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Information on EC 1.8.98.2 - sulfiredoxin and Organism(s) Mus musculus and UniProt Accession Q9D975

for references in articles please use BRENDA:EC1.8.98.2
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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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Mus musculus
UNIPROT: Q9D975
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The taxonomic range for the selected organisms is: Mus musculus
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
neoplastic progression 3
-
-
Srx1
-
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sulfiredoxin-1
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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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
peroxiredoxin III-(S-hydroxy-S-oxocysteine) + ATP + GSH
peroxiredoxin III-(S-hydroxycysteine) + ADP + phosphate + GSSG
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
?
-
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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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-
?
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 thioredoxin
peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + thioredoxin disulfide
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
catalyzes the reduction of cysteine sulfinic acid to sulfenic acid in oxidized proteins and protects them from inactivation
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RNAi
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SRXN1_MOUSE
136
0
14149
Swiss-Prot
Mitochondrion (Reliability: 5)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
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disruption of Nrf2 signaling down-regulates the expression of Srx1
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Nrf2, nuclear factor erythroid-2-related factor, up-regulates Srx1 expression during oxidative stress caused by cigarette smoke exposure in the lungs
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chang, T.S.; Jeong, W.; Woo, H.A.; Lee, S.M.; Park, S.; Rhee, S.G.
Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
J. Biol. Chem.
279
50994-51001
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Singh, A.; Ling, G.; Suhasini, A.N.; Zhang, P.; Yamamoto, M.; Navas-Acien, A.; Cosgrove, G.; Tuder, R.M.; Kensler, T.W.; Watson, W.H.; Biswal, S.
Nrf2-dependent sulfiredoxin-1 expression protects against cigarette smoke-induced oxidative stress in lungs
Free Radic. Biol. Med.
46
376-386
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Baek, J.Y.; Han, S.H.; Sung, S.H.; Lee, H.E.; Kim, Y.M.; Noh, Y.H.; Bae, S.H.; Rhee, S.G.; Chang, T.S.
Sulfiredoxin protein is critical for redox balance and survival of cells exposed to low steady-state levels of H2O2
J. Biol. Chem.
287
81-89
2012
Mus musculus (Q9D975), Mus musculus
Manually annotated by BRENDA team
Rhee, S.G.; Kil, I.S.
Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin Linking mitochondrial function to circadian rhythm
Free Radic. Biol. Med.
99
120-127
2016
Mus musculus
Manually annotated by BRENDA team
Kil, I.S.; Bae, S.H.; Rhee, S.G.
Study of the signaling function of sulfiredoxin and peroxiredoxin III in isolated adrenal gland unsuitability of clonal and primary adrenocortical cells
Methods Enzymol.
527
169-181
2013
Mus musculus
Manually annotated by BRENDA team