1.11.1.29: mycoredoxin-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about mycoredoxin-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.29
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1.11.1.29
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peroxiredoxins
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tuberculosis
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mtahpe
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sulfenic
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peroxidatic
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pka
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overoxidation
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peroxynitrite
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sulfur
- 1.11.1.29
- peroxiredoxins
- tuberculosis
-
mtahpe
-
sulfenic
-
peroxidatic
- pka
-
overoxidation
- peroxynitrite
- sulfur
Reaction
Synonyms
AhpE, alkyl hydroperoxide reductase E, alkyl hydroxyperoxide reductase E, EC 1.11.1.15, mycothiol/mycoredoxin-1-dependent peroxidase, peroxiredoxin AhpE, Rv2238c
ECTree
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Systematic Name
Systematic Name on EC 1.11.1.29 - mycoredoxin-dependent peroxiredoxin
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mycoredoxin:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [1]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Mycoredoxin-dependent enzymes are found in Mycobacteria. Following the reduction of the substrate, the sulfenic acid derivative of the peroxidatic cysteine forms a protein mixed disulfide with the N-terminal cysteine of mycoredoxin, which is then reduced by the C-terminal cysteine of mycoredoxin, restoring the peroxiredoxin to active state and resulting in an intra-protein disulfide in mycoredoxin. The disulfide is eventually reduced by mycothiol.