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Literature summary extracted from
- Structure of Staphylococcus aureus adenylosuccinate lyase (PurB) and assessment of its potential as a target for structure-based inhibitor discovery (2010), Acta Crystallogr. Sect. D, 66, 881-888.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.3.2.2 | in complex with AMP, at 2.5 A resolution, and modeling of oxalate in the active site. Comparisons with the enzyme from Escherichia coli and with human PurB show close similarity of the active sites, but differences in the way that the subunits are assembled into dimers | Staphylococcus aureus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.3.2.2 | 49600 | - |
4 * 49600, calculated. Enzyme forms a dimer of dimers, crystallization data | Staphylococcus aureus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.2.2 | Staphylococcus aureus | Q7A0G9 | - |
- |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.2.2 | tetramer | 4 * 49600, calculated. Enzyme forms a dimer of dimers, crystallization data | Staphylococcus aureus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.2.2 | PurB | - |
Staphylococcus aureus |
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Release 2023.1 (January 2023)
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