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Literature summary for 3.4.22.29 extracted from

  • Bonderoff, J.M.; Larey, J.L.; Lloyd, R.E.
    Cleavage of poly(A)-binding protein by poliovirus 3C proteinase inhibits viral internal ribosome entry site-mediated translation (2008), J. Virol., 82, 9389-9399.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information coxsackievirus 2Apro cleaves eIF4G, separating the domains of eIF4GI or eIF4GII that bind to eIF4E (and mRNA) and eIF3 (and the 40S ribosome) and inhibits de novo translation initiation by interfering with the ribosome mRNA binding step ?
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Organism

Organism UniProt Comment Textmining
coxsackievirus
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Purification (Commentary)

Purification (Comment) Organism
Coxsackievirus B3 2Apro is purified from pET-Cx2A using ion-exchange chromatography and gel filtration coxsackievirus

Source Tissue

Source Tissue Comment Organism Textmining
infected cell
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coxsackievirus
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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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cleavage of poly(A)-binding protein by 2Apro is incomplete, a single 2Apro cleavage product can be observed late in the reaction, and 8fold-higher levels of 2A protease produce only marginally higher levels of cleavage coxsackievirus
additional information
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combined 2Apro and 3Cpro result in a net stimulation of poliovirus internal ribosome entry site-mediated translation, the resulting rate of translation is about 3fold greater than the control value but not as great as the 4fold stimulation of translation from preincubation with 2Apro alone coxsackievirus
additional information
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low concentrations of 2Apro produce complete cleavage of eIF4GI in less than 5 min, producing several cleavage products from the multiple eIF4GI isoforms coxsackievirus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 2Apro cleaves eIF4G, separating the domains of eIF4GI or eIF4GII that bind to eIF4E (and mRNA) and eIF3 (and the 40S ribosome) and inhibits de novo translation initiation by interfering with the ribosome mRNA binding step coxsackievirus ?
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?

Synonyms

Synonyms Comment Organism
2A proteinase
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coxsackievirus
2Apro
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coxsackievirus

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
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assay at coxsackievirus