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Literature summary for 3.4.22.29 extracted from

  • Bovee, M.L.; Lamphear, B.J.; Rhoads, R.E.; Lloyd, R.E.
    Direct cleavage of eIF4G by poliovirus 2A protease is inefficient in vitro (1998), Virology, 245, 241-249.
    View publication on PubMed
Search for more literature for 3.4.22.29

Organism

Organism UniProt Comment Textmining
coxsackievirus
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 B4
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Enterovirus C
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-
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Human rhinovirus sp.
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-
-

Purification (Commentary)

Purification (Comment) Organism
expression in Escherichia coli Enterovirus C
expression in Escherichia coli coxsackievirus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
eIF4G + H2O cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity Enterovirus C ?
-
 ?
eIF4G + H2O cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity coxsackievirus ?
-
 ?
eIF4G + H2O cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity Human rhinovirus sp. ?
-
 ?
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 Enterovirus C ?
-
 ?