EC Number   |
Natural Substrates |
|---|
   3.4.23.16 | GagPol polyprotein + H2O |
- |
| 3.4.23.16 | matrix-capsid polyprotein + H2O |
i.e. DTGNNSQVSQNYPIVQNLQGQMVH |
| 3.4.23.16 | 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 |
| 3.4.23.16 | 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 |
| 3.4.23.16 | 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 |
| 3.4.23.16 | more |
the enzyme facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins |
| 3.4.23.16 | more |
the enzyme is essential for the replication of the virus |
| 3.4.23.16 | more |
the enzyme is involved in regulation of the incorporation of reverse transcriptase in the viral early assembly complex comprising reverse transcriptase, genomic RNA, Gag, Gag-Pol, tRNALys, and lysyl tRNA synthetase, HIV-1 protease activity is negatively regulated by the lysyl tRNA synthetase |
| 3.4.23.16 | more |
Arg-Val-Leu-Ala-Glu-Ala-Met mimics the real substrate |
| 3.4.23.16 | nucleocapsid protein + H2O |
- |
