 5, Entamoeba histolytica cysteine-proteinase, Entamoeba histolytica neutral thiol proteinase, Histolysin, More, PCP5, ppEhCP-B9, Proteinase, Entamoeba histolytica cysteine
ECTree
3.4.22.35 HistolysainAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.22.35 - Histolysain
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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
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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
?
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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
?
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disruption of the protective mucin layer of targeted host cells, entry mechanism of the pathogen, overview
-
-
?
MUC2 mucin + H2O
?
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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
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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
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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
-
-
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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
?
-
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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
-
?
