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Literature summary for 1.7.2.4 extracted from
- Structural studies of Apo NosL, an accessory protein of the nitrous oxide reductase system: insights from structural homology with MerB, a mercury resistance protein (2006), Biochemistry, 45, 12240-12252.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Achromobacter cycloclastes |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu | Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase | Achromobacter cycloclastes |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Achromobacter cycloclastes | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DEAE-FF ion exchange chromatography and Resource Q column chromatography | Achromobacter cycloclastes |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| N2OR | - |
Achromobacter cycloclastes |
| nitrous oxide reductase | - |
Achromobacter cycloclastes |
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Release 2023.1 (January 2023)
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