Information on EC 1.11.1.15 - peroxiredoxin

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.15
-
RECOMMENDED NAME
GeneOntology No.
peroxiredoxin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glutathione metabolism
-
-
Glutathione metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
thiol-containing-reductant: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 [1]. 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 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 (R'-SH) (e.g. thioredoxin, AhpF, tryparedoxin or AhpD), 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 [1]. To recycle the disulfide, known atypical 2-Cys Prxs appear to use thioredoxin as an electron donor [3]. The 1-Cys Prxs conserve only the peroxidatic cysteine, so that its oxidized form is directly reduced to cysteine by the reductant molecule [4].
CAS REGISTRY NUMBER
COMMENTARY hide
207137-51-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aeropyrum pernix DSM 11879
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
subsp. pekinensis
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Zhikong scallop
UniProt
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
Chinese mitten crab
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. Gerbel
-
-
Manually annotated by BRENDA team
tammar wallaby
UniProt
Manually annotated by BRENDA team
natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain
-
-
Manually annotated by BRENDA team
L. cv. Dong-jin
-
-
Manually annotated by BRENDA team
BKM-F-1767
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-
Manually annotated by BRENDA team
BKM-F-1767
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isoform peroxiredoxin 1
UniProt
Manually annotated by BRENDA team
Populus tremula x Populus tremuloides
SwissProt
Manually annotated by BRENDA team
sheep scab mite
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
isozyme Gpx1
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
YT-1
-
-
Manually annotated by BRENDA team
YT-1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene TP0509
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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E8VQ78, E8VUX3
UniProt
Manually annotated by BRENDA team
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E8VQ78, E8VUX3
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene prxq or bcp
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-palmitoyl-2-arichidonoyl-sn-glycero-3-phosphocholine + GSH
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine hydroperoxide + GSH
?
show the reaction diagram
-
specific substrate for peroxiredoxin 6
-
-
?
2 GSH + H2O2
GSSG + 2 H2O
show the reaction diagram
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
2 thioredoxin + cumene hydroperoxide
thioredoxin disulfide + H2O + 2-phenylpropan-2-ol
show the reaction diagram
2 thioredoxin + H2O2
thioredoxin disulfide + 2 H2O
show the reaction diagram
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
2 thioredoxin + t-butyl hydroperoxide
thioredoxin disulfide + H2O + t-butanol
show the reaction diagram
arachidonoyl hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
cumene hydroperoxide + GSH
2-phenylpropan-2-ol + GSSG
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
show the reaction diagram
low activity
-
-
?
cumene hydroperoxide + reduced glutaredoxin
2-phenylpropan-2-ol + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + reduced thioredoxin
2-phenylpropan-2-ol + oxidized thioredoxin + H2O
show the reaction diagram
cumene hydroperoxide + reduced thioredoxin
?
show the reaction diagram
cumene hydroperoxide + tryparedoxin 2
2-phenylpropan-2-ol + oxidized tryparedoxin 2
show the reaction diagram
-
57% of the activity with H2O2
-
-
?
dithiothreitol + H2O2
oxidized dithiothreitol + H2O
show the reaction diagram
-
-
-
?
ethyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
-
-
-
?
Gardos channel + ?
?
show the reaction diagram
-
activates the Gardos channel
-
-
?
glycine chloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
H2O2 + 2 GSH
2 H2O + GSSG
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
H2O2 + dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
H2O2 + ferrithiocyanate
?
show the reaction diagram
H2O2 + GSH
H2O + GSSG
show the reaction diagram
H2O2 + NADPH
H2O + NADP+
show the reaction diagram
-
reaction is driven by glutathione which is maintained reduced via NADPH and glutathione reductase. Both the peroxiredoxin and glutaredoxin domains are biochemically active in the natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain. When expressed separately, the glutaredoxin domain is catalytically active and the peroxiredoxin domain posseses a weak activity when supplemented with expoenous glutaredoxin
-
-
?
H2O2 + NADPH + H+
2 H2O + 2 NADP+
show the reaction diagram
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
show the reaction diagram
H2O2 + reduced glutaredoxin
H2O + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
H2O2 + reduced plasmoredoxin
H2O + oxidized plasmoredoxin
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 + reduced thioredoxin A
2 H2O + oxidized thioredoxin A
show the reaction diagram
H2O2 + S128WNTD
H2O + ?
show the reaction diagram
S128WNTD is the S128W mutant of the N-terminal domain of AhpF (a flavoprotein disulfide reductase)
-
-
?
H2O2 + thioredoxin
?
show the reaction diagram
1-Cys peroxiredoxin is less active than 2-Cys peroxiredoxin
-
-
?
H2O2 + tryparedoxin
H2O + oxidized tryparedoxin
show the reaction diagram
H2O2 + tryparedoxin 2
H2O + oxidized tryparedoxin 2
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
-
-
?
linoleic acid hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
-
-
-
?
linoleic acid hydroperoxide + tryparedoxin 2
?
show the reaction diagram
-
7.8% of the activity with H2O2
-
-
?
linolenoyl hydroperoxide + GSH
?
show the reaction diagram
-
-
-
-
?
linoleoyl hydroperoxide + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
monochloramine + dithiothreitol
?
show the reaction diagram
slow reaction
-
-
?
N-ethylmaleimide + reduced thioredoxin
?
show the reaction diagram
-
Prx 3 reacts very slowly with N-ethylmaleimide
-
-
?
NADPH + H2O2
NADP+ + H2O
show the reaction diagram
-
-
-
?
paraquat + dithiothreitol
?
show the reaction diagram
peroxinitrite + reduced thioredoxin
?
show the reaction diagram
-
-
-
-
?
peroxinitrite + thioredoxin
?
show the reaction diagram
-
-
-
-
?
peroxynitrite + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
peroxynitrite + H2O2
nitrite + ?
show the reaction diagram
-
CPX and MPX catalytically reduce peroxynitrite to nitrite through a fast-reacting thiol group located at the peroxidatic cysteine residue (Cys52 and Cys81 in CPX and MPX respectively), thus acting as tryparedoxin/peroxynitrite oxidoreductases
-
-
?
peroxynitrite + paredoxin
?
show the reaction diagram
peroxynitrite + reduced thioredoxin
?
show the reaction diagram
-
AhpE reduces peroxynitrite 2 orders of magnitude faster than H2O2
-
-
?
phosphatidyl choline hydroperoxide + tryparedoxin 2
?
show the reaction diagram
-
3.8% of the activity with H2O2
-
-
?
phosphatidylcholine hydroperoxide + reduced glutaredoxin
? + oxidized glutaredoxin
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 + GSH
t-butanol + GSSG
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + GSH
tert-butanol + GSSG
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
tert-butyl hydroperoxide + reduced glutaredoxin
tert-butanol + oxidized glutaredoxin
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
?
show the reaction diagram
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
? + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + reduced thioredoxin
tert-butanol + oxidized thioredoxin + H2O
show the reaction diagram
tert-butyl hydroperoxide + tryparedoxin 2
tert-butanol + oxidized tryparedoxin 2
show the reaction diagram
-
95% of the activity with H2O2
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 GSH + ROOH
GSSG + H2O + ROH
show the reaction diagram
2 thioredoxin + ROOH
thioredoxin disulfide + H2O + ROH
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
inhibitory at 2 mM
AMP
inhibitory at 2 mM
ATP
3 mM ATP in concert with Mg2+, Ca2+, Mn2+, or Zn2+ lowers the peroxidase activity in a dose-dependent manner
Ca2+
92% inhibition at 2 mM, in the presence of 3 mM ATP
imidazole
Mercaptosuccinate
Mg2+
in the presence of 2 mM Mg2+, the rate of H2O2 removal is inhibited by 60%, 5% and 5% when it is assayed with 2 mM ADP, AMP or phosphate, respectively, total inactivation of 2-Cys Prx is caused by incubation with 3 mM ATP and 3 mM Mg2+
Mn2+
85% 92% inhibition at 2 mM, in the presence of 3 mM ATP
peptidoglycan
downregulates Prx expression in lymphoid tissue and heart, but not in hemocytes
peroxynitrite
phosphate
inhibitory at 2 mM
tert-butyl hydroperoxide
-
substrate inhibition
Zn2+
65% inhibition at 2 mM, in the presence of 3 mM ATP
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
stimulates enzyme expression
dithiothreitol
forkhead box transcription factor 3A
-
depletion of forkhead box transcription factor 3A leads to a dramatic reduction of Prx III mRNA showing that endogenous FOXO3A is necessary for base-line expression of Prx
-
lipopolysaccharide
stimulates enzyme expression
lipoteichoic acid
stimulates enzyme expression
-
Na+
Na+ at 25 mM stimulates expression of PrxII F
thiol
dependent
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.129
1-palmitoyl-2-arichidonoyl-sn-glycero-3-phosphocholine
-
-
0.12
1-palmitoyl-2-linolenoyl-sn-glycero-3-phosphocholine hydroperoxide
-
-
0.135
arachidonoyl hydroperoxide
-
-
0.00665 - 0.191
cumene hydroperoxide
0.0045
Ethyl hydroperoxide
in 50 mM potassium phosphate pH 7.0, at 25C
0.00038 - 16.28
H2O2
0.141
linolenoyl hydroperoxide
-
-
0.023
phosphatidylcholine hydroperoxide
-
pH 8.0, 30C
0.0024 - 0.004
reduced thioredoxin
0.0079 - 0.0087
reduced thioredoxin A
0.003 - 0.0113
S128W NTD
0.072 - 0.193
t-butyl hydroperoxide
0.00004 - 0.313
tert-butyl hydroperoxide
0.001 - 0.0794
thioredoxin
0.0319
tryparedoxin 2
-
pH 7.6, 25C
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.274 - 52
cumene hydroperoxide
52.7
Ethyl hydroperoxide
Salmonella enterica subsp. enterica serovar Typhimurium
P0A251
in 50 mM potassium phosphate pH 7.0, at 25C
0.285 - 957
H2O2
2.1
phosphatidylcholine hydroperoxide
Populus x canadensis
-
-
0.098 - 2.9
reduced thioredoxin A
33.8 - 109
S128W NTD
2 - 20.9
t-butyl hydroperoxide
1.5 - 368
tert-butyl hydroperoxide
9.65 - 20.9
thioredoxin
37
tryparedoxin 2
Leishmania infantum
-
pH 7.6, 25C
-