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Literature summary for 1.18.6.1 extracted from
- Nitrogenase in the archaebacterium Methanosarcina barkeri 227 (1990), J. Bacteriol., 172, 6789-6796.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the nitrogenase activity is resolved into two components. The component 1 has a molecular size of approximately 250 kDa, as estimated by gel filtration, and sodium dodecyl sulfate-polyacrylamide gels reveals two predominant bands with molecular sizes near 57000 and 62000 Da, consistent with an alpha2beta2 tetramer as in eubacterial component 1 proteins. For the component 2 a molecular size of approximately 120000 Da is estimated by gel filtration, with a subunit molecular size near 31000 Da, indicating that the component 2 protein is a tetramer | Methanosarcina barkeri |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | - |
- |
- |
| Methanosarcina barkeri 227 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanosarcina barkeri |
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