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
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sulfenic
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peroxidatic
- 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
- 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
1.8.98.2 sulfiredoxinAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.8.98.2 - sulfiredoxin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Cys peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
2-Cys peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
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?
overoxidized human peroxiredoxin V + reduced thioredoxin
? + oxidized thioredoxin
Arabidopsis enzyme is able to reduce overoxidized human Prx V
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?
peroxiredoxin IIF-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin IIF-(S-hydroxycysteine) + ADP + phosphate + GSSG
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-
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-
?
peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 H2S
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + HS-SH
preference for H2S to support the repair of mitochondrial hyperoxidized Prx3 by Srx. Combined GSH and H2S for the repair of cytosolic Prx2
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
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-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + thioredoxin 1
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin 1 disulfide
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-
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r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
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both glutathione and thioredoxin are potential physiological electron donors
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
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both glutathione and thioredoxin are potential physiological electron donors
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
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formation of a covalent thiosulfinate peroxiredoxin-sulfiredoxin species as an intermediate on the catalytic pathway
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + GTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
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both glutathione and thioredoxin are potential physiological electron donors
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-
?
sulfinic form of peroxiredoxin IIF + oxidized thioredoxin
? + reduced thioredoxin
in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent
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-
?
sulfinic form of peroxiredoxin IIF + reduced thioredoxin
? + oxidized thioredoxin
in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
combined GSH and H2S for the repair of cytosolic Prx2
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
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r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
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r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications. Srx also has a role in the reduction of glutathionylation a post-translational, oxidative modification that occurs on numerous proteins and has been implicated in a wide variety of pathologies, including Parkinsons disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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both glutathione and thioredoxin are potential physiological electron donors
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
the ATP molecule is cleaved between the beta- and gamma-phosphate groups
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
hyperoxidized Prx1
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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reduction of Cys-SO2H by Srx is specific to 2-Cys peroxiredoxin isoforms. For proteins such as Prx VI and GAPDH, sulfinic acid formation might be an irreversible process that causes protein damage
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
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-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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-
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-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteinesulphinic acid modifications, and in signalling pathways involving protein oxidation
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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the rate-limiting step of the reaction is associated with the chemical process of transfer of the gamma-phosphate of ATP to the sulfinic acid. Two pKapp values of 6.2 and 7.5 of the bell-shaped pH-rate profile correspond to the gamma-phosphate of ATP, and to an acid-base catalyst, respectively
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
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-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
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-
-
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
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?
additional information
?
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assay conditions optimization, overview
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?
additional information
?
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enzyme is able to act as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme. Sulfiredoxin functions as a nuclease enzyme that can use single-stranded and double-stranded DNAs as substrates. The active site of the reductase function of sulfiredoxin is not involved in its nuclease function
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?
additional information
?
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AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo
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additional information
?
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AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo
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additional information
?
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AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo. Overall structure of ADP-bound AtSrx, ADP is bound at a positive charged pocket of AtSrx, detailed overview. AtSrx forms a complex with AtPrxA in vitro, modeling
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additional information
?
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AtSrx has sulfinic acid reductase activity to catalyze the reduction of the overoxidized form of 2-Cys Prx in vitro and in vivo. Overall structure of ADP-bound AtSrx, ADP is bound at a positive charged pocket of AtSrx, detailed overview. AtSrx forms a complex with AtPrxA in vitro, modeling
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additional information
?
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assay conditions optimization, overview
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?
additional information
?
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catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
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?
additional information
?
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promotes the reversal of cysteine modified PTP1B to its reduced and enzymatically active form
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?
additional information
?
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reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress
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?
additional information
?
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Srx forms a complex with the endoplasmic reticulum-resident protein thioredoxin domain-containing protein 5 (TXNDC5) in vivo and in vitro. TXNDC5 directly interacts with Srx through its thioredoxin-like domains, mapping of the interacting domains between Srx and TXNDC5, the thioredoxin-like domains 1 and 3 are responsible for the binding to Srx, overview. Deletion of the first or third thioredoxin-like domain in TXNDC5 results in a significant loss of its binding to Srx, whereas deletion of the second (the one in the middle) thioredoxin-like domain does not compromise its binding to Srx. The Srx-TXNDC5 is a relatively stable complex that is not affected by the treatment with exogenous H2O2
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additional information
?
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Srx forms a complex with the endoplasmic reticulum-resident protein thioredoxin domain-containing protein 5 (TXNDC5) in vivo and in vitro. TXNDC5 directly interacts with Srx through its thioredoxin-like domains, mapping of the interacting domains between Srx and TXNDC5, the thioredoxin-like domains 1 and 3 are responsible for the binding to Srx, overview. Deletion of the first or third thioredoxin-like domain in TXNDC5 results in a significant loss of its binding to Srx, whereas deletion of the second (the one in the middle) thioredoxin-like domain does not compromise its binding to Srx. The Srx-TXNDC5 is a relatively stable complex that is not affected by the treatment with exogenous H2O2
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additional information
?
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specificity of human sulfiredoxin for reductant and peroxiredoxin oligomeric state, overview. The resolution of the Prx-Srx complex involves the reduction of the thiosulfinate intermediate (Prx-CP-S=O-S-Srx) to yield the Prx Cys-sulfenic acid intermediate (Prx-CP-SOH). Yeast Srx contains an adjacent resolving Cys residue (Cys-SR) that can react with the thiosulfinate intermediate leading to the formation of an Srx intramolecular disulfide (Srx-(S-S)). In contrast, human Srx has only one Cys residue and requires an exogenous reductant. Possible reductants include the Trx system (Trx/TrxR/NADPH), glutathione (GSH) and hydrogen sulfide (H2S), these reductants would ultimately yield reduced Srx (Srx-SH). Enzyme-substrate binding studies with mutant Prx1 (e.g. Prx1 C83V and Prx1 C71S/C173S). Repair of hyperoxidized Prx2, Prx3 and their chimeras, the C-terminal sequence differences between Prx2 and Prx3 impact the rate of repair by Srx
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additional information
?
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specificity of human sulfiredoxin for reductant and peroxiredoxin oligomeric state, overview. The resolution of the Prx-Srx complex involves the reduction of the thiosulfinate intermediate (Prx-CP-S=O-S-Srx) to yield the Prx Cys-sulfenic acid intermediate (Prx-CP-SOH). Yeast Srx contains an adjacent resolving Cys residue (Cys-SR) that can react with the thiosulfinate intermediate leading to the formation of an Srx intramolecular disulfide (Srx-(S-S)). In contrast, human Srx has only one Cys residue and requires an exogenous reductant. Possible reductants include the Trx system (Trx/TrxR/NADPH), glutathione (GSH) and hydrogen sulfide (H2S), these reductants would ultimately yield reduced Srx (Srx-SH). Enzyme-substrate binding studies with mutant Prx1 (e.g. Prx1 C83V and Prx1 C71S/C173S). Repair of hyperoxidized Prx2, Prx3 and their chimeras, the C-terminal sequence differences between Prx2 and Prx3 impact the rate of repair by Srx
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additional information
?
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Srx transfers the gamma-phosphate of ATP to Cp sulfinic acid on hyperoxidized Prxs and produces sulfinic phosphoryl ester. Subsequent involvement of GSH and thioredoxin will ensure the reduction of sulfinic phosphoryl ester to sulfenic acid
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additional information
?
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Srx transfers the gamma-phosphate of ATP to Cp sulfinic acid on hyperoxidized Prxs and produces sulfinic phosphoryl ester. Subsequent involvement of GSH and thioredoxin will ensure the reduction of sulfinic phosphoryl ester to sulfenic acid
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additional information
?
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catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
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?
