HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.8.98.2 - sulfiredoxin
for references in articles please use BRENDA:EC1.8.98.2
Word Map on EC 1.8.98.2
- 1.8.98.2
- peroxiredoxins
-
hyperoxidized
- thioredoxins
-
overoxidized
-
peroxidatic
-
sulfinylated
-
2-related
-
prxiii
-
peroxide-mediated
-
cys-so2h
-
prdxs
- thiosulfinate
-
deglutathionylation
- medicine
- drug development
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.8.98.2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
sulfiredoxin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
reduction
-
ATP-dependent reduction of cysteinesulfinic acid of hyperoxidized peroxiredoxin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. Apparently the reductase first catalyses the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes. Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
710319-61-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfinic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx and the conserved Srx is capable of regenerating the functionality of both pea and Arabidopsis Prx-SO2H
physiological function
-
sulfiredoxin Srx1 reactivates the yeast peroxiredoxin Prx1 peroxidase activity that is inactivated by H2O2, whereas it decreases the chaperone activity enhanced by H2O2. Srx1 dissociates the H2O2-induced high molecular weight Prx1 complex, and the Srx1 Cys84 residue is critical for its dissociation
physiological function
exposure of low steady-state levels ofH2O2 to A-549 or wild-type mouse embryonic fibroblast cells does not lead to any significant change in oxidative injury. Loss-of-function studies using sulfiredoxin-depleted A549 and sulfiredoxin -/- cells demonstrate a dramatic increase in extra- and intracellular H2O2, sulfinic 2-Cys peroxiredoxins, and apoptosis. Concomitant with hyperoxidation of mitochondrial peroxiredoxin Prx III, sulfiredoxin-depleted cells show an activation of mitochondria-mediated apoptotic pathways including mitochondria membrane potential collapse, cytochrome c release, and caspase activation
physiological function
-
enzyme induction is the pivotal compensatory protection mechanism against oxidative stress in diabetes or hyperglycaemia
physiological function
-
mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin
physiological function
-
sulfiredoxin-1 protects PC-12 cells against oxidative stress induced by hydrogen peroxide
physiological function
-
the antioxidant function of 2-Cys peroxiredoxin, Prx, EC 1.11.1.15, involves the oxidation of its conserved peroxidatic cysteine to sulfinic acid that is recycled by a reductor agent. Sulfiredoxin reduces the sulfinic 2-Cys Prx, Prx-SO2H. The activity of sulfiredoxin is dependent on the concentration of the sulfinic form of Prx and the conserved Srx is capable of regenerating the functionality of both pea and Arabidopsis Prx-SO2H
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
?
overoxidized human peroxiredoxin V + reduced thioredoxin
? + oxidized thioredoxin
Arabidopsis enzyme is able to reduce overoxidized human Prx V
-
-
?
peroxiredoxin IIF-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin IIF-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG
-
-
-
-
?
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 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 + GSSG
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dGTP + R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
formation of a covalent thiosulfinate peroxiredoxin-sulfiredoxin species as an intermediate on the catalytic pathway
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + gamma-S-ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + thiophosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + GTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
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
-
-
?
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
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
-
-
-
-
?
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 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
-
-
-
-
?
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 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
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 Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
-
-
?
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
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
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
-
-
?
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 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
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 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
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
-
-
?
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 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
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
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
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 + GSSG
-
-
-
-
-
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
-
-
?
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
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
additional information
?
-
-
assay conditions optimization, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
assay conditions optimization, overview
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
additional information
?
-
-
promotes the reversal of cysteine modified PTP1B to its reduced and enzymatically active form
-
-
-
additional information
?
-
-
reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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 + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
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 Parkinson‘s disease. Unlike the reduction of peroxiredoxin overoxidation, Srx-dependent deglutathionylation appears to be nonspecific
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Q9BYN0
repairs the inactivated forms of typical two-Cys peroxiredoxins implicated in hydrogen peroxide-mediated cell signaling
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
Srx is largely responsible for reduction of the Cys-SO2H of peroxiredoxin in A549 human cells
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
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
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
sulphiredoxin is important for the antioxidant function of peroxiredoxins, and is likely to be involved in the repair of proteins containing cysteine–sulphinic acid modifications, and in signalling pathways involving protein oxidation
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Q8GY89
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
-
-
-
-
?
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
screening for Srx inhibitors is carried out in an automated setup using 25000 chemicals
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis, overview
-
0.029
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
0.079
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00042
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
0.011
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cortical glial cell, in both neurons and glia, Nrf2 expression and treatment with chemopreventive Nrf2 activators, including 3H-1,2-dithiole-3-thione and sulforaphane, upregulate sulfiredoxin, an enzyme responsible for reducing hyperoxidized peroxiredoxins
-
cortical neuron, in both neurons and glia, Nrf2 expression and treatment with chemopreventive Nrf2 activators, including 3H-1,2-dithiole-3-thione and sulforaphane, upregulate sulfiredoxin, an enzyme responsible for reducing hyperoxidized peroxiredoxins
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Srx possesses a chloroplast transit peptide in the N-terminus
-
Srx possesses a chloroplast transit peptide in the N-terminus
-
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11546
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
13914
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
?
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of the wild-type and SeMet forms of ET-hSrx were obtained by the vapor diffusion method. 1.65 A crystal structure of human Srx
-
vapour diffusion method, 2.6 A crystal structure of the sulphiredoxin–peroxiredoxin-I complex
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-Srx proteins are purified from cell lysates by chromatography on a column on Ni-chelating Sepharose
-
recombinant wild-type Srx and mutants to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of N-terminally His6-tagged wild-type Srx and mutants in Escherichia coli strain BL21(DE3)
-
expressed in Saccharomyces cerevisiae
expression in Escherichia coli
the 5' flanking region of the human Srx1 promoter region, -3664 - +19, is ligated into the vector pCR2.1
-
the vectors pcDNA3 and pFLAG-CMV2 are used, a leader sequence is cloned into the N-terminus coding region of Srx
-
transient expression of an AtSrx-GFP fusion in Nicotiana tabacum leaves
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
adrenocortical tumor cell lines show increased enzyme expression. Adrenocorticotropic hormone also induces upregulation of the enzyme with its levels peaking at 3-6 h after injection of adrenocorticotropic hormone
-
disruption of Nrf2 signaling down-regulates the expression of Srx1
Nrf2, nuclear factor erythroid-2-related factor, up-regulates Srx1 expression during oxidative stress caused by cigarette smoke exposure in the lungs
oxidative stress and growth factors can markedly upregulate Srx transcript and protein levels
-
Nrf2, nuclear factor erythroid-2-related factor, up-regulates Srx1 expression during oxidative stress caused by cigarette smoke exposure in the lungs
-
Nrf2, nuclear factor erythroid-2-related factor, up-regulates Srx1 expression during oxidative stress caused by cigarette smoke exposure in the lungs
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C72S
E76A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
K40Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
R28Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C72S
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
E76A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
R28Q
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
C99S
C106A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A/C106A
-
mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C84S
-
Srx1 reactivates the yeast Prx1 peroxidase activity that is inactivated by H2O2. Mutant C84S does not induce the reactivation of inactivated Prx1 or dissociation of the high molecular weight Prx1 complex
additional information
C72S
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
C72S
-
loss of sulfinate reductase activity, no effect on DNA binding and hydrolizing activities
C99S
-
mutant created to show the importance of the cytosine residue in the deglutathionylation function of the protein
additional information
-
construction of a Srx knockout mutant, phenotype, overview
additional information
-
construction of a Srx knockout mutant, phenotype, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
Srx may be a potential target for prevention or treatment of cancer, the colorimetric assay would be useful for high-throughput screening of Srx inhibitors as demonstrated
medicine
medicine
-
oxidative stress results in protein oxidation and is involved in the pathogenesis of lung diseases such as chronic obstructive pulmonary disorder, COPD, in lungs from COPD patients the expression of Srx1 is dramatically decreased
medicine
-
oxidative stress results in protein oxidation and is involved in the pathogenesis of lung diseases such as chronic obstructive pulmonary disorder, COPD, in lungs from COPD patients the expression of Srx1 is dramatically decreased
medicine
-
increased sulfiredoxin has been linked with oncogenic transformation, data support a role for Srx in controlling the phosphorylation status of key regulatory kinases
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.8.98.2)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
