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Results 1 - 10 of 18 > >>
EC Number
Natural Substrates
Commentary (Nat. Sub.)
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
Gag polyprotein + H2O
-
Gag polyprotein + H2O
substrate sites, overview
Gag protein + H2O
proteolytic cleavage in the host cell cytoplasm
Gag-Pol polyprotein + H2O
-
Gag-Pol polyprotein + H2O
proteolytic cleavage in the host cell cytoplasm
GagPol polyprotein + H2O
-
more
the enzyme plays an essential role in the late-stage maturation step of the virus replication cycle. HIV-1 proteinase autocatalyzes its own cleavage from the Pr165 polyprotein precursor and then cleaves both polyproteins at other specific sites to produce mature proteins
more
regulation of the protease in the viral life cycle: transframe region flanking the N-terminus of the protease may function as a negative regulator for protein folding and dimerization. The low dimer stability of the protease precursor relative to that of the mature enzyme is an ideal way of preventing the emergence of enzymatic functions until assembly of the viral particle is complete
more
the enzyme is responsible for the processing of gag and gag-pol polyprotein precursors to produce structural proteins and enzymes for the mature virus
Results 1 - 10 of 18 > >>