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Information on EC 3.4.22.29 - picornain 2A
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3.4.22.29 picornain 2ASpecify your search results
Word Map
- 3.4.22.29
- polyprotein
- enteroviruses
- eif4gi
-
capsid
- picornaviruses
- foot-and-mouth
-
enteroviral
- 3cpro
-
shutoff
- rhinoviruses
- myocarditis
-
cap-independent
-
deubiquitinating
-
poliovirus-infected
-
encephalomyocarditis
- picornaviridae
-
cap-binding
-
eif-4f
-
ires-driven
-
dicistronic
- polioviruses
-
ires-dependent
-
2a-mediated
-
rhinoviral
-
polya-binding
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
2apro, 2a protease, usp2a, protease 2a, 2a proteinase, proteinase 2a, poliovirus 2apro, poliovirus 2a protease, ubiquitin-specific protease 2a, poliovirus protease 2a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2A protease
2A proteinase
2Apro
enterovirus 2A protease
EV71-2A
P2A
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-
-
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picornaviral 2A proteinase
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-
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picornavirus 2A proteinase
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picornavirus endopeptidase 2A
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poliovirus protease 2A
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-
-
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protease 2A
proteinase 2A
proteinase 2Apro
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-
-
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proteinase, poliovirus, 2A
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-
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PV 2Apro
rhinovirus protease 2A
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-
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Y-G proteinase 2A
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-
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2A protease
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-
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2A proteinase
-
-
-
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protease 2A
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Tyr-/-Gly bond in picornavirus polyprotein
-
-
-
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selective cleavage of Tyr-/-Gly bond in picornavirus polyprotein
substrate region exchanges in and out of a conformation in which it occupies the active site with association and dissociation rates in the range of 100 to 1000 per s
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
103406-62-8
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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
1C'D2A precursor polypeptide + H2O
?
-
i.e. autocatalytic cis cleavage activity, cleaves at 1D/2A junction in very rapid cotranslational reaction
-
-
?
2-aminobenzoic acid-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Phe(NO2)-Ala-OH + H2O
?
-
-
-
-
?
3CD-precursor poliovirus protein + H2O
poliovirus 3C' and 3D'-protein
-
-
-
?
acetyl-LSTT-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-LSTT + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Arg-Arg-Asn-Thr-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Arg-Arg-Asn-Thr-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein, poor substrate
-
?
Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P7-P8', hydrolyzed with about the same relative efficiency compared to P8-P8'
-
?
capsid precursor protein P1 + H2O
viral protein 1ABC + viral protein 1D
-
-
-
?
cellular eukaryotic translation initiation factor eIF4GI + H2O
peptides
-
-
-
-
?
cellular eukaryotic translation initiation factor eIF4GII + H2O
peptides
-
-
-
-
?
Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein
-
?
Glu-Arg-Ala-Ser-Leu-Ile-Thr-Thr-Gly-Pro-Tyr-Gly-His-Gln-Ser-Gly + H2O
Glu-Arg-Ala-Ser-Leu-Ile-Thr-Thr-Gly-Pro-Tyr + Gly-His-Gln-Ser-Gly
-
-
-
-
?
Gly-Leu-Gly-Gln-Met methyl ester + H2O
Gly-Leu-Gly-Gln-Met + CH3OH
-
esterase activity
-
?
Grb2-associated binding protein 1 + H2O
?
-
GAB1 is cleaved during CV-B3 infection by viral proteinase 2A
-
-
?
GRTTLST-(3-nitrotyrosine)-GPPR-(lysine anthranilide)-Y + H2O
GRTTLST-(3-nitrotyrosine) + GPPR-(lysine anthranilide)-Y
-
-
-
-
?
HRV 3Cpro precursor 3CD + H2O
3Cpro + 3Dpro
-
activation of 3C protease, EC 3.4.22.28, of human rhinovirus A-16
-
-
?
human eukaryotic translation initiation factor 4 G I + H2O
?
human eIF4GI
-
-
?
human eukaryotic translation initiation factor 4 G II + H2O
?
human eIF4GII
-
-
?
Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P5-P8', poor substrate
-
?
Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P4-P8', poor substrate
-
?
modified pentadecameric peptides + H2O
?
-
i.e. synthetic P8-P7' peptides, intermolecular specificity, changes at P2 and P1' are highly deleterious
-
-
?
oligopeptides corresponding to cleavage sites of coxsackievirus + H2O
?
-
-
-
-
?
oligopeptides corresponding to cleavage sites of human rhinovirus + H2O
?
-
-
-
-
?
oligopeptides derived from eIF-4gamma + H2O
?
-
human rhinovirus, common cleavage site: Ala-Gly
-
-
?
picornavirus polyprotein + H2O
?
-
intramolecular reaction, processing begins before synthesis of the polyprotein is complete, cleavage separates capsid protein precursor and noncapsid protein precursor
-
-
?
poliovirus polyprotein fragment + H2O
hydrolyzed poliovirus polyprotein fragment
-
containing cleavage site at P1/P2 junction
partially cleaved in trans
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
-
contains 1 cleavage site for 2A proteinase within the proline-rich linker domain
-
-
?
Pro-Arg-Ala-Ser-Met-Lys-Thr-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Arg-Ala-Ser-Met-Lys-Thr-Val + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
poor substrate
-
?
Pro-Arg-Glu-Asn-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Arg-Glu-Asn-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein, poor substrate
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
i.e. synthetic peptide P6-P5', hydrolyzed with 42% relative efficiency compared to P8-P8'
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
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i.e. synthetic peptide P6-P6', hydrolyzed with 45% relative efficiency compared to P8-P8', smallest cleavable symmetric peptide
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
i.e. synthetic peptide P6-P7', hydrolyzed with 55% relative efficiency compared to P8-P8'
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
RKGDIKS-(3-nitrotyrosine)-GPGP-(lysine-anthranilide)-Y + H2O
RKGDIKS-(3-nitrotyrosine) + GPGP-(lysine-anthranilide)-Y
-
-
-
-
?
RKGDIKT-(3-nitrotyrosine)-GPGP-(lysine-anthranilide)-Y + H2O
RKGDIKT-(3-nitrotyrosine) + GPGP-(lysine-anthranilide)-Y
-
-
-
-
?
Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein
-
?
Ser-Thr-Lys-Asn-Leu-Thr-Thr-Gly-Phe-Gly-His-Gln-Asn-Lys-Ala + H2O
Ser-Thr-Lys-Asn-Leu-Thr-Thr-Tyr + Gly-Phe-Gly-His-Gln-Asn-Lys-Ala
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synthetic hexadecapeptide corresponding to P1/P2 junction
-
?
Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr-Gly-Phe-Gly-His-Gln-Asn-Lys-Ala + H2O
Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr + Glys-Phe-Gly-His-Gln-Asn-Lys-Ala
-
poor substrate
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + glycine
-
i.e. synthetic peptide P8-P1', poor substrate, smallest cleavable asymmetric peptide
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro
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i.e. synthetic peptide P8-P2', hydrolyzed with about the same relative efficiency as P8-P8'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp
-
i.e. peptide P8-P4'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
i.e. peptide P8-P5'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
-
i.e. synthetic peptide P8-6'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
i.e. synthetic peptide P8-7'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Val-Tyr + H2O
?
-
-
-
-
?
TRPIITT-(3-nitrotyrosine)-GPSD-(lysine-anthranilate)-Y + H2O
TRPIITT-(3-nitrotyrosine) + GPSD-(lysine-anthranilate)-Y
-
-
-
-
?
cellular eukaryotic translation initiation factor 4G + H2O
?
-
eIF4GI, trans-cleavage
-
-
?
cytokeratin 8 + H2O
?
-
the cleavage results in removal of 14 amino acids from the N-terminal head domain of cytokeratin 8
-
-
?
cytokeratin 8 + H2O
?
-
the cleavage results in removal of 14 amino acids from the N-terminal head domain of cytokeratin 8. Cleavage occurs late in the infection cycle at the time of the onset of the cytopathic effect
-
-
?
death-associated protein 5 + H2O
?
-
DAP5, generation of 45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments, respectively. DAP5 is cleaved at amino acid G434
-
-
?
dystrophin + H2O
?
-
human dystrophin is cleaved between residue 588 and 589 and between residue 2434 and 2435. Rat dystrophin is cleaved between resiue 590 and 591 and between residue 2427 and 2428
-
-
?
dystrophin + H2O
?
-
cleavage of mouse dystrophin at residue 2427 and human dystrophin at residue 2434
-
-
?
dystrophin + H2O
?
-
the protease cleaves dystrophin in coxsackievirus B3-infected myocytes. The cleavage functionally impairs dystrophin
-
-
?
dystrophin + H2O
?
-
functional impairment and morphological disruption of dystrophin
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eIF4G + H2O
?
-
recombinant enzyme cleaves either rabbit or human eIF4G or their derived peptides, cleaves the 4G-derived peptides with 100fold lower efficiency than with a peptide derived from the poliovirus polyprotein. Up to 25fold molar excess of the enzyme over eIF4G protein is required to cause greater than 50% cleavage
-
-
?
eIF4G + H2O
?
-
self-processing is prerequisite for eIF4GI cleavage
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
-
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vitro
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
mapping of cleavage site
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
i.e. (eIF)-4Fgamma
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from HeLa cell extracts
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from rabbit
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
cleavage site: Arg486-Gly (rabbit), Arg485-Gly (human)
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vivo
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in-trans activity
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vitro
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
mapping of cleavage site
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
i.e. (eIF)-4Fgamma
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from HeLa cell extracts
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from rabbit
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
cleavage site: Arg486-Gly (rabbit), Arg485-Gly (human)
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vivo
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
the 2Apro cleavage site on eIF4GI is TLSTR*GPPR
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
eIF4G
-
-
?
Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
-
GAB2 is cleaved at G238 during CV-B3 infection by viral proteinase 2A, generating two cleaved fragments of GAB2-N1-237 and GAB2-C238-676
-
-
?
Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
-
GAB2 is cleaved at G238 during CV-B3 infection by viral proteinase 2A, generating two cleaved fragments of GAB2-N1-237 and GAB2-C238-676. mutant GAB2G238E is non-cleavable for the enzyme
-
-
?
nuclear factor of activated T cells 5/tonicity enhancer binding protein
?
-
NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, inactivation of NFAT5
-
-
?
nuclear factor of activated T cells 5/tonicity enhancer binding protein
?
-
NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, which is the only CVB3 protease 2A cleavage site on NFAT5, leading to inactivation of NFAT5
-
-
?
oligopeptides corresponding to cleavage sites of poliovirus type 1 + H2O
?
-
-
-
-
?
oligopeptides corresponding to cleavage sites of poliovirus type 1 + H2O
?
-
-
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from poliovirus
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from rhinovirus, cleaves P1/P2 junction
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro