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Literature summary for 3.4.21.19 extracted from
- The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus (2004), Acta Crystallogr. Sect. D, 60, 256-259.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 7 mg/ml purified enzyme in 50 mM HEPES, pH 8.6, 50 mM KCl, 15% PEG 500 monomethylester, hanging drop method over a reservoir solution containing 0.1 M KCl, 0.1 M HEPES, and 20% PEG 5000 monomethyl ester, 293 K, X-ray diffraction structure determination and analysis at 1.9 A resolution | Staphylococcus aureus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Staphylococcus aureus | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
enzyme belongs to the pancreatic serine proteases, but possesses no disulfide bridges | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Preferential cleavage: Glu-/-, Asp-/- | absolutely specific for cleavage sites Glu-/-Xaa and Asp-/-Xaa, cleavage exclusively at the carboxylic side, active site Ser169 | Staphylococcus aureus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the positively charged N-terminus is involved in determination of substrate specificity | Staphylococcus aureus | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| V8 protease | - |
Staphylococcus aureus |
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