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Literature summary for 3.4.22.28 extracted from

  • Rivera, C.I.; Lloyd, R.E.
    Modulation of enteroviral proteinase cleavage of poly(A)-binding protein (PABP) by conformation and PABP-associated factors (2008), Virology, 375, 59-72.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.28

Activating Compound

Activating Compound Comment Organism Structure
additional information proteinase-active polypeptide precursor (3CD) and mature 3Cpro have equivalent cleavage activity on purified poly(A) binding protein, but only 3Cpro cleavage activity is stimulated by poly(A) binding protein-binding viral RNA Enterovirus C

Inhibitors

Inhibitors Comment Organism Structure
eukaryotic release factor 3 increasing concentrations of recombinant His-tagged eRF3 lead to partial inhibition of 3Cpro-proteolytic cleavage of poly(A) binding protein that increases modestly Enterovirus C
PABP-interacting protein 2 increasing concentrations of 1-3 microg inhibit cleavage of poly(A) binding protein by 3Cpro in a dose-dependent manner Enterovirus C

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
poly(A) binding protein + H2O Enterovirus C contains 2 main cleavage sites for 3C proteinase within the proline-rich linker domain, cleavage of recombinant protein with 3C proteinase heavily favors the 3Cpro primary cleavage site Q537/G538 over the 3CAlt cleavage site Q413/T414 fragments of poly(A) binding protein
-
 ?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O Enterovirus C
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 fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
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 ?

Organism

Organism UniProt Comment Textmining
Enterovirus C
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
infected cell
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 Enterovirus C
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 3Cpro cleavage of endogenous poly(A) binding protein in HeLa S10 lysates displays a rapid initial cleavage rate where 70% cleavage requires only 10 min incubation but very little additional substrate is cleaved upon extended incubation periods Enterovirus C
additional information
-
 addition of increasing concentrations of PABP-interacting protein 1 do not affect 3Cpro-mediated cleavage of poly(A) binding protein, at the highest concentration (3 microg) of PABP-interacting protein 1 tested, increasing concentrations of 3Cpro (1-3 microg) lead to a dose-dependent increase in cleavage of poly(A) binding protein Enterovirus C
additional information
-
 biphasic poly(A) binding protein cleavage kinetics by 3Cpro, about 30% of total protein is rapidly cleaved in 10 min, followed by a much slower cleavage rate that does not reach completion by 60 min or extended incubation periods Enterovirus C
additional information
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 cleavage kinetics analysis indicates that poly(A) binding protein exists in multiple conformations, some of which are resistant to 3Cpro cleavage and can be modulated by reducing potential Enterovirus C
additional information
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 poly(A) binding protein on cellular polysomes is cleaved only by 3Cpro Enterovirus C
additional information
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 poly(A) binding protein sediments with non-ribosome fractions, 40S and 80S ribosomes and polysome fractions, addition of 3Cpro to each of these fractions leads to partial cleavage in every case, and only slightly higher percent cleavage of poly(A) binding protein in polysome fractions or 40S-80S fractions Enterovirus C
additional information
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 the Ras-GTPase activating protein SH3 domain-binding protein 1 is rapidly cleaved by 3Cpro to completion when supplied as purified recombinant protein or as endogenous protein in HeLa S10 lysates Enterovirus C
additional information
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 while only 40-75% of poly(A) binding protein in S10 lysates is cleaved in vitro by 3Cpro, a crude ribosome pellet fraction, which is deficient in endogenous PABP-interacting protein 2, is cleaved by 95% Enterovirus C

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(A) binding protein + H2O contains 2 main cleavage sites for 3C proteinase within the proline-rich linker domain, cleavage of recombinant protein with 3C proteinase heavily favors the 3Cpro primary cleavage site Q537/G538 over the 3CAlt cleavage site Q413/T414 Enterovirus C fragments of poly(A) binding protein
-
 ?
Ras-GTPase activating protein SH3 domain-binding protein 1 + H2O
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 Enterovirus C fragments of Ras-GTPase activating protein SH3 domain-binding protein 1
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 ?

Synonyms

Synonyms Comment Organism
3C proteinase
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 Enterovirus C
3Cpro
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 Enterovirus C

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Enterovirus C

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Enterovirus C