Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | Q8NMX8 | - |
- |
Corynebacterium glutamicum | Q8NN44 | - |
- |
Corynebacterium glutamicum ATCC 13032 | Q8NMX8 | - |
- |
Corynebacterium glutamicum ATCC 13032 | Q8NN44 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD | Corynebacterium glutamicum | ? | - |
- |
|
additional information | AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD | Corynebacterium glutamicum ATCC 13032 | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
ahpD1 | - |
Corynebacterium glutamicum |
ahpD2 | - |
Corynebacterium glutamicum |
Organism | Comment | Expression |
---|---|---|
Corynebacterium glutamicum | induced under various stresses | up |
General Information | Comment | Organism |
---|---|---|
malfunction | DELTAahpD1DELTAahpD2 mutants exhibit significantly decreased resistance to adverse stress conditions and increased accumulation of reactive oxygen species (ROS) | Corynebacterium glutamicum |
physiological function | AhpD acts as a backup of thioredoxin to provide reducing power for peroxidase | Corynebacterium glutamicum |