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Literature summary extracted from
- Zn2+-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation (2009), Proteins, 74, 222-239.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.5 | Ni2+ | required for activity | Helicobacter pylori |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.5 | Helicobacter pylori | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.5 | urease | - |
Helicobacter pylori |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.5 | physiological function | the biosynthesis of the active metal-bound form of the nickel-dependent enzyme urease involves the formation of a lysine-carbamate functional group concomitantly with the delivery of two Ni2+- ions into the precast active site of the apoenzyme and with GTP hydrolysis. In the urease system, this role is performed by UreG, an accessory protein belonging to the group of homologous P-loop GTPases | Helicobacter pylori |
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