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Literature summary for 3.4.22.44 extracted from
- Functional regulation of PVBV nuclear inclusion protein-a protease activity upon interaction with viral protein genome-linked and phosphorylation (2012), Virology, 422, 254-264.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| co-expression of NIa-Pro and Vg-Pro in Escherichia coli | Chilli veinal mottle virus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C151A | site-directed mutagenesis, a NIa-Pro active site mutant | Chilli veinal mottle virus |
| E191A | site-directed mutagenesis, a VPg-Pro mutant | Chilli veinal mottle virus |
| S129A | site-directed mutagenesis, a NIa-Pro phosphorylation-deficient mutant | Chilli veinal mottle virus |
| S129D | site-directed mutagenesis, a NIa-Pro phosphorylation-mimic mnutant | Chilli veinal mottle virus |
| W143A | site-directed mutagenesis, the NIa-Pro W143A mutant can bind the substrate with almost equal affinity as that of the wild-type protease, although its ability to catalyze the cleavage reaction is highly reduced | Chilli veinal mottle virus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.05 | - |
WDGGEVAHQAGESV | recombinant S129D NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus |  |
| 0.06 | - |
WDGGEVAHQAGESV | recombinant S129A NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.15 | - |
WDGGEVAHQAGESV | recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.44 | - |
WDGGEVAHQAGESV | recombinant wild-type NIa-Pro, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.45 | - |
WDGGEVAHQAGESV | recombinant E191A VPg-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.69 | - |
WDGGEVAHQAGESV | recombinant W143A NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 1.67 | - |
WDGGEVAHQAGESV | recombinant VPg-Pro, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 11.4 | - |
WDGGEVAHQAGESV | recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C | Chilli veinal mottle virus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Chilli veinal mottle virus | interaction between purified recombinant NIa-Pro and VPg domains, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chilli veinal mottle virus | - |
PVBV | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | the protease activity of NIa-Pro can be modulated by phosphorylation at Ser129 | Chilli veinal mottle virus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | interaction between purified recombinant NIa-Pro and VPg domains, overview | Chilli veinal mottle virus | ? | - |
? | |
| WDGGEVAHQAGESV + H2O | - |
Chilli veinal mottle virus | WDGGEVAHQ + AGESV | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NIa-Pro | - |
Chilli veinal mottle virus |
| nuclear inclusion protein-a protease | - |
Chilli veinal mottle virus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Chilli veinal mottle virus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.002 | - |
WDGGEVAHQAGESV | recombinant W143A NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.004 | - |
WDGGEVAHQAGESV | recombinant S129D NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.005 | - |
WDGGEVAHQAGESV | recombinant S129A NIa-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.006 | - |
WDGGEVAHQAGESV | recombinant S129D NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.01 | - |
WDGGEVAHQAGESV | recombinant W143A NIa-Pro mutant in presence of the VPg domain, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.034 | - |
WDGGEVAHQAGESV | recombinant wild-type NIa-Pro, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.063 | - |
WDGGEVAHQAGESV | recombinant E191A VPg-Pro mutant, pH 8.5, 25°C | Chilli veinal mottle virus | |
| 0.23 | - |
WDGGEVAHQAGESV | recombinant VPg-Pro, pH 8.5, 25°C | Chilli veinal mottle virus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Chilli veinal mottle virus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the full-length potyviral genome protease, VPg-Pro, has two domains: an N-terminal viral protein genome-linked, VPg, and a C-terminal protease NIa-Pro. Regulation of nuclear inclusion protein-a protease is crucial for polyprotein processing and hence, for successful infection by potyviruses, mechanisms regulating nuclear inclusion protein-a protease activity. Firstly, the influence of the VPg domain on the proteolytic activity of NIa-Pro increases when the two domains interact each other. Secondly, the protease activity of NIa-Pro can also be modulated by phosphorylation at Ser129. interaction with VPg as well as phosphorylation of Ser129 relays a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro, molecular modeling, homology modeling, and molecular dynamics simulations, overview | Chilli veinal mottle virus |
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