Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ventoso, I.; Blanco, R.; Perales, C.; Carrasco, L.
    HIV-1 protease cleaves eukaryotic initiation factor 4G and inhibits cap-dependent translation (2001), Proc. Natl. Acad. Sci. USA, 98, 12966-12971.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.16 eIF4GI + H2O Human immunodeficiency virus 1 perhaps cleavage of eIF4G is an event that contributes to a more efficient translation of the genomic HIV-1 mRNA, proteolysis of eIF4GI inhibits protein synthesis directed by capped mRNAs but allows internal ribosome entry site-driven translation, purified enzyme cleaves at positions 678-679, 681-682 and 1086-1087, separating the three domains of the initiation factor ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.16 Human immunodeficiency virus 1
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.16 eIF4GI + H2O perhaps cleavage of eIF4G is an event that contributes to a more efficient translation of the genomic HIV-1 mRNA, proteolysis of eIF4GI inhibits protein synthesis directed by capped mRNAs but allows internal ribosome entry site-driven translation, purified enzyme cleaves at positions 678-679, 681-682 and 1086-1087, separating the three domains of the initiation factor Human immunodeficiency virus 1 ?
-
?
3.4.23.16 elF4GI + H2O purified enzyme cleaves at positions 678-679, 681-682 and 1086-1087, separating the three domains of the initiation factor Human immunodeficiency virus 1 additional information
-
?