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Literature summary for 3.4.23.B4 extracted from
- Feline immunodeficiency virus retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 178-182.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is a model target for development of inhibitors due to its similarity with the HIV-1 retropepsin, overview | feline immunodeficiency virus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the enzyme is encoded in the 5' end of the pol gene of FIV, nucleotide sequence determination, high-level recombinant expression, expression in Escherichia coli | feline immunodeficiency virus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure determination and analysis, recombinant enzyme | feline immunodeficiency virus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D30N | inactive mutant | feline immunodeficiency virus |
| additional information | generation of autolysis defective mutant enzymes | feline immunodeficiency virus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ac-GSGVFPSI[CH2NH]VVNGL-NH2 | strong inhibition of FIV retropepsin | feline immunodeficiency virus |  |
| Ac-naphthylalanine-Val-statine-Glu-naphthylalanine-NH2 | an inhibitor derived from aspartic proteinase inhibitors, statine is 3-hydroxy-4-amino-7-methylheptanoic acid | feline immunodeficiency virus | |
| additional information | structural features of compounds with high inhibitory potency, overview, e.g. small P3 residues results in highly inhibitory compounds | feline immunodeficiency virus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.033 | - |
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR | pH 5.3, 0.2 M NaCl, 0.1 mM EDTA, 1 mM DTT | feline immunodeficiency virus | |
| 10 | - |
RKEEGPPQAYPIQTVNGPQYR | pH 5.3, 37°C, 1 M NaCl | feline immunodeficiency virus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | increasing salt concentration up to 1.5 M increases the enzyme activity | feline immunodeficiency virus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gag-Pol polyprotein + H2O | feline immunodeficiency virus | processing of the precursor protein into several mature proteins | ? | - |
? | |
| Gag-Pol polyprotein + H2O | feline immunodeficiency virus FIV | processing of the precursor protein into several mature proteins | ? | - |
? | |
| additional information | feline immunodeficiency virus | the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa | ? | - |
? | |
| additional information | feline immunodeficiency virus FIV | the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| feline immunodeficiency virus | - |
FIV | - |
| feline immunodeficiency virus FIV | - |
FIV | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme performs autolytic processing of precursor protein | feline immunodeficiency virus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli | feline immunodeficiency virus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory | structure-function relationship and analysis, Asp30 is the catalytic residue | feline immunodeficiency virus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ac-RPQAYPIQTR-NH2 + H2O | specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of FIV | feline immunodeficiency virus | Ac-RPQAY + PIQTR-NH2 | - |
? | |
| Ac-RPQAYPIQTR-NH2 + H2O | specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of FIV | feline immunodeficiency virus FIV | Ac-RPQAY + PIQTR-NH2 | - |
? | |
| Ac-RSQNYPIVQR-NH2 + H2O | specific cleavage between Tyr and Pro, the peptide substrate represents the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein of HIV-1 | feline immunodeficiency virus | Ac-RSQNY + PIVQR-NH2 | - |
? | |
| Gag-Pol polyprotein + H2O | processing of the precursor protein into several mature proteins | feline immunodeficiency virus | ? | - |
? | |
| Gag-Pol polyprotein + H2O | cleavage between Tyr and Pro in the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein | feline immunodeficiency virus | ? | - |
? | |
| Gag-Pol polyprotein + H2O | processing of the precursor protein into several mature proteins | feline immunodeficiency virus FIV | ? | - |
? | |
| Gag-Pol polyprotein + H2O | cleavage between Tyr and Pro in the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein | feline immunodeficiency virus FIV | ? | - |
? | |
| additional information | the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa | feline immunodeficiency virus | ? | - |
? | |
| additional information | substrate specificity, cleavage sites of synthetic peptides corresponding to the natural cleavage sites of the Gag-Pol polyprotein, overview | feline immunodeficiency virus | ? | - |
? | |
| additional information | the enzyme performs autolytic processing of the precursor protein of which it is a part, cutting out itself and other proteins, the Gag polyprotein occurs in different splicing forms and sizes of 50-60 kDa to 150-200 kDa | feline immunodeficiency virus FIV | ? | - |
? | |
| additional information | substrate specificity, cleavage sites of synthetic peptides corresponding to the natural cleavage sites of the Gag-Pol polyprotein, overview | feline immunodeficiency virus FIV | ? | - |
? | |
| RALTK(epsilon-ABZ)VQF(NO2)VQSKGR + H2O | the synthetic peptide substrate mimicks the capsid/nucleocapsid cleavage site | feline immunodeficiency virus | RALTK(epsilon-ABZ)VQ + F(NO2)VQSKGR | - |
? | |
| RKEEGPPQAYPIQTVNGPQYR + H2O | the addition of Arg at the ends of the peptides subtrate increases the solubility, specific cleavage between Tyr and Pro, the peptide mimicks the linking of Ma and CA proteins of the Gag region in the Gag-Pol polyprotein in HIV-1 | feline immunodeficiency virus | RKEEGPPQAY + PIQTVNGPQYR | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | enzyme structure analysis, the FIV retropepsin contains three large surface loops, the central core is exposed, flaps cover the active-site cleft, structure comparison with the HIV-1 retropepsin, overview | feline immunodeficiency virus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Feline immunodeficiency virus retropepsin | - |
feline immunodeficiency virus |
| FIV retropepsin | - |
feline immunodeficiency virus |
| More | the enzyme belongs to the A2 peptidase family | feline immunodeficiency virus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | feline immunodeficiency virus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.29 | - |
RALTK(epsilon-ABZ)VQF(NO2)VQSKGR | pH 5.3, 0.2 M NaCl, 0.1 mM EDTA, 1 mM DTT | feline immunodeficiency virus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | - |
feline immunodeficiency virus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
feline immunodeficiency virus | |
| 0.00026 | - |
Ac-naphthylalanine-Val-statine-Glu-naphthylalanine-NH2 | - |
feline immunodeficiency virus | |
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