Any feedback?
Literature summary for 2.7.2.4 extracted from
- Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulatory domain of aspartokinase (Rv3709c) from Mycobacterium tuberculosis (2011), Acta Crystallogr. Sect. F, 67, 380-385.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Mycobacterium tuberculosis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| regulatory domain (AK-beta) in the presence of the potential feedback inhibitor threonine is crystallized to 1.6 A resolution. Crystal form belongs to space group P2-1-2-12-1, with unit-cell parameters a = 53.70, b = 63.43, c = 108.85 A and two molecules per asymmetric unit | Mycobacterium tuberculosis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| threonine | - |
Mycobacterium tuberculosis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Mycobacterium tuberculosis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| aspartokinase | - |
Mycobacterium tuberculosis |
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