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Information on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin and Organism(s) Helicobacter pylori and UniProt Accession P21762

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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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Helicobacter pylori
UNIPROT: P21762
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The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
peroxiredoxin, prdx2, prx i, peroxiredoxin 1, prx ii, prdx5, peroxiredoxin 2, alkyl hydroperoxide reductase, thioredoxin peroxidase, 2-cys prx, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thioredoxin-dependent alkyl hydroperoxide reductase
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BCP
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PrxQ
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thioredoxin peroxidase
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Tpx
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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
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-
-
?
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
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-
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?
H2O2 + tryparedoxin
H2O + oxidized tryparedoxin
show the reaction diagram
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-
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?
peroxynitrite + paredoxin
?
show the reaction diagram
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?
tert-butyl hydroperoxide + peroxynitrite
?
show the reaction diagram
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?
additional information
?
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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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thioredoxin
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Swissprot
Manually annotated by BRENDA team
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, L.M.; Raudonikiene, A.; Hoffman, P.S.; Poole, L.B.
Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
J. Bacteriol.
183
1961-1973
2001
Helicobacter pylori (P21762), Helicobacter pylori
Manually annotated by BRENDA team
Trujillo, M.; Ferrer-Sueta, G.; Radi, R.
Kinetic studies on peroxynitrite reduction by peroxiredoxins
Methods Enzymol.
441
173-196
2008
Saccharomyces cerevisiae, Helicobacter pylori, Homo sapiens, Mycobacterium tuberculosis, Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team