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Information on EC 1.11.1.24 - thioredoxin-dependent peroxiredoxin and Organism(s) Homo sapiens and UniProt Accession Q13162

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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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Homo sapiens
UNIPROT: Q13162
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
peroxiredoxin IV
-
PRx IV
2-Cys peroxiredoxin
BCP
-
-
-
-
calpromotin
-
-
natural killer enhancing factor-B
-
-
NES-Prx1
-
in cytoplasm
NLS-Prx1
-
in nucleus
nuclear export signal-Prx1
-
-
nuclear localization signal-Prx1
-
-
peroxiredoxin 1
-
peroxiredoxin 2
peroxiredoxin 3
-
a typical 2-Cys peroxiredoxin
peroxiredoxin 5
peroxiredoxin-1
-
-
peroxiredoxin-3
-
-
PRDX I
isozyme
PRDX II
isozyme
PRDX III
-
isozyme
Prx 3
-
-
Prx I
Prx II
Prx III
-
-
Prx V
Prx VI
-
1-Cys-Prx
Prx3
-
-
Prx5
-
-
PrxQ
-
-
-
-
PrxV
-
-
thiol-specific antioxidant/protector protein
-
-
thioredoxin peroxidase
-
-
-
-
thioredoxin peroxidase B
-
-
thioredoxin peroxidase II
-
-
torin
-
-
Tpx
-
-
-
-
TPx-B
-
-
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
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
-
-
-
?
cumene hydroperoxide + reduced dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
low activity
-
-
?
Gardos channel + ?
?
show the reaction diagram
-
activates the Gardos channel
-
-
?
glycine chloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
H2O2 + reduced thioredoxin
H2O + oxidized thioredoxin
show the reaction diagram
H2O2 + reduced thioredoxin 2
H2O + oxidized thioredoxin 2
show the reaction diagram
-
-
-
?
H2O2 + tryparedoxin
H2O + oxidized tryparedoxin
show the reaction diagram
-
-
-
-
?
histamine chloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
HOCl + dithiothreitol
?
show the reaction diagram
low activity
-
-
?
iodoacetamide + reduced thioredoxin
?
show the reaction diagram
-
Prx 3 reacts very slowly with iodoacetamide
-
-
?
monochloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
N-ethylmaleimide + reduced thioredoxin
?
show the reaction diagram
-
Prx 3 reacts very slowly with N-ethylmaleimide
-
-
?
peroxinitrite + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
peroxynitrite + dithiothreitol
?
show the reaction diagram
-
-
-
?
peroxynitrite + paredoxin
?
show the reaction diagram
-
-
-
-
?
taurine chloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
tert-butyl hydroperoxide + dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
-
-
-
?
tert-butyl hydroperoxide + peroxynitrite
?
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
show the reaction diagram
low activity
-
-
?
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thioredoxin
thioredoxin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
benzoate
in orthorhombic 1 form, the benzoate ion is present close to the Cp residue in both fully folded subunits the benzoate ion is not observed in the six oxidized subunits in which the disulfide bond is formed
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
peroxynitrite
-
excess of peroxynitrite inactivates the enzyme by overoxidation
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
H2O2
-
Km below 0.0007 mM, at 25°C and pH 7.4
0.0024 - 0.004
reduced thioredoxin
0.001
thioredoxin
-
pH 7.0, 37°C
additional information
additional information
-
the Km-value for H2O2 is below 0.02 mM
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
0.003 mg Prx I per mg of soluble protein Prx I, 0.0027 mg Prx II per mg of soluble protein, 0.001 mg Prx III per mg of soluble protein, 0.00003 mg Prx V per mg of soluble protein and 0.0002 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
0.0033 mg Prx I per mg of soluble protein Prx I, 0.0013 mg Prx II per mg of soluble protein, 0.0005 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0017 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
0.0027 mg Prx I per mg of soluble protein Prx I, 0.001 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0001 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
0.0033 mg Prx I per mg of soluble protein Prx I, 0.002 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0003 mg Prx V per mg of soluble protein and more than 0.005 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
-
0.0027 mg Prx I per mg of soluble protein Prx I, 0.0005 mg Prx II per mg of soluble protein, less than 0.0003 mg Prx III per mg of soluble protein, 0.0005 mg Prx V per mg of soluble protein and 0.0013 mg Prx VI per mg of soluble protein
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
NES-Prx1
Manually annotated by BRENDA team
-
NLS-Prx1
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRDX4_HUMAN
271
0
30540
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
SDS-PAGE
17000
-
2 * 17000, SDS-PAGE
17030
-
2 * 17030, calculation from nucleotide sequence
21805
1 * 21805, electrospray ionization mass spectrometry
21810
electrospray ionization mass spectrometry
219700
Prx1, Q-TOF mass spectrometry
34000
-
gel filtration
43630
Prx2, Q-TOF mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
Prx IV oligomers contain two prevalent species with apparent molecular masses of 27 and 54 kDa corresponding to Prx IV monomers and disulfide-linked homodimers
decamer
dimer
homodimer
-
-
monomer
1 * 21805, electrospray ionization mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.5 A resolution crystal structure of peroxiredoxin 5 in the reduced form
crystal form of human peroxiredoxin 5 is described at 2.0 A resolution
hanging drop vapour diffusion method with 100 mM citrate (pH 4.6) and 10% polyethylene glycol
structure of decameric 2-Cys peroxiredoxin at 1.7 A resolution
-
sulfredoxin in complex with PrxI, hanging-drop vapour diffusion method, in 20 mM HEPES pH 7.5 and 100 mM NaCl
the C72S mutant is crystallized by hanging drop vapour diffusion method with sodium cacodylate 0.1 M pH 6.5, PEG8000 20% (w/v), sodium acetate 0.1 M, and 6-aminocaproic acid 3% (w/v), at 18°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C151S
the mutation of the resolving cysteine residue does not affect peroxidatic cysteine residue reactivity
C152S
-
mutant enzyme shows no detectable thioredoxin-dependent peroxidase activity
C48S
-
mutant enzyme shows no detectable thioredoxin-dependent peroxidase activity
C52S
mutant lacks antioxidant activity
C52S/C173S
-
glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation
C72S
the C72S mutation improves the crystallization in oxidizing conditions
C73S
-
mutation has no effect on activity
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Prx can become inactivated through the hyperoxidation of an active site Cys residue to Cys sulphinic acid
689157
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Superdex 200 gel filtration
DEAE-Sepharose column chromatography, Superdex 75 gel filtration, and Superdex 200 gel filtration
-
HiPrep 16/10 DEAE column chromatography
phenyl-Sepharose column chromatography, S-Sepharose column chromatography, hydroxyapatite column chromatography, and G25 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HT-1080 cells
expressed in Escherichia coli C41(DE3) cells
expressed in LnCaP cells, LN3, C4-2, and C4-2B prostate cancer cells
expression in COS-7 cells
-
expression in Escherichia coli
-
expression of Prx I, Prx II and Prx III in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rhee, S.G.; Kang, S.W.; Chang, T.S.; Jeong, W.; Kim, K.
Peroxiredoxin, a novel family of peroxidases
IUBMB Life
52
35-41
2001
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Kang, S.W.; Chae, H.Z.; Seo, M.S.; Kim, K.; Baines, I.C.; Rhee, S.G.
Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
J. Biol. Chem.
273
6297-6302
1998
Homo sapiens
Manually annotated by BRENDA team
Seo, M.S.; Kang, S.W.; Kim, K.; Baines, I.C.; Lee, T.H.; Rhee, S.G.
Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
J. Biol. Chem.
275
20346-20354
2000
Homo sapiens
Manually annotated by BRENDA team
Declercq, J.P.; Evrard, C.; Clippe, A.; Stricht, D.V.; Bernard, A.; Knoops, B.
Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution
J. Mol. Biol.
311
751-759
2001
Homo sapiens (P30044), Homo sapiens
Manually annotated by BRENDA team
Evrard, C.; Capron, A.; Marchand, C.; Clippe, A.; Wattiez, R.; Soumillion, P.; Knoops, B.; Declercq, J.P.
Crystal structure of a dimeric oxidized form of human peroxiredoxin 5
J. Mol. Biol.
337
1079-1090
2004
Homo sapiens (P30044), Homo sapiens
Manually annotated by BRENDA team
Schroder, E.; Littlechild, J.A.; Lebedev, A.A.; Errington, N.; Vagin, A.A.; Isupov, M.N.
Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution
Structure Fold. Des.
8
605-615
2000
Homo sapiens
Manually annotated by BRENDA team
Low, F.M.; Hampton, M.B.; Winterbourn, C.C.
Peroxiredoxin 2 and peroxide metabolism in the erythrocyte
Antioxid. Redox Signal.
10
1621-1630
2008
Homo sapiens
Manually annotated by BRENDA team
Zhang, H.; Go, Y.M.; Jones, D.P.
Mitochondrial thioredoxin-2/peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress
Arch. Biochem. Biophys.
465
119-126
2007
Homo sapiens
Manually annotated by BRENDA team
Trujillo, M.; Clippe, A.; Manta, B.; Ferrer-Sueta, G.; Smeets, A.; Declercq, J.P.; Knoops, B.; Radi, R.
Pre-steady state kinetic characterization of human peroxiredoxin 5: taking advantage of Trp84 fluorescence increase upon oxidation
Arch. Biochem. Biophys.
467
95-106
2007
Homo sapiens (P30044), Homo sapiens
Manually annotated by BRENDA team
Smeets, A.; Marchand, C.; Linard, D.; Knoops, B.; Declercq, J.P.
The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins
Arch. Biochem. Biophys.
477
98-104
2008
Homo sapiens (P30044), Homo sapiens
Manually annotated by BRENDA team
Tavender, T.J.; Sheppard, A.M.; Bulleid, N.J.
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells
Biochem. J.
411
191-199
2008
Homo sapiens (Q13162), Homo sapiens
Manually annotated by BRENDA team
Park, S.Y.; Yu, X.; Ip, C.; Mohler, J.L.; Bogner, P.N.; Park, Y.M.
Peroxiredoxin 1 interacts with androgen receptor and enhances its transactivation
Cancer Res.
67
9294-9303
2007
Homo sapiens (Q06830)
Manually annotated by BRENDA team
Hansen, J.M.; Moriarty-Craige, S.; Jones, D.P.
Nuclear and cytoplasmic peroxiredoxin-1 differentially regulate NF-kappaB activities
Free Radic. Biol. Med.
43
282-288
2007
Homo sapiens
Manually annotated by BRENDA team
Peskin, A.V.; Low, F.M.; Paton, L.N.; Maghzal, G.J.; Hampton, M.B.; Winterbourn, C.C.
The high reactivity of peroxiredoxin 2 with H(2)O(2) is not reflected in its reaction with other oxidants and thiol reagents
J. Biol. Chem.
282
11885-11892
2007
Homo sapiens (P32119), Homo sapiens
Manually annotated by BRENDA team
Lee, W.; Choi, K.S.; Riddell, J.; Ip, C.; Ghosh, D.; Park, J.H.; Park, Y.M.
Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of Cys83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2
J. Biol. Chem.
282
22011-22022
2007
Homo sapiens (P32119), Homo sapiens (Q06830), Homo sapiens
Manually annotated by BRENDA team
Bae, J.Y.; Ahn, S.J.; Han, W.; Noh, D.Y.
Peroxiredoxin I and II inhibit H2O2-induced cell death in MCF-7 cell lines
J. Cell. Biochem.
101
1038-1045
2007
Homo sapiens (P30044), Homo sapiens (P32119), Homo sapiens (Q06830), Homo sapiens (Q13162)
Manually annotated by BRENDA team
Joensson, T.J.; Johnson, L.C.; Lowther, W.T.
Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace
Nature
451
98-101
2008
Homo sapiens (Q06830)
Manually annotated by BRENDA team
Hong, S.; Kim, C.Y.; Lee, J.H.; Seong, G.J.
Immunohistochemical localization of 2-Cys peroxiredoxins in human ciliary body
Tissue Cell
39
365-368
2007
Homo sapiens, Homo sapiens (P32119), Homo sapiens (Q06830)
Manually annotated by BRENDA team
Manta, B.; Hugo, M.; Ortiz, C.; Ferrer-Sueta, G.; Trujillo, M.; Denicola, A.
The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2
Arch. Biochem. Biophys.
484
146-154
2009
Homo sapiens
Manually annotated by BRENDA team
Cox, A.G.; Peskin, A.V.; Paton, L.N.; Winterbourn, C.C.; Hampton, M.B.
Redox potential and peroxide reactivity of human peroxiredoxin 3
Biochemistry
48
6495-6501
2009
Homo sapiens
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
Park, J.W.; Piszczek, G.; Rhee, S.G.; Chock, P.B.
Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity
Biochemistry
50
3204-3210
2011
Homo sapiens
Manually annotated by BRENDA team