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Literature summary extracted from
- Aconitase functions as a pleiotropic posttranscriptional regulator in Helicobacter pylori (2015), J. Bacteriol., 197, 3076-3086 .
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.3 | Helicobacter pylori | A0A2X5AHR8 | - |
- |
| 4.2.1.3 | Helicobacter pylori ATCC 43504 | A0A2X5AHR8 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.3 | AcnB | - |
Helicobacter pylori |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.1.3 | physiological function | apo-AcnB is able to bind to RNA transcripts of hpn encoding a nickel-sequestering protein, ahpC encoding alkyl hydroperoxide reductase, and flgR encoding flagellum response regulator. Compared to the wild-type, the AcnB mutant strain has decreased activities of the nickel-containing enzymes urease and hydrogenase, and lower total nickel levels within the cells. Binding of apo-AcnB to the hpn 5' untranslated region may inhibit the expression of Hpn. AcnB mutant cells display oxidative-stress-sensitive phenotypes and have a lesser motility ability than the wild-type strain | Helicobacter pylori |
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