Cloned (Comment) | Organism |
---|---|
genetic organization, processing steps, expression of the viral enzyme in bacterial and yeast recombinant systems | Human immunodeficiency virus 2 |
Crystallization (Comment) | Organism |
---|---|
substrate binding pocket structure analysis | Human immunodeficiency virus 2 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a hybrid gene with the viral reverse transcriptase, constuction of a hybrid comprising HIV-1 and HIV-2 retropepsin, overview | Human immunodeficiency virus 2 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 2 | |
acetyl-pepstatin | - |
Human immunodeficiency virus 2 | |
pepstatin A | - |
Human immunodeficiency virus 2 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Human immunodeficiency virus 2 | |
0.16 | - |
YVSQNFPIVQNR | pH 4.7 | Human immunodeficiency virus 2 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 2 | - |
i.e. HIV-2 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | self-processing of the immature progeny virus at the host cell membrane prior to virus budding, dimerization occurs before proteolytic cleavage | Human immunodeficiency virus 2 |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Endopeptidase for which the P1 residue is preferably hydrophobic | substrate binding pocket structure and reaction mechanism, the enzyme prefers the cleavage site sequence VSQNY*PIVQ with Glu being preferred at the P2' site | Human immunodeficiency virus 2 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
HIV-1 Gag-Pol poylprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 2 | ? | - |
? | |
HIV-2 Gag-Pol poylprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 2 | ? | - |
? | |
Lys-Ala-Arg-Val-Nle-Nph-Glu-Ala-Nle-NH2 + H2O | the enzyme is highly active with peptide substrates containing variations of this cleavage sequence | Human immunodeficiency virus 2 | Lys-Ala-Arg-Val-Nle + Nph-Glu-Ala-Nle-NH2 | - |
? | |
additional information | the enzyme prefers the cleavage site sequence VSQNY*PIVQ with Glu being preferred at the P2' site | Human immunodeficiency virus 2 | ? | - |
? | |
myristylated p53-Gag precursor + H2O | - |
Human immunodeficiency virus 2 | ? | - |
? | |
p24-Gag protein + H2O | - |
Human immunodeficiency virus 2 | ? | - |
? | |
YVSQNFPIVQNR + H2O | synthetic peptide substrate based on the Ma/Ca cleavage site of HIV-1 Gag | Human immunodeficiency virus 2 | YVSQNF + PIVQNR | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the HIV-2 retropepsin must form a homodimer in order to create a functional active site, dimerization occurs before proteolytic cleavage | Human immunodeficiency virus 2 |
Synonyms | Comment | Organism |
---|---|---|
HIV-2 proteinase | - |
Human immunodeficiency virus 2 |
human immunodeficiency virus 2 retropepsin | - |
Human immunodeficiency virus 2 |
More | the enzyme belongs to the peptidase family A2 | Human immunodeficiency virus 2 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.7 | - |
assay at | Human immunodeficiency virus 2 |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0000012 | - |
(hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 2 | |
0.000005 | - |
acetyl-pepstatin | pH 4.7, competitive versus YVSQNFPIVQNR | Human immunodeficiency virus 2 | |
0.000015 | - |
pepstatin A | pH 4.7 | Human immunodeficiency virus 2 |