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Literature summary for 7.1.2.2 extracted from
- Dependence on the F0F1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases 1 and 2 during glucose and glycerol fermentation at high and low pH in Escherichia coli (2011), J. Bioenerg. Biomembr., 43, 645-650.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
several strains | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| F0F1-ATP synthase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | Escherichia coli FoF1-ATP synthase atp mutant strain DK8 lacks hydrogenase activity during fermentative growth on glucose at pH 7.0, while at pH 5.5 hydrogenase activity is only 20% that of the wild-type | Escherichia coli |
| physiological function | FoF1-ATP synthase is the main membrane protein complex of bioenergetic relevance catalyzing ATP synthesis as terminal step in oxidative phosphorylation. Requirement for the FoF1-ATP synthase for the activities of the hydrogen-oxidizing hydrogenases Hyd-1 and Hyd-2 | Escherichia coli |
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Release 2023.1 (January 2023)
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