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Literature summary for 1.11.1.29 extracted from

  • Hugo, M.; Van Laer, K.; Reyes, A.; Vertommen, D.; Messens, J.; Radi, R.; Trujillo, M.
    Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis (2014), J. Biol. Chem., 289, 5228-5239 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) as a recombinant His-tagged protein Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Mycobacterium tuberculosis 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
mycoredoxin-1 + ROOH Mycobacterium tuberculosis mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE mycoredoxin-1 disulfide + H2O + ROH
-
?
mycoredoxin-1 + ROOH Mycobacterium tuberculosis ATCC 25618 mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE mycoredoxin-1 disulfide + H2O + ROH
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIE3
-
-
Mycobacterium tuberculosis ATCC 25618 P9WIE3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mycoredoxin-1 + H2O2 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 Mycobacterium tuberculosis mycoredoxin-1 disulfide + 2 H2O
-
?
mycoredoxin-1 + H2O2 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 Mycobacterium tuberculosis ATCC 25618 mycoredoxin-1 disulfide + 2 H2O
-
?
mycoredoxin-1 + ROOH mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE Mycobacterium tuberculosis mycoredoxin-1 disulfide + H2O + ROH
-
?
mycoredoxin-1 + ROOH mycoredoxin-1 (MtMrx1) acts in combination with mycothiol and mycothiol disulfide reductase, is a biologically relevant reducing system for MtAhpE Mycobacterium tuberculosis ATCC 25618 mycoredoxin-1 disulfide + H2O + ROH
-
?

Synonyms

Synonyms Comment Organism
alkyl hydroxyperoxide reductase E
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Mycobacterium tuberculosis
mycothiol/mycoredoxin-1-dependent peroxidase
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Mycobacterium tuberculosis
peroxiredoxin AhpE
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Mycobacterium tuberculosis
Rv2238c
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Mycobacterium tuberculosis