3.4.23.16: HIV-1 retropepsin
This is an abbreviated version!
For detailed information about HIV-1 retropepsin, go to the full flat file.
Word Map on EC 3.4.23.16
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3.4.23.16
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antiretroviral
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ritonavir
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transcriptase
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saquinavir
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indinavir
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nelfinavir
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hiv-infected
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lopinavir
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polyproteins
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flap
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darunavir
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amprenavir
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drug-resistant
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anti-hiv
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atazanavir
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virological
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haart
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gag-pol
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peptidomimetic
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virion
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p-glycoprotein
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lipodystrophy
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non-nucleoside
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integrase
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cross-resistance
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isostere
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nonpeptidic
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zidovudine
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nevirapine
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virus-1
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tipranavir
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cyp3a4
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nnrti
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drug-drug
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treatment-experienced
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lamivudine
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didanosine
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ritonavir-boosted
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autoprocessing
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efavirenz
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protease-inhibitor
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stavudine
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treatment-naive
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analysis
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raltegravir
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zalcitabine
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plasmepsins
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antiretroviral-naive
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pi-based
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pharmacology
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drug development
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medicine
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hiv-rna
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lipoatrophy
- 3.4.23.16
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antiretroviral
- ritonavir
- transcriptase
- saquinavir
- indinavir
- nelfinavir
-
hiv-infected
- lopinavir
- polyproteins
- flap
- darunavir
- amprenavir
-
drug-resistant
-
anti-hiv
- atazanavir
-
virological
-
haart
- gag-pol
-
peptidomimetic
- virion
- p-glycoprotein
- lipodystrophy
-
non-nucleoside
-
integrase
-
cross-resistance
- isostere
-
nonpeptidic
- zidovudine
- nevirapine
- virus-1
- tipranavir
- cyp3a4
-
nnrti
-
drug-drug
-
treatment-experienced
- lamivudine
- didanosine
-
ritonavir-boosted
-
autoprocessing
- efavirenz
-
protease-inhibitor
- stavudine
-
treatment-naive
- analysis
- raltegravir
- zalcitabine
-
plasmepsins
-
antiretroviral-naive
-
pi-based
- pharmacology
- drug development
- medicine
-
hiv-rna
-
lipoatrophy
Reaction
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro =
Synonyms
CRF01_AE protease, Gag protease, HIV aspartyl protease, HIV PR, HIV protease, HIV-1 aspartyl protease, HIV-1 PR, HIV-1 protease, HIV-1 proteinase, HIV-1PR, HIV-2 protease, HIVPR, human immunodeficiency virus 1 protease, human immunodeficiency virus 1 retropepsin, human immunodeficiency virus protease, human immunodeficiency virus type 1 protease, human immunodeficiency virus type I protease, More, PR, PR1, PR2, retropepsin, retroproteinase
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 3.4.23.16 - HIV-1 retropepsin
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REACTION DIAGRAM
eIF4GI + H2O
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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
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Gag polyprotein + H2O
matrix-capsid polyprotein + ?
Gag polyprotein with cleavage-site P12-P5/P5'-P12' residues
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Gag precursor polyprotein + H2O
mature Gag polyprotein + ?
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Gag protein + H2O
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proteolytic cleavage in the host cell cytoplasm
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Gag-Pol precursor polyprotein + H2O
mature Gag-Pol polyprotein + ?
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matrix-capsid polyprotein + H2O
DTGNNSQVSQNY + PIVQNLQGQMVH
i.e. DTGNNSQVSQNYPIVQNLQGQMVH
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Gag-Pol polyprotein + H2O
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proteolytic cleavage in the host cell cytoplasm
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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
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additional information
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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
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additional information
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the enzyme is responsible for the processing of gag and gag-pol polyprotein precursors to produce structural proteins and enzymes for the mature virus
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additional information
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the enzyme facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins
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additional information
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the enzyme is essential for the replication of the virus
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additional information
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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
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additional information
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Arg-Val-Leu-Ala-Glu-Ala-Met mimics the real substrate
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