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Literature summary extracted from
- Human immunodeficiency virus 2 retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rowlings, N. D. ; Woessner, J. F. , eds. ), 1, 154-157.
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.23.16 | - |
Human immunodeficiency virus 1 |
| 3.4.23.47 | genetic organization, processing steps, expression of the viral enzyme in bacterial and yeast recombinant systems | Human immunodeficiency virus 2 |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.23.16 | substrate binding pocket structure analysis | Human immunodeficiency virus 1 |
| 3.4.23.47 | substrate binding pocket structure analysis | Human immunodeficiency virus 2 |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.23.16 | additional information | constuction of a hybrid comprising HIV-1 and HIV-2 retropepsin, overview | Human immunodeficiency virus 1 |
| 3.4.23.47 | 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
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.23.16 | (hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 1 |  |
| 3.4.23.16 | acetyl-pepstatin | - |
Human immunodeficiency virus 1 | |
| 3.4.23.16 | pepstatin A | - |
Human immunodeficiency virus 1 | |
| 3.4.23.47 | (hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 2 | |
| 3.4.23.47 | acetyl-pepstatin | - |
Human immunodeficiency virus 2 | |
| 3.4.23.47 | pepstatin A | - |
Human immunodeficiency virus 2 | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.23.16 | additional information | - |
additional information | - |
Human immunodeficiency virus 1 | |
| 3.4.23.16 | 0.064 | - |
YVSQNFPIVQNR | pH 4.7 | Human immunodeficiency virus 1 | |
| 3.4.23.47 | additional information | - |
additional information | - |
Human immunodeficiency virus 2 | |
| 3.4.23.47 | 0.16 | - |
YVSQNFPIVQNR | pH 4.7 | Human immunodeficiency virus 2 | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.23.16 | Human immunodeficiency virus 1 | - |
i.e. HIV-1 | - |
| 3.4.23.47 | Human immunodeficiency virus 2 | - |
i.e. HIV-2 | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.23.16 | 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 1 |
| 3.4.23.47 | 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
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.23.47 | 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 and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.23.16 | HIV-1 Gag-Pol polyprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 1 | ? | - |
? | |
| 3.4.23.16 | HIV-2 Gag-Pol poylprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 1 | ? | - |
? | |
| 3.4.23.16 | YVSQNFPIVQNR + H2O | synthetic peptide substrate based on the Ma/Ca cleavage site of HIV-1 Gag | Human immunodeficiency virus 1 | YVSQNF + PIVQNR | - |
? | |
| 3.4.23.47 | HIV-1 Gag-Pol poylprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 2 | ? | - |
? | |
| 3.4.23.47 | HIV-2 Gag-Pol poylprotein + H2O | site-specific proteolytic cleavage, protein precursors and peptides derived thereof | Human immunodeficiency virus 2 | ? | - |
? | |
| 3.4.23.47 | 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 | - |
? | |
| 3.4.23.47 | additional information | the enzyme prefers the cleavage site sequence VSQNY*PIVQ with Glu being preferred at the P2' site | Human immunodeficiency virus 2 | ? | - |
? | |
| 3.4.23.47 | myristylated p53-Gag precursor + H2O | - |
Human immunodeficiency virus 2 | ? | - |
? | |
| 3.4.23.47 | p24-Gag protein + H2O | - |
Human immunodeficiency virus 2 | ? | - |
? | |
| 3.4.23.47 | YVSQNFPIVQNR + H2O | synthetic peptide substrate based on the Ma/Ca cleavage site of HIV-1 Gag | Human immunodeficiency virus 2 | YVSQNF + PIVQNR | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.23.16 | 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 1 |
| 3.4.23.47 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.23.16 | HIV-1 proteinase | - |
Human immunodeficiency virus 1 |
| 3.4.23.16 | human immunodeficiency virus 1 retropepsin | - |
Human immunodeficiency virus 1 |
| 3.4.23.16 | More | the enzyme belongs to the peptidase family A2 | Human immunodeficiency virus 1 |
| 3.4.23.47 | HIV-2 proteinase | - |
Human immunodeficiency virus 2 |
| 3.4.23.47 | human immunodeficiency virus 2 retropepsin | - |
Human immunodeficiency virus 2 |
| 3.4.23.47 | More | the enzyme belongs to the peptidase family A2 | Human immunodeficiency virus 2 |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.16 | 4.7 | - |
assay at | Human immunodeficiency virus 1 |
| 3.4.23.47 | 4.7 | - |
assay at | Human immunodeficiency virus 2 |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.23.16 | 0.0000000075 | - |
(hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 1 | |
| 3.4.23.16 | 0.0000014 | - |
pepstatin A | about, pH 4.7 | Human immunodeficiency virus 1 | |
| 3.4.23.16 | 0.00002 | - |
acetyl-pepstatin | pH 4.7, competitive versus YVSQNFPIVQNR | Human immunodeficiency virus 1 | |
| 3.4.23.47 | 0.0000012 | - |
(hydroxyethyl)amide isostere | - |
Human immunodeficiency virus 2 | |
| 3.4.23.47 | 0.000005 | - |
acetyl-pepstatin | pH 4.7, competitive versus YVSQNFPIVQNR | Human immunodeficiency virus 2 | |
| 3.4.23.47 | 0.000015 | - |
pepstatin A | pH 4.7 | Human immunodeficiency virus 2 | |
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