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Literature summary for 3.4.21.115 extracted from
- Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction (2007), J. Biol. Chem., 282, 24928-24937.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Tuner (DE3) cells using the pET-24a vector, two recombinant constructs generated by site-directed mutagenesis of the IPNV VP4 protease analyzed | infectious pancreatic necrosis virus |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| two crystal structures of the IPNV VP4 protease solved from two different crystal symmetries, refinement to 2.2 A resolution reveals the acyl-enzyme complex formed with an internal VP4 cleavage site, substrate binding pockets S1, S3, S5, and S6 identified, conserved overall structure of VP4 determined by three-dimensional alignments | infectious pancreatic necrosis virus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K674A | two recombinant constructs VP4_524-716-K674A and VP4_514-716-K674A generated by site-directed mutagenesis | infectious pancreatic necrosis virus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 20500 | - |
recombinant protein VP4_524-716-K674A (VP4hex), 194 residues long, theoretical isoelectric point of 4.3 estimated | infectious pancreatic necrosis virus |
| 21700 | - |
recombinant protein VP4_514-716-K674A (VP4tri), 204 residues long, theoretical isoelectric point of4.5 estimated | infectious pancreatic necrosis virus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| infectious pancreatic necrosis virus | Q703G9 | IPNV, Aquabirnavirus | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | large polyprotein NH2-pVP2-VP4-VP3-COOH processed through its own protease, VP4 required to release the proteins pVP2 and VP3 | infectious pancreatic necrosis virus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| gel filtration, native and recombinant proteins | infectious pancreatic necrosis virus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
first identification of an acyl-enzyme complex for a Ser/Lys dyad protease, catalytic mechanism and substrate recognition indicated | infectious pancreatic necrosis virus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | acyl-enzyme complex for intermolecular self-cleavage reaction determined by crystallization, conserved overall structure of VP4 determined despite of only 20% sequence identity between different VP4 proteins | infectious pancreatic necrosis virus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| infectious pancreatic necrosis birnavirus Vp4 protease | - |
infectious pancreatic necrosis virus |
| VP4 | - |
infectious pancreatic necrosis virus |
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