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
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mtahpe
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sulfenic
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peroxidatic
- pka
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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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Substrates Products
Substrates Products on EC 1.11.1.29 - mycoredoxin-dependent peroxiredoxin
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REACTION DIAGRAM
mycoredoxin + ROOH
mycoredoxin disulfide + H2O + ROH
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Mycobacteria employ a versatile machinery of the mycothiol-dependent system, containing the proteins mycothiol disulfide reductase, the oxido-reductase Mycoredoxin-1 and the alkyl-hydroperoxide subunit E (AhpE). The mycothiol-dependent protein ensemble regulates the balance of oxidized-reduced mycothiol, to ensure a reductive intracellular environment for optimal functioning of its proteins even upon exposure to oxidative stress. The epitopes of MtMrx-1 and MtAhpE interaction are described
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mycoredoxin + H2O2
mycoredoxin disulfide + 2 H2O
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mycoredoxin + H2O2
mycoredoxin disulfide + H2O
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mycoredoxin-1 + arachidonic acid hydroperoxide
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mycoredoxin-1 disulfide + 2 H2O
mycoredoxin-1 (MtMrx1), a glutaredoxin-like, mycothiol-dependent oxidoreductase, directly reduces the oxidized form of the enzyme (MtAhpE), through a protein mixed disulfide with the N-terminal cysteine of MtMrx1 and the sulfenic acid derivative of the peroxidatic cysteine of MtAhpE. This disulfide is then reduced by the C-terminal cysteine in MtMrx1. Accordingly, MtAhpE catalyzes the oxidation of wild-type MtMrx1 by hydrogen peroxide but not of MtMrx1 lacking the C-terminal cysteine, confirming a dithiolic mechanism
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mycoredoxin-1 + H2O2
mycoredoxin-1 disulfide + 2 H2O
mycoredoxin-1 (MtMrx1), a glutaredoxin-like, mycothiol-dependent oxidoreductase, directly reduces the oxidized form of the enzyme (MtAhpE), through a protein mixed disulfide with the N-terminal cysteine of MtMrx1 and the sulfenic acid derivative of the peroxidatic cysteine of MtAhpE. This disulfide is then reduced by the C-terminal cysteine in MtMrx1. Accordingly, MtAhpE catalyzes the oxidation of wild-type MtMrx1 by hydrogen peroxide but not of MtMrx1 lacking the C-terminal cysteine, confirming a dithiolic mechanism
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mycoredoxin-1 disulfide + H2O + ROH
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mycoredoxin-1 + ROOH
mycoredoxin-1 disulfide + H2O + ROH
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mycoredoxin-1 + ROOH
mycoredoxin-1 disulfide + H2O + ROH
mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE
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mycoredoxin-1 + ROOH
mycoredoxin-1 disulfide + H2O + ROH
mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE
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mycoredoxin-1 + ROOH
mycoredoxin-1 disulfide + H2O + ROH
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mycothiol + ROOH
mycothiol disulfide + H2O + ROH
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