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Literature summary for 2.7.7.2 extracted from
- Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes (2009), Acta Crystallogr. Sect. F, 65, 1285-1288.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 (DE3), a SeMet-version is generated | Corynebacterium ammoniagenes |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapor-diffusion method, 277 K | Corynebacterium ammoniagenes |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 37120 | - |
electrospray mass spectrometry, Se-Met-enzyme, 36843.5 is the theoretical value for the native protein | Corynebacterium ammoniagenes |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium ammoniagenes | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate fractionation, Phenyl-Sepharose chromatography, DEAE-Cellulose chromatography | Corynebacterium ammoniagenes |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FAD synthetase | bifunctional enzyme: riboflavin kinase | Corynebacterium ammoniagenes |
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