Information on EC 1.8.98.2 - sulfiredoxin

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.8.98.2
-
RECOMMENDED NAME
GeneOntology No.
sulfiredoxin
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
reduction
-
ATP-dependent reduction of cysteinesulfinic acid of hyperoxidized peroxiredoxin
reduction
-
reduction of hyperoxidized 2-Cys peroxiredoxin
reduction
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtSrx
Q8GY89
-
cysteine-sulfinic acid reductase
-
-
neoplastic progression 3
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
-
-
protein cysteine sulfinic acid reductase
-
-
Srx
Arabidopsis thaliana Columbia
-
-
-
Srx
D2KKL9
-
Srx1
-
-
sulfiredoxin
Q8GY89
-
sulfiredoxin
D2KKL9
-
sulfiredoxin
-
-
sulfiredoxin 1
-
-
sulfiredoxin-1
-
-
sulphiredoxin
-
-
sulphiredoxin
-
-
CAS REGISTRY NUMBER
COMMENTARY
710319-61-2
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Q9D975
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
Arabidopsis thaliana Columbia
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
overoxidized human peroxiredoxin V + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
Q8GY89
Arabidopsis enzyme is able to reduce overoxidized human Prx V
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 DTT
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + DTT disulfide
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Columbia
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Columbia
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
r
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-, Q8GY89
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
Q8GY89
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q9BYN0
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
show the reaction diagram
-
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
show the reaction diagram
Arabidopsis thaliana, Arabidopsis thaliana Columbia
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
show the reaction diagram
-
-
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + GSSG
show the reaction diagram
-
identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-, Q8GY89
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + GTP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + GDP + phosphate + R-S-S-R
show the reaction diagram
-
both glutathione and thioredoxin are potential physiological electron donors
-
-
?
sulfinic form of peroxiredoxin IIF + oxidized thioredoxin
? + reduced thioredoxin
show the reaction diagram
D2KKL9, -
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
show the reaction diagram
Q8GY89
in mitochondria, sulfiredoxin catalyzes the retroreduction of the inactive sulfinic form of atypical peroxiredoxin IIF using thioredoxin as reducing agent
-
-
?
additional information
?
-
-
no activity with CTP, UTP, dCTP, or dTTP
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
additional information
?
-
-
catalyzes the deglutathionylation of actin
-
-
-
additional information
?
-
-
promotes the reversal of cysteine modified PTP1B to its reduced and enzymatically active form, reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress
-
-
-
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
?
-
Arabidopsis thaliana Columbia
-
assay conditions optimization, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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 + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
-, Q8GY89
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
-
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
siRNA
-
-
-
additional information
-
screening for Srx inhibitors is carried out in an automated setup using 25000 chemicals
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
ATP
-
-
0.125
-
ATP
-
pH 7.0, 30°C
0.13
-
gamma-S-ATP
-
pH 7.0, 30°C
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
0.0012
-
thioredoxin 1
-
-
1.8
-
GSH
-
-
additional information
-
additional information
-
kinetic analysis, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
ATP
-
wild-type, pH 7.0, 30°C
0.016
-
gamma-S-ATP
-
wild-type, pH 7.0, 30°C
0.00042
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, saturating ATP, 0.03 mM Srx, 0.04 mM substrate
0.003
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
at 30°C
0.011
-
peroxiredoxin-(S-hydroxy-S-oxocysteine)
-
pH 7.5, 30°C, 1 mM ATP, 0.03 mM Srx, saturating substrate concentration
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
malachite green assay at room temperature
30
-
-
kinetic assay
30
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9.86
-
-
mature enzyme, sequence calculation
10.76
-
-, Q8GY89
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia
-
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Srx possesses a chloroplast transit peptide in the N-terminus
Manually annotated by BRENDA team
Arabidopsis thaliana Columbia
-
Srx possesses a chloroplast transit peptide in the N-terminus
-
Manually annotated by BRENDA team
-
cytosolic Srx is translocated into the mitochondria under oxidative conditions
Manually annotated by BRENDA team
Q8GY89
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
Manually annotated by BRENDA team
D2KKL9, -
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
Manually annotated by BRENDA team
Q8GY89
dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting
Manually annotated by BRENDA team
D2KKL9, -
dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12000
-
-
SDS-PAGE
13910
-
-, Q8GY89
-
14000
-
-
-
15000
-
-
Srx monomer, determined by SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
?
Arabidopsis thaliana Columbia
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type Srx and mutants to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
His-Srx proteins are purified from cell lysates by chromatography on a column on Ni-chelating Sepharose
-
Ni2+-NTA column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q8GY89
expression in Escherichia coli
-
transient expression of an AtSrx-GFP fusion in Nicotiana tabacum leaves
-, Q8GY89
expressed in HEK293 cells and Escherichia coli
-
expression in Escherichia coli
-
for expression in Escherichia coli BL21DE3 cells
-
into the vector pcDNA3
-
into the vector pET14b for expression in Escherichia coli BL21 cells
-
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
-
expression in Escherichia coli
-
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
R28Q/E76A
-
site-directed mutagenesis, inactive mutant
C72S
Arabidopsis thaliana Columbia
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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R28Q
Arabidopsis thaliana Columbia
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
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R28Q/E76A
Arabidopsis thaliana Columbia
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site-directed mutagenesis, inactive mutant
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C99A
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Cys99 replaced by Ala
C99S
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mutant created to show the importance of the cytosine residue in the deglutathionylation function of the protein
C99S
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Cys99 replaced by Ser
C99S
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mutant, substitution of serine for Cys99 blocks the release of phosphate
C99S
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catalytic cysteine mutant
D57N
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Asp57 replaced by Asn
D79N
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Asp60 replaced by Asn
H100N
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Srx mutant
H99N
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His99 replaced by Asn
K60R
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Lys60 replaced by Arg
R100M
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Arg100 replaced by Met
R101M
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Srx mutant
R50M
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Arg50 replaced by Met
Y92R
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Srx mutant
C106A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C48A/C106A
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mutant, constructed to address questions regarding the catalytic mechanisms and the role of the cysteine residues
C84S
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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
K40Q
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site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
additional information
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construction of a Srx knockout mutant, phenotype, overview
E76A
Arabidopsis thaliana Columbia
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
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additional information
Arabidopsis thaliana Columbia
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construction of a Srx knockout mutant, phenotype, overview
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
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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
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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
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increased sulfiredoxin has been linked with oncogenic transformation, data support a role for Srx in controlling the phosphorylation status of key regulatory kinases
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