1.8.98.2: sulfiredoxin
This is an abbreviated version!
For detailed information about sulfiredoxin, go to the full flat file.

Word Map on EC 1.8.98.2
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1.8.98.2
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peroxiredoxins
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hyperoxidation
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thioredoxins
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overoxidized
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sulfenic
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peroxidatic
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txnrd1
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sulfinylated
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deglutathionylation
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prxiii
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prdxs
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cys-so2h
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medicine
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drug development
- 1.8.98.2
- peroxiredoxins
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hyperoxidation
- thioredoxins
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overoxidized
-
sulfenic
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peroxidatic
- txnrd1
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sulfinylated
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deglutathionylation
-
prxiii
-
prdxs
-
cys-so2h
- medicine
- drug development
Reaction
Synonyms
AtSrx, cysteine-sulfinic acid reductase, neoplastic progression 3, peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase, protein cysteine sulfinic acid reductase, Srx, Srx1, Srxn1, sulfiredoxin, sulfiredoxin 1, sulfiredoxin-1, sulphiredoxin
ECTree
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Results
in table
1
1793
17
50
26
54
Localization
Localization on EC 1.8.98.2 - sulfiredoxin
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colocalization of Srx and TXNDC5 in endoplasmic reticulum of cultured cells

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Srx possesses a chloroplast transit peptide in the N-terminus

residues 1-22 of AtSrx are predicted as a chloroplast-targeting transit peptide

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Srx possesses a chloroplast transit peptide in the N-terminus
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cytosolic Srx is translocated into the mitochondria under oxidative conditions

dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting. In mitochondria, enzyme interacts with peroxiredoxin IIF and thioredoxin. Sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent

dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting. In mitochondria, enzyme interacts with peroxiredoxin IIF and thioredon. Sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent

dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting

dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting
