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Information on EC 1.8.98.2 - sulfiredoxin and Organism(s) Arabidopsis thaliana and UniProt Accession Q8GY89

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IUBMB Comments
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.
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Arabidopsis thaliana
UNIPROT: Q8GY89
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
sulfiredoxin, srxn1, sulfiredoxin-1, atsrx, sulfiredoxin 1, sulphiredoxin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cysteine-sulfinic acid reductase
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
710319-61-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
overoxidized human peroxiredoxin V + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
Arabidopsis enzyme is able to reduce overoxidized human Prx V
-
-
?
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 + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
?
sulfinic form of peroxiredoxin IIF + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 GSH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + G-S-S-G
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 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + R-SH
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
show the reaction diagram
AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature
-
-
?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 0.079
peroxiredoxin-(S-hydroxy-S-oxocysteine)
additional information
additional information
-
kinetic analysis, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00042 - 0.011
peroxiredoxin-(S-hydroxy-S-oxocysteine)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.86
sequence calculation
9.86
-
mature enzyme, sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
dual localization to plastid and mitochondrion, in line with the prediction of a signal peptide for dual targeting
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
AtSrx has more positive charges than human enzyme HsSrx. The theoretical pI of AtSrx is 9.86, much higher than 5.47 of HsSrx. There are 10 arginine residues and 7 lysine residues in AtSrx but only 5 arginine residues and 3 lysine residues in HsSrx. For negatively charged amino acids residues, there are 6 glutamic acid residues and 4 aspartic acid residues in AtSrx, while there are 2 glutamic acid residues and 8 aspartic acid residues in HsSrx. Abundant charged amino acids of AtSrx provide more positive charge at ADP binding pocket and more interaction with active
physiological function
2-Cys peroxiredoxins (Prxs) are highly abundant peroxidases that play as peroxide sensors promoting H2O2 signaling and oxidative stress resistance in respond to elevated oxidative levels. Prxs use a peroxidatic cysteine (Cys-SpH) to catalytically decompose peroxides. During normal catalysis, the peroxidatic Cys residue (Cys-SpH) is oxidized to Cys sulfenic acid (Cys-SpOH) and further inactivation by peroxidation of the peroxidatic cysteine residue to Cys sulfinic acid (Cys-SpO2-). Importantly, Prxs can be reactivated with the Cys-SPO2- moiety reduced to Cys sulfenic acid (Cys-SpOH) by a repaired enzyme known as sulfiredoxin (Srx). This reversible event is a physiologically important process against the oxidative stress that can allow cells to return to homeostasis
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SRX_ARATH
125
0
13914
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 13914, immature enzyme, sequence calculation, x * 11546, mature enzyme, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme AtSrx in complex with ADP, sitting drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM DTT, with 0.001 ml of well solution containing 0.8 M NaH2PO4/1.2M KH2PO4, and acetate, pH 4.5, at 16°C, 1 week, X-ray diffraction structure determination and analysis at 3.20 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C72S
site-directed mutagenesis, the cysteine-deficient mutation at the active completely abolishes activity of Srx
R28Q
site-directed mutagenesis, the mutation in AtSrx only partially reduces its activity and needs the additional mutation of E76 to totally inactivation. The survived activity of AtSrx may be the result of that AtSrx has two more arginine residues at the loop next to alpha1. The side chains of Arg32 and Arg34, which can swing to the side of Cys72, may partially compensate for the effects of the loss of Arg28
R28Q/E76A
site-directed mutagenesis, the double mutation disrupts the stability of the loop in which Arg32/Arg34 is located, therefore AtSrx is completely inactivated
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
R28Q/E76A
-
site-directed mutagenesis, inactive mutant
additional information
-
construction of a Srx knockout mutant, phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant wild-type Srx and mutants to homogeneity from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
gene SRX, overexpression of recombinant His-tagged full-length enzyme in Escherichia coli strain BL21(DE3)
transient expression of an AtSrx-GFP fusion in Nicotiana tabacum leaves
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)
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
under the oxidation stress elicited by hydrogen peroxide, the transcription level of AtSrx is significantly increased
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, X.P.; Liu, X.Y.; Zhang, J.; Xia, Z.L.; Liu, X.; Qin, H.J.; Wang, D.W.
Molecular and functional characterization of sulfiredoxin homologs from higher plants
Cell Res.
16
287-296
2006
Arabidopsis thaliana (Q8GY89), Oryza sativa
Manually annotated by BRENDA team
Rey, P.; Becuwe, N.; Barrault, M.B.; Rumeau, D.; Havaux, M.; Biteau, B.; Toledano, M.B.
The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response
Plant J.
49
505-514
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q8GY89)
Manually annotated by BRENDA team
Iglesias-Baena, I.; Barranco-Medina, S.; Lazaro-Payo, A.; Lopez-Jaramillo, F.J.; Sevilla, F.; Lazaro, J.J.
Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin
J. Exp. Bot.
61
1509-1521
2010
Arabidopsis thaliana, Arabidopsis thaliana Columbia
Manually annotated by BRENDA team
Chi, Y.H.; Kim, S.Y.; Jung, I.J.; Shin, M.R.; Jung, Y.J.; Park, J.H.; Lee, E.S.; Maibam, P.; Kim, K.S.; Park, J.H.; Kim, M.J.; Hwang, G.Y.; Lee, S.Y.
Dual functions of Arabidopsis sulfiredoxin: acting as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme
FEBS Lett.
586
3493-3499
2012
Arabidopsis thaliana
Manually annotated by BRENDA team
Iglesias-Baena, I.; Barranco-Medina, S.; Sevilla, F.; Lazaro, J.J.
The dual-targeted plant sulfiredoxin retroreduces the sulfinic form of atypical mitochondrial peroxiredoxin
Plant Physiol.
155
944-955
2011
Arabidopsis thaliana (Q8GY89), Pisum sativum (D2KKL9), Pisum sativum
Manually annotated by BRENDA team
Sevilla, F.; Camejo, D.; Ortiz-Espin, A.; Calderon, A.; Lazaro, J.J.; Jimenez, A.
The thioredoxin/peroxiredoxin/sulfiredoxin system current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species
J. Exp. Bot.
66
2945-2955
2015
Arabidopsis thaliana
Manually annotated by BRENDA team
Liu, M.; Wang, J.; Li, X.; Sylvanno, M.J.; Li, M.; Zhang, M.; Wang, M.
The crystal structure of sulfiredoxin from Arabidopsis thaliana revealed a more robust antioxidant mechanism in plants
Biochem. Biophys. Res. Commun.
520
347-352
2019
Arabidopsis thaliana (Q8GY89), Arabidopsis thaliana
Manually annotated by BRENDA team