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Information on EC 3.4.23.16 - HIV-1 retropepsin
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3.4.23.16 HIV-1 retropepsinSpecify your search results
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- 3.4.23.16
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antiretroviral
- ritonavir
- transcriptase
- saquinavir
- indinavir
- nelfinavir
- proteases
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hiv-infected
- flap
- polyproteins
- amprenavir
- lopinavir
- darunavir
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drug-resistant
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anti-hiv
- atazanavir
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virological
-
haart
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peptidomimetic
- p-glycoprotein
- virion
- gag-pol
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cross-resistance
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nonpeptidic
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non-nucleoside
-
integrase
- isostere
- lipodystrophy
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drug-drug
- zidovudine
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nnrti
- nevirapine
- tipranavir
- cyp3a4
- lamivudine
- didanosine
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treatment-naive
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treatment-experienced
-
protease-inhibitor
- stavudine
-
ritonavir-boosted
- efavirenz
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pi-based
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autoprocessing
- analysis
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plasmepsins
- zalcitabine
- pharmacology
- medicine
- raltegravir
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antiretroviral-naive
- drug development
-
inhibitor-containing
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hiv-rna
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
the kinetic mechanism of HIV-1 protease is random, in which products bind to form both binary and ternary enzyme-product complexes, depending on the substrate used
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specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
proteolysis mechanism whereby only one active site Asp is initially protonated. The steps of this mechanism are: asymmetric binding of the substrate, hydration of the peptidic carbonyl by an active site water, proton translocation between the active site Asp residue simultaneously with carbonyl hydration
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specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
flap closing and conformational change mechanism induced by substrate binding in HIV-1 aspartic protease, flap conformations in the active site during the catalytic cycle, molecular dynamic simulations, overview
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specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
the active site structure and conformational flexibility
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specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro
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