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Literature summary for 3.4.21.91 extracted from
- Structural platform for the autolytic activity of an intact NS2B-NS3 protease complex from dengue virus (2012), Biochemistry, 51, 2840-2851.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| protocol for the preparation of the full-length NS2B/NS3 complex from dengue serotype 2 virus by utilizing a Mistic-fusion expression cassette in Escherichia coli | Dengue virus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G148A | mutant exhibits impaired autolytic activity | Dengue virus |
| K26A | mutant exhibits impaired autolytic activity | Dengue virus |
| additional information | random mutagenesis study. Among 103 clones, 58 represent functionally inactive mutants. All tested alanine-substituted mutants exhibit impaired autolytic activity | Dengue virus |
| S135A | inactive | Dengue virus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Dengue virus | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dengue virus | - |
type 2 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| protocol for the preparation of the full-length NS2B/NS3 complex from dengue serotype 2 virus by utilizing a Mistic-fusion expression cassette in Escherichia coli. The protease complex is successfully solubilized and stabilized from the bacterial membrane and purified with the use of foscholine-14 detergent. The detergent-solubilized protease complex retains autolytic activity and exists as a robust trimer, implying a molecular assembly in the membrane | Dengue virus |
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