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Information on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin and Organism(s) Caenorhabditis elegans and UniProt Accession A0A0K3AUJ9

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.24 thioredoxin-dependent peroxiredoxin
IUBMB Comments
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins . The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
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Caenorhabditis elegans
UNIPROT: A0A0K3AUJ9
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
peroxiredoxin, prdx2, prx i, peroxiredoxin 1, prx ii, peroxiredoxin 2, prdx5, alkyl hydroperoxide reductase, thioredoxin peroxidase, 2-cys prx, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PRDX-2
Q8IG31
a 2-Cys peroxiredoxin
BCP
-
-
-
-
PRDX-3
a 2-Cys peroxiredoxin
PrxQ
-
-
-
-
thioredoxin peroxidase
-
-
-
-
Tpx
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thioredoxin:hydroperoxide oxidoreductase
Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant proteins. They can be divided into three classes: typical 2-Cys, atypical 2-Cys and 1-Cys peroxiredoxins [4]. The peroxidase reaction comprises two steps centred around a redox-active cysteine called the peroxidatic cysteine. All three peroxiredoxin classes have the first step in common, in which the peroxidatic cysteine attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid) (see {single/111115a::mechanism}). The second step of the peroxidase reaction, the regeneration of cysteine from S-hydroxycysteine, distinguishes the three peroxiredoxin classes. For typical 2-Cys Prxs, in the second step, the peroxidatic S-hydroxycysteine from one subunit is attacked by the 'resolving' cysteine located in the C-terminus of the second subunit, to form an intersubunit disulfide bond, which is then reduced by one of several cell-specific thiol-containing reductants completing the catalytic cycle. In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its resolving cysteine are in the same polypeptide, so their reaction forms an intrachain disulfide bond. The 1-Cys Prxs conserve only the peroxidatic cysteine, so its regeneration involves direct interaction with a reductant molecule. Thioredoxin-dependent peroxiredoxins are the most common. They have been reported from archaea, bacteria, fungi, plants, and animals.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q21824, Q8IG31
-
-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
Q21824, Q8IG31
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thioredoxin
Q21824, Q8IG31
-
thioredoxin
Q21824, Q8IG31
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRDX_CAEEL
201
0
22413
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
Q21824, Q8IG31
reduced PRDX-2, SDS-PAGE
20000
Q21824, Q8IG31
reduced PRDX-3, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PRDX-2 is sensitive to hydrogen peroxide-induced oxidation, after treatment with 5.0 mM H2O2, reduced PRDX-2 is replaced with a hyperoxidized monomeric form and an additional peroxide-induced PRDX-2 disulfide
Q21824, Q8IG31
700970
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olahova, M.; Taylor, S.R.; Khazaipoul, S.; Wang, J.; Morgan, B.A.; Matsumoto, K.; Blackwell, T.K.; Veal, E.A.
A redox-sensitive peroxiredoxin that is important for longevity has tissue- and stress-specific roles in stress resistance
Proc. Natl. Acad. Sci. USA
105
19839-19844
2008
Caenorhabditis elegans (Q21824), Caenorhabditis elegans (Q8IG31), Caenorhabditis elegans
Manually annotated by BRENDA team