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Literature summary for 3.2.2.24 extracted from
- Characterization of the interaction of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum with bacterial membranes (1999), Arch. Microbiol., 172, 51-58.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | GTP may be involved in regulation of enzyme by controlling the extent of enzyme association with the membrane | Rhodospirillum rubrum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | associated to membrane. Purified enzyme reversibly binds to bacterial pellet fractions requiring a protein component in the membrane. Guanosine and uridine tri- and di-nucleotides specifically dissociate enzyme from membrane fractions | Rhodospirillum rubrum | 16020 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodospirillum rubrum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rhodospirillum rubrum |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | purified enzyme reversibly binds to bacterial pellet fractions, dissociation is mediated by guanosine and uridine tri- and di-nucleotides | Rhodospirillum rubrum |
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