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Information on EC 1.11.1.7 - peroxidase and Organism(s) Homo sapiens and UniProt Accession A1KZ92

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.7 peroxidase
IUBMB Comments
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
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This record set is specific for:
Homo sapiens
UNIPROT: A1KZ92
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
2
phenolic donor
+
H2O2
=
2
phenoxyl radical of the donor
+
2
H2O
2
phenolic donor
+
=
2
phenoxyl radical of the donor
+
2
Synonyms
horseradish peroxidase, horseradish peroxidase (hrp), rhepo, lactoperoxidase, eosinophil peroxidase, guaiacol peroxidase, heme peroxidase, rubrerythrin, cyp119, thiol peroxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
VPO2
isozyme
eosinophil peroxidase
-
-
-
-
extensin peroxidase
-
-
-
-
guaiacol peroxidase
-
-
-
-
Hb peroxidase
-
-
heme peroxidase
-
-
-
-
hemoglobin peroxidase
-
as a hemoprotein, hemoglobin can, in the presence of H2O2, act as a peroxidase
horseradish peroxidase (HRP)
-
-
-
-
Japanese radish peroxidase
-
-
-
-
lactoperoxidase
-
-
-
-
myeloperoxidase
oxyperoxidase
-
-
-
-
protoheme peroxidase
-
-
-
-
pyrocatechol peroxidase
-
-
-
-
rhEPO
-
recombinant human eosinophil peroxidase
scopoletin peroxidase
-
-
-
-
thiocyanate peroxidase
-
-
-
-
vascular peroxidase 1
-
verdoperoxidase
-
-
-
-
VPO1
isozyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phenolic donor:hydrogen-peroxide oxidoreductase
Heme proteins with histidine as proximal ligand. The iron in the resting enzyme is Fe(III). They also peroxidize non-phenolic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS). Certain peroxidases (e.g. lactoperoxidase, SBP) oxidize bromide, iodide and thiocyanate.
CAS REGISTRY NUMBER
COMMENTARY hide
9003-99-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,3',5,5'-tetramethylbenzidine + H2O2
?
show the reaction diagram
-
-
-
?
luminol + H2O2
?
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
show the reaction diagram
-
-
-
-
?
3,3',5,5'-tetramethylbenzidine + H2O2
?
show the reaction diagram
-
-
-
?
4-aminophenazone + H2O2
?
show the reaction diagram
-
-
-
-
r
Amplex Red + H2O2
?
show the reaction diagram
-
-
-
-
?
Br- + H2O2
?
show the reaction diagram
-
-
-
-
?
Cl- + H2O2
?
show the reaction diagram
-
-
-
-
?
Cl- + H2O2
HClO + H2O
show the reaction diagram
-
-
-
-
?
Cl- + H2O2
HOCl + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
luminol + H2O2
?
show the reaction diagram
-
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
purpurogallin + H2O
show the reaction diagram
-
-
-
-
?
SCN- + H2O2
OSCN- + H2O
show the reaction diagram
-
-
-
-
?
taurine + Cl- + H2O2
taurine chloramine + HOCl + H2O
show the reaction diagram
-
-
-
-
?
West Pico + H2O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
under conditions of severe inflammation and oxidative stress, peroxidase activity of hemoglobin-haptoglobin covalent aggregates may cause macrophage dysfunction and microvascular vasoconstriction
-
-
?
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
?
-
-
under conditions of severe inflammation and oxidative stress, peroxidase activity of hemoglobin-haptoglobin covalent aggregates may cause macrophage dysfunction and microvascular vasoconstriction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
69% inhibition at 5 mM
1-(5-fluoro-1H-indol-3-yl)methanamine
-
-
1-methyl-L-tryptophan
-
-
2,2'-bipyridyl
-
25% inhibition at 5 mM
2-(5-fluoro-1H-indol-3-yl)-N,N-dimethylethanamine
-
-
2-(5-fluoro-1H-indol-3-yl)-N-methylethanamine
-
-
3-(5-fluoro-1H-indol-3-yl)-N,N-dimethylpropan-1-amine
-
-
3-(5-fluoro-1H-indol-3-yl)-N-methylpropan-1-amine
-
-
3-(5-fluoro-1H-indol-3-yl)-N-propylpropan-1-amine
-
-
3-(5-fluoro-1H-indol-3-yl)propan-1-amine
-
-
4-(5-fluoro-1H-indol-3-yl)butan-1-amine
-
-
5-(5-fluoro-1H-indol-3-yl)pentan-1-amine
-
-
5-chlorotryptamine
-
-
5-fluoro-3-[(4-methylpiperazin-1-yl)methyl]-1H-indole
-
-
5-fluoro-3-[2-(4-methylpiperazin-1-yl)ethyl]-1H-indole
-
-
5-fluoro-3-[2-(pyrrolidin-1-yl)ethyl]-1H-indole
-
-
5-fluoro-3-[3-(4-methylpiperazin-1-yl)propyl]-1H-indole
-
-
5-fluoro-3-[3-(pyrrolidin-1-yl)propyl]-1H-indol
-
-
5-fluoro-3-[3-(pyrrolidin-1-yl)propyl]-1H-indole
-
-
5-fluoro-L-tryptophan
-
-
5-fluorotryptamine
-
-
6-(5-fluoro-1H-indol-3-yl)hexan-1-amine
-
-
diethyldithiocarbamate
-
87% inhibition at 1 mM
ethylene diamine tetraacetic acid
-
17% inhibition at 10 mM
Flufenamic acid
-
-
Haptoglobin
-
mixed type of inhibition, haptoglobin binds with hemoglobin and weakens hemoglobin peroxidase activity
-
hydroxylamine
-
84% inhibition at 1 mM
L-tryptophan
-
-
L-tryptophan benzyl ester
-
-
N,N-diethyl-2-(5-fluoro-1H-indol-3-yl)ethanamine
-
-
N,N-diethyl-3-(5-fluoro-1H-indol-3-yl)propan-1-amine
-
-
N-ethyl-2-(5-fluoro-1H-indol-3-yl)ethanamine
-
-
N-ethyl-3-(5-fluoro-1H-indol-3-yl)propan-1-amine
-
-
N-ethyl-N-[(5-fluoro-1H-indol-3-yl)methyl]ethanamine
-
-
N-ethylmaleimide
-
18% inhibition at 5 mM
N-[2-(5-fluoro-1H-indol-3-yl)ethyl]butan-1-amine
-
-
N-[2-(5-fluoro-1H-indol-3-yl)ethyl]propan-1-amine
-
-
N-[3-(5-fluoro-1H-indol-3-yl)propyl]butan-1-amine
-
-
NaCN
-
0.5 mM, 93% inhibition
Nalpha-methoxycarbonyl-L-tryptophan methyl ester
-
-
Nalpha-methyl-L-tryptophan
-
-
NaN3
-
99% inhibition at 20 mM
tryptamine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
-
-
83.33
4-aminophenazone
-
-
1.3
Br-
-
20°C, pH 6.5
10.5
guaiacol
-
-
1.5
H2O2
isozyme VPO1
0.48
o-Dianisidine
-
-
23.8
pyrogallol
-
-
0.076
SCN-
-
20°C, pH 6.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
3,3',5,5'-tetramethylbenzidine
isozyme VPO1
0.46
Br-
-
20°C, pH 6.5
13.6
SCN-
-
20°C, pH 6.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009
1-(5-fluoro-1H-indol-3-yl)methanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00175
1-methyl-L-tryptophan
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
0.00009
2-(5-fluoro-1H-indol-3-yl)-N,N-dimethylethanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0002
2-(5-fluoro-1H-indol-3-yl)-N-methylethanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00013
3-(5-fluoro-1H-indol-3-yl)-N,N-dimethylpropan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0002
3-(5-fluoro-1H-indol-3-yl)-N-methylpropan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00017
3-(5-fluoro-1H-indol-3-yl)-N-propylpropan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00005
3-(5-fluoro-1H-indol-3-yl)propan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.000015
4-(5-fluoro-1H-indol-3-yl)butan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.000008
5-(5-fluoro-1H-indol-3-yl)pentan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.001
5-fluoro-3-[(4-methylpiperazin-1-yl)methyl]-1H-indole
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0002
5-fluoro-3-[2-(4-methylpiperazin-1-yl)ethyl]-1H-indole
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00004
5-fluoro-3-[2-(pyrrolidin-1-yl)ethyl]-1H-indole
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00035
5-fluoro-3-[3-(4-methylpiperazin-1-yl)propyl]-1H-indole
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00032
5-fluoro-3-[3-(pyrrolidin-1-yl)propyl]-1H-indol
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00325
5-fluoro-L-tryptophan
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
0.0002
5-fluorotryptamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00026
6-(5-fluoro-1H-indol-3-yl)hexan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00225
L-tryptophan
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
0.000175
L-tryptophan benzyl ester
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
0.00016
N,N-diethyl-2-(5-fluoro-1H-indol-3-yl)ethanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00035
N,N-diethyl-3-(5-fluoro-1H-indol-3-yl)propan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0003
N-ethyl-2-(5-fluoro-1H-indol-3-yl)ethanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0003
N-ethyl-3-(5-fluoro-1H-indol-3-yl)propan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0002
N-ethyl-N-[(5-fluoro-1H-indol-3-yl)methyl]ethanamine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00103
N-[2-(5-fluoro-1H-indol-3-yl)ethyl]butan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0008
N-[2-(5-fluoro-1H-indol-3-yl)ethyl]propan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.0015
N-[3-(5-fluoro-1H-indol-3-yl)propyl]butan-1-amine
Homo sapiens
-
in phosphate buffer pH 7.4, at 37°C
0.00035
Nalpha-methoxycarbonyl-L-tryptophan methyl ester
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
0.0052
Nalpha-methyl-L-tryptophan
Homo sapiens
-
at 25°C in 0.2 M sodium phosphate buffer, pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.05
-
with 2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
thioreoxin peroxidase
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PXDNL_HUMAN
1463
0
163686
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
165000
SDS-PAGE
165000
SDS-PAGE
31000
-
recombinant thioredoxin peroxidase, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
production of rhEPO by Pichia pastoris as a glycosylated dimer
proteolytic modification
-
production of rhEPO by Pichia pastoris as a glycosylated dimer precursor of approximately 80 kDa. Proteolytic processing, similar to that in the native host, to generate two chains of approximately 50 kDa and 20 kDa
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expression in Pichia pastoris
-
VPO1 is expressed in HEK-293H cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.005-0.05 mg/ml Oenothera paradoxa extract, penta-O-galloyl-beta-D-glucose, indomethacin, catechin and gallic acid significantly inhibit myeloperoxidase release
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jin, D.Y.; Chae, H.Z.; Rhee, S.G.; Jeang, K.T.
Regulatory role for a novel human thioredoxin peroxidase in NF-.kappa.B activation
J. Biol. Chem.
272
30952-30961
1997
Homo sapiens
Manually annotated by BRENDA team
Shindler, J.S.; Childs, R.E.; Bardsley, W.G.
Peroxidase from human cervical mucus. The isolation and characterisation
Eur. J. Biochem.
65
325-331
1976
Homo sapiens
Manually annotated by BRENDA team
Ciaccio, C.; Gambacurta, A.; De Sanctis, G.; Spagnolo, D.; Sakarikou, C.; Petrella, G.; Coletta, M.
rhEPO (recombinant human eosinophil peroxidase): expression in Pichia pastoris and biochemical characterization
Biochem. J.
395
295-301
2006
Homo sapiens
Manually annotated by BRENDA team
Cheng, G.; Salerno, J.C.; Cao, Z.; Pagano, P.J.; Lambeth, J.D.
Identification and characterization of VPO1, a new animal heme-containing peroxidase
Free Radic. Biol. Med.
45
1682-1694
2008
Mus musculus, Homo sapiens (A1KZ92), Homo sapiens (Q92626), Homo sapiens
Manually annotated by BRENDA team
Kapralov, A.; Vlasova, I.I.; Feng, W.; Maeda, A.; Walson, K.; Tyurin, V.A.; Huang, Z.; Aneja, R.K.; Carcillo, J.; Bayir, H.; Kagan, V.E.
Peroxidase activity of hemoglobin-haptoglobin complexes: Covalent aggregation and oxidative stress in plasma and macrophages
J. Biol. Chem.
284
30395-30407
2009
Homo sapiens
Manually annotated by BRENDA team
Sliskovic, I.; Abdulhamid, I.; Sharma, M.; Abu-Soud, H.M.
Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase
Free Radic. Biol. Med.
47
1005-1013
2009
Homo sapiens
Manually annotated by BRENDA team
Kiss, A.K.; Filipek, A.; Czerwinska, M.; Naruszewicz, M.
Oenothera paradoxa defatted seeds extract and its bioactive component penta-O-galloyl-beta-D-glucose decreased production of reactive oxygen species and inhibited release of leukotriene B4, interleukin-8, elastase, and myeloperoxidase in human neutrophils
J. Agric. Food Chem.
58
9960-9966
2010
Homo sapiens
Manually annotated by BRENDA team
Soubhye, J.; Prevost, M.; Van Antwerpen, P.; Zouaoui Boudjeltia, K.; Rousseau, A.; Furtmueller, P.G.; Obinger, C.; Vanhaeverbeek, M.; Ducobu, J.; Neve, J.; Gelbcke, M.; Dufrasne, F.O.
Structure-Bbased design, synthesis, and pharmacological evaluation of 3-(aminoalkyl)-5-fluoroindoles as myeloperoxidase inhibitors
J. Med. Chem.
53
8747-8759
2010
Homo sapiens
Manually annotated by BRENDA team