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Literature summary for 3.4.23.B9 extracted from
- Bovine leukemia virus retropepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 169-171.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | bovine leukemia virus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ac-Pro-Glu-Val-Leu-azetidine-Val-Met | IC50: 0.250 mM | bovine leukemia virus |  |
| Ac-Pro-Glu-Val-Leu-pipecolic acid-Val-Met | IC50: 0.015 mM | bovine leukemia virus | |
| cerulenin | IC50: 5 mM | bovine leukemia virus | |
| Cu2+ | - |
bovine leukemia virus | |
| Gly-Val-Leu-Tyr-statine-Glu-Ala | IC50: 0.10 mM | bovine leukemia virus | |
| pepstatin A | IC50: 0.3-0.5 mM | bovine leukemia virus | |
| Pro-Glu-Val-statine-Ala-Leu | IC50: 0.10 mM | bovine leukemia virus | |
| YDPPAI-statine-II | strong inhibition, IC50: 0.0005 mM | bovine leukemia virus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| ammonium sulfate | activates | bovine leukemia virus | |
| NaCl | activates at 1-2 M | bovine leukemia virus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 14000 | - |
2 * 14000 | bovine leukemia virus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gag polyprotein + H2O | bovine leukemia virus | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | ? | - |
? | |
| Gag polyprotein + H2O | bovine leukemia virus BLV | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | ? | - |
? | |
| Gag-Pol polyprotein + H2O | bovine leukemia virus | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | ? | - |
? | |
| Gag-Pol polyprotein + H2O | bovine leukemia virus BLV | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| bovine leukemia virus | - |
BLV | - |
| bovine leukemia virus BLV | - |
BLV | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | autolytic processing, the enzyme can hydrolyze its own N- and C-terminals, e.g. by cleaving the C-terminal site ASISI-/-PEEV during storage | bovine leukemia virus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from viral particles under denaturing conditions, and recombinant enzyme from Escherichia coli | bovine leukemia virus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| The best substrate YDPPAILPII is bearing the natural cleavage site between the matrix and the capsid proteins of BLV Gag precursor. polyprotein. Good cleavage of the peptide bonds: Leu-Pro, Leu-Val, Gly-Val and Leu-Pro | the enzyme contains the aspartic protease sequence Asp-Thr-Gly | bovine leukemia virus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Gag polyprotein + H2O | - |
bovine leukemia virus | ? | - |
? | |
| Gag polyprotein + H2O | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | bovine leukemia virus | ? | - |
? | |
| Gag polyprotein + H2O | - |
bovine leukemia virus BLV | ? | - |
? | |
| Gag polyprotein + H2O | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | bovine leukemia virus BLV | ? | - |
? | |
| Gag-Pol polyprotein + H2O | - |
bovine leukemia virus | ? | - |
? | |
| Gag-Pol polyprotein + H2O | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | bovine leukemia virus | ? | - |
? | |
| Gag-Pol polyprotein + H2O | - |
bovine leukemia virus BLV | ? | - |
? | |
| Gag-Pol polyprotein + H2O | processing of the precursor protein into mature structural proteins of the matrix, capsid, and nucleocapsid, and the functional protease | bovine leukemia virus BLV | ? | - |
? | |
| YDPPAILPII + H2O | represents the CA/NC cleavage site of the Gag polyprotein | bovine leukemia virus | YDPPAIL + Pro-Ile-Ile | - |
? | |
| YDPPAILPII + H2O | represents the CA/NC cleavage site of the Gag polyprotein | bovine leukemia virus BLV | YDPPAIL + Pro-Ile-Ile | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 14000 | bovine leukemia virus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BLV endopeptidase | - |
bovine leukemia virus |
| BLV protease | - |
bovine leukemia virus |
| bovine leukemia virus retropepsin | - |
bovine leukemia virus |
| More | the enzyme belongs to the A2 peptidase family | bovine leukemia virus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
bovine leukemia virus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
80 | active range | bovine leukemia virus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6 | - |
bovine leukemia virus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 7.5 | active range | bovine leukemia virus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6.5 | the purified enzyme is more stable at pH 5.0 than at pH 6.5 due to the reduced autolytic activity at the C-terminus | bovine leukemia virus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| bovine leukemia virus | - |
- |
10.2 |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.0005 | - |
strong inhibition, IC50: 0.0005 mM | bovine leukemia virus | YDPPAI-statine-II | |
| 0.015 | - |
IC50: 0.015 mM | bovine leukemia virus | Ac-Pro-Glu-Val-Leu-pipecolic acid-Val-Met | |
| 0.1 | - |
IC50: 0.10 mM | bovine leukemia virus | Pro-Glu-Val-statine-Ala-Leu | |
| 0.1 | - |
IC50: 0.10 mM | bovine leukemia virus | Gly-Val-Leu-Tyr-statine-Glu-Ala | |
| 0.25 | - |
IC50: 0.250 mM | bovine leukemia virus | Ac-Pro-Glu-Val-Leu-azetidine-Val-Met | |
| 0.3 | 0.5 | IC50: 0.3-0.5 mM | bovine leukemia virus | pepstatin A | |
| 5 | - |
IC50: 5 mM | bovine leukemia virus | cerulenin | |
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