1.20.4.3: mycoredoxin
This is an abbreviated version!
For detailed information about mycoredoxin, go to the full flat file.
Word Map on EC 1.20.4.3
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1.20.4.3
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mycobacterium
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corynebacterium
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tuberculosis
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thioredoxin
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glutamicum
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sigh
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stress-responsive
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sulfenic
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s-mycothiolated
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extracytoplasmic
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trx
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monothiolic
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glutaredoxins
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dithiolic
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msras
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thienopyrimidine
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peroxidatic
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mtahpe
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non-replicating
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antitubercular
- 1.20.4.3
- mycobacterium
- corynebacterium
- tuberculosis
- thioredoxin
- glutamicum
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sigh
-
stress-responsive
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sulfenic
-
s-mycothiolated
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extracytoplasmic
- trx
-
monothiolic
- glutaredoxins
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dithiolic
- msras
-
thienopyrimidine
-
peroxidatic
-
mtahpe
-
non-replicating
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antitubercular
Reaction
Synonyms
glutaredoxin A1, Mrx-1, Mrx1, Mrx2, MrxI, mycoredoxin, mycoredoxin 1, mycoredoxin-1, mycoredoxin-2, mycothiol-dependent reductase, Rv2466c, Strop1447
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Substrates Products
Substrates Products on EC 1.20.4.3 - mycoredoxin
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REACTION DIAGRAM
arsenite + mycothiol-mycoredoxin disulfide
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a second mycothiol recycles mycoredoxin and forms mycothione
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arseno-mycothiol + mycoredoxin
arsenite + mycothiol-mycoredoxin disulfide
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reduction of arsenate is part of a defense mechanism of the cell against toxic arsenate. The substrate arseno-mycothiol is formed by arsenate-mycothiol transferase. A second mycothiol recycles mycoredoxin and forms mycothione
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the enzyme reduces the sulfenic acid intermediate via the formation of an S-mycothiolated methionine sulfoxide reductase A intermediate which is then recycled by mycoredoxin and the second molecule of mycothiol
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additional information
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the enzyme serve as reducing power for mycothiol peroxidase
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additional information
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the enzyme directly reduces the oxidized form of alkyl hydroxyperoxide reductase E, through a protein mixed disulfide with the N-terminal cysteine of mycoredoxin-1 and the sulfenic acid derivative of the peroxidatic cysteine of alkyl hydroxyperoxide reductase E
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additional information
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the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
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additional information
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the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
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additional information
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the enzyme receives electrons through the mycothiol/mycothione reductase/NADPH pathway to activate TP053, preferentially via a dithiol-disulfide mechanism. The enzyme uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides. The enzyme has no oxidase properties
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additional information
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isoform mycoredoxin-1 acts as an oxidoreductase exclusively linked to the mycothiol electron transfer pathway and can reduce S-mycothiolated mixed disulfides. Mycoredoxin-1 has a redox potential of -218 mV and hydrogen bonding with neighbouring residues lowers the pKa of its N-terminal nucleophilic cysteine
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