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Literature summary for 1.11.1.28 extracted from

  • Su, T.; Si, M.; Zhao, Y.; Yao, S.; Che, C.; Liu, Y.; Chen, C.
    Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in Corynebacterium glutamicum (2019), J. Gen. Appl. Microbiol., 65, 72-79 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NMX8
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Corynebacterium glutamicum Q8NN44
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Corynebacterium glutamicum ATCC 13032 Q8NMX8
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Corynebacterium glutamicum ATCC 13032 Q8NN44
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Substrates and Products (Substrate)

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 ?
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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

Synonyms Comment Organism
ahpD1
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Corynebacterium glutamicum
ahpD2
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Corynebacterium glutamicum

Expression

Organism Comment Expression
Corynebacterium glutamicum induced under various stresses up

General Information

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