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Information on EC 1.11.1.8 - iodide peroxidase and Organism(s) Homo sapiens

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.8 iodide peroxidase
IUBMB Comments
Thyroid peroxidase catalyses the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine. It catalyses both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
thyroid peroxidase, thyroperoxidase, bromoperoxidase, vanadium bromoperoxidase, iodide peroxidase, hrtpo, iodinase, hmw-tpo, tyrosine iodinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
high-molecular weight-thyroid peroxidase
-
-
HMW-TPO
-
-
hrTPO
-
-
hTPO
-
-
iodide peroxidase-tyrosine iodinase
-
-
-
-
iodinase
-
-
-
-
iodoperoxidase (heme type)
-
-
-
-
thyroid peroxidase
thyroperoxidase
TPOX
-
-
tyrosine iodinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iodination
-
-
-
-
oxidation
-
-
-
-
peroxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
iodide:hydrogen-peroxide oxidoreductase
Thyroid peroxidase catalyses the biosynthesis of the thyroid hormones L-thyroxine and triiodo-L-thyronine. It catalyses both the iodination of tyrosine residues in thyroglobulin (forming mono- and di-iodinated forms) and their coupling to form either L-thyroxine or triiodo-L-thyronine.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-28-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3 I- + H2O2 + 2 H+
triiodide + 2 H2O ?
show the reaction diagram
-
-
-
-
?
3,3',5,5'-tetramethylbenzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
3,3'-dimethylbenzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
benzidine + H2O2
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenoquinone + H2O
show the reaction diagram
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
?
guaiacol + H2O2 + H+
3,3'-dimethoxy-4,4'-biphenoquinone + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2 + I-
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
I- + H2O2
triiodide + ?
show the reaction diagram
-
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
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
iodide + H2O2
iodine + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2',4,4'-tetrahydroxybenzophenone
2-mercaptobenzothiazole
-
3,4,5-hydroxybenzoic acid propyl ester
-
mixed type inhibition
3-methylcholanthrene
-
-
6-Propyl-2-thiouracil
-
amino-1,2,4-triazole
-
-
arsenic trioxide
benzhydrol
-
reduces the enzyme activity by about 30% from 0.01 to 0.1 mM
benzo(e)pyrene
-
-
benzo(k)fluoranthene
-
-
benzophenone
-
-
benzophenone 2
-
inactivation is prevented by iodideone of the most potent inhibitors of TPO
bisphenol A
-
-
cysteine
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
F21388
-
-
genistein
H2O2
-
inactivation is prevented by iodide
heptachlor
-
weakly inhibits the enzyme activity by about 50% at 0.01 mM
histidine
-
-
mearnsitrin
-
IC50: 0.00197 mM. Flavonoid from aqueous partition of Myrcia uniflora. Indiscriminated consumption of Myrcia uniflora pharmaceutical products allied to the nutritional deficiency of iodine might contribute to the development of hypothyroidism and goiter
methimazol
-
-
Methimazole
methionine
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
Myricitrin
-
IC50: 0.00188 mM. Flavonoid from aqueous partition of Myrcia uniflora. Indiscriminated consumption of Myrcia uniflora pharmaceutical products allied to the nutritional deficiency of iodine might contribute to the development of hypothyroidism and goiter
perfluorooctane sulfonate
-
-
Perfluorooctanoic acid
-
slight inhibition at 0.01 mM
phenylalanine
-
-
propylthiouracil
-
-
pyrene
-
-
reduced glutathione
-
presence of 0.1 ppm minimally affects enzyme activity. Presence of 0.1 ppm arsenic trioxide plus 0.1 ppm reduced glutathione leads to complete inhibition
resorcinol
-
sunitinib
-
sunitinib is a tyrosine kinase inhibitor with antitumor and antiangiogenic effects. Its antithyroid effect appears to be inhibition of peroxidase
TR1.9 autoantibody
preferentially binds the TPO monomer and inhibits the catalytic activity
-
tryptophan
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
tyrosine
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dihydroxy-4-methoxy benzophenone
-
increases the enzyme activity by about 1.5fold
2,4-dihydroxy benzophenone
-
increases the enzyme activity by about 1.5fold
dibenzo(a,h)anthracene
-
2fold activation between 0.01 and 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.166
3,3',5,5'-tetramethylbenzidine
-
pH 5.5
0.058
3,3'-dimethoxybenzidine
-
pH 5.5
0.177
3,3'-dimethylbenzidine
-
pH 5.5
0.049
benzidine
-
pH 5.5
5.55 - 9.67
guaiacol
7.7
I-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34.6
3,3',5,5'-tetramethylbenzidine
-
pH 5.5
11.9
3,3'-dimethoxybenzidine
-
pH 5.5
27.5
3,3'-dimethylbenzidine
-
pH 5.5
6
benzidine
-
pH 5.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009
3,4,5-hydroxybenzoic acid propyl ester
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00197
mearnsitrin
Homo sapiens
-
IC50: 0.00197 mM. Flavonoid from aqueous partition of Myrcia uniflora. Indiscriminated consumption of Myrcia uniflora pharmaceutical products allied to the nutritional deficiency of iodine might contribute to the development of hypothyroidism and goiter
0.00188
Myricitrin
Homo sapiens
-
IC50: 0.00188 mM. Flavonoid from aqueous partition of Myrcia uniflora. Indiscriminated consumption of Myrcia uniflora pharmaceutical products allied to the nutritional deficiency of iodine might contribute to the development of hypothyroidism and goiter
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180
-
pH 7.4, 25°C
2.42
mutant G387R, pH 7.4, temperature not specified in the publication
3.06
mutant C808R, pH 7.4, temperature not specified in the publication
381
-
purified enzyme with guaiacol as substrate
4.6
mutant P499L, pH 7.4, temperature not specified in the publication
7.22
wild-type, pH 7.4, temperature not specified in the publication
additional information
-
development of an ELISA system for quantitative determination of thyroid peroxidase in biological fluids, based on the use of an analytical pair of monoclonal antibodies, one of which is immobilized on solid phase, the other being present in solution. The use of this system made it possible to determine the biochemical characteristics of immunoaffinity chromatography of the enzyme and propose a new method for obtaining a highly purified preparation of its protein
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
calculated
6.4
and 7.1, isoelectric focusing, breast tissue isoform
7.1
and 6.4, isoelectric focusing, breast tissue isoform
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the molecular weight of breast TPO is slightly lower than that of thyroid TPO due to decreased glycosylation. Enzymatic activity and isoelectric point of the isomforms are comparable
Manually annotated by BRENDA team
-
follicular carcinoma cell
Manually annotated by BRENDA team
TPO is expressed at gene and protein levels in endometrium and placenta, expression is mainly localized to he syncytiotrophoblasts and invasive trophoblast cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
lesion, negative correlation between thyroperoxidase and dual oxidase H2O2-generating activities
Manually annotated by BRENDA team
TPO is expressed at gene and protein levels in endometrium and placenta, expression is mainly localized to glandular and luminal epithelial cells in the endometrium
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in Graves‘ disease, the nuclear envelope, enlarged rough endoplasmic reticulum, and apical vesicles are strongly TPO positive
Manually annotated by BRENDA team
-
wild-type enzyme and mutant enzymes G614A, G1687T, 1808-13del, C2083, G2401A
Manually annotated by BRENDA team
-
of Graves‘ disease thyroid, enzyme is absent in the microvilli in multinodular goiter
Manually annotated by BRENDA team
-
in the perinodular normal tissue the enzyme is detected mainly in the nuclear envelope, rough endoplasmic reticulum, and subapical vesicles. In cells from Hashimoto‘s thyroiditis detected in scarce rough endoplasmic reticulum. In Graves‘ disease, the nuclear envelope, enlarged rough endoplasmic reticulum, and apical vesicles are strongly TPO positive
Manually annotated by BRENDA team
-
in Graves' disease, the nuclear envelope, enlarged rough endoplasmic reticulum, and apical vesicles are strongly TPO positive, in the perinodular normal tissue the enzyme is detected mainly in the nuclear envelope, rough endoplasmic reticulum, and subapical vesicles
Manually annotated by BRENDA team
additional information
-
in the perinodular normal tissue the enzyme is absent in the apical surface, enzyme from multinodular goiter is absent in the microvilli
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the transfer of iodine to thyroglobulin during thyroid hormone synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PERT_HUMAN
933
1
102963
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A0G2JR31_HUMAN
859
1
94837
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2JRX3_HUMAN
347
1
38977
TrEMBL
other Location (Reliability: 3)
Q502Y3_HUMAN
933
1
102937
TrEMBL
Secretory Pathway (Reliability: 1)
Q53QT2_HUMAN
916
1
101085
TrEMBL
Secretory Pathway (Reliability: 1)
A0M8X1_HUMAN
933
1
102945
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2JP53_HUMAN
933
1
102979
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2JR90_HUMAN
743
1
82719
TrEMBL
Secretory Pathway (Reliability: 1)
H7C1F5_HUMAN
404
1
45183
TrEMBL
other Location (Reliability: 3)
A0A0G2JRZ1_HUMAN
916
1
101101
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
105000
107600
-
2 * 107600, calculated from SDS-PAGE
110000
-
2 * 110000, SDS-PAGE
220000 - 240000
-
the high-molecular weight-thyroid peroxidase is in the 220000-240000 Da range, SDS-PAGE
91000
-
native enzyme, SDS-PAGE, double band of MW 94000
94000
-
native enzyme, SDS-PAGE, double band of MW 91000
96000
-
recombinant enzyme, SDS-PAGE, double band of MW 99000
97000
-
SDS-PAGE, double band with 105000 species
99000
-
recombinant enzyme, SDS-PAGE, double band of MW 96000
additional information
-
conformational dominant epitopes on thyroid peroxidase recognized by human autoantibodies
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
and monomer, 1 * 110000, SDS-PAGE, recombinant His-tagged TPO construct lacking the propeptide and recombinant GCN4 leucine zipper-tagged TPO construct lacking the propeptide
homodimer
monomer
and dimer, 1 * 110000, SDS-PAGE, recombinant His-tagged TPO construct lacking the propeptide and recombinant GCN4 leucine zipper-tagged TPO construct lacking the propeptide
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C808R
natural missense mutation, mutant shows higher Km values and lower reaction efficiencies thna wild-type
D358A
-
mutation at position 358 led to a loss of the binding of human anti-TPO autoantibodies as efficient as a mutation of the entire region 353–363
D574/L575del
-
expressed to some extent on the cell surface, prolongation in kinetics, increasing interaction with calnexin
G387R
natural missense mutation, mutant shows higher Km values and lower reaction efficiencies thna wild-type
G533C
-
expressed to some extent on the cell surface, prolongation in kinetics, increasing interaction with calnexin
G771R
-
expressed to some extent on the cell surface, prolongation in kinetics, increasing interaction with calnexin
P499L
natural missense mutation, mutant shows higher Km values and lower reaction efficiencies thna wild-type
Q446H
-
the mutation is associated with the occurrence of congenital hypothyroidism
W527C
-
the mutation is associated with the occurrence of congenital hypothyroidism
W873X
-
the mutation is associated with the occurrence of congenital hypothyroidism
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C or -4°C, enzyme retains its immunoreactivity
-
-18°C, 4 months, ability of the protein to interact with autoantibodies is decreased by 20%
-
-70°C, 50 mM Tris-HCl, 0.15 M NaCl, pH 8.5, 0.1% deoxycholate
-
-70°C, purified recombinant protein treated with 600 microM hemin, stable for for 4 years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CHO-K1 cells introduced with mutated TPO-MRNA
-
expressed in CHO cells
-
expressed in FTC-238 cells
-
expressed in High Five cells, active enzyme
-
expressed in High Five cells, activity similar to native enzyme when grown in presence of delta-aminolevulinic acid, enzyme in supernatant
-
expressed in High Five cells, enzyme insoluble and inactive
-
expressed in insect cells and in Chinese hamster ovary cells, activity detected when grown in presence of hematin or hemin
-
expressed in Sf9 cells, no activity when grown in serum free medium, active when grown in medium containing 10% fetal calf serum and 1 mg/l haematin
-
expression in AD-293 cell
-
expression in baculovirus system
expression in Chinese hamster ovary (CHO) cells
-
expression in CHO and LentiX-293 cell
stable expression of mutant enzymes at the surface of CHO cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
thyroid-stimulating hormone (10 mUI/ml, for 24 h) does not affect TPO mRNA level
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Czarnocka, B.; Ruf, J.; Ferrand, M.; Carayon, P.; Lissitzky, S.
Purification of the human thyroid peroxidase and its identification as the microsomal antigen involved in autoimmune thyroid diseases
FEBS Lett.
190
147-152
1985
Homo sapiens
Manually annotated by BRENDA team
Fan, J.L.; Patibandla, S.A.; Kimura, S.; Rao, T.N.; Desai, R.K.; Seetharamaiah, G.S.; Kurosky, A.; Prabhakar, B.S.
Purification and characterization of a recombinant human thyroid peroxidase expressed in insect cells
J. Autoimmun.
9
529-536
1996
Homo sapiens
Manually annotated by BRENDA team
Grennan Jones, F.; Wolstenholme, A.; Fowler, S.; Smith, S.; Ziemnicka, K.; Bradbury, J.; Furmaniak, J.; Smith, B.R.
High-level expression of recombinant immunoreactive thyroid peroxidase in the High Five insect cell line
J. Mol. Endocrinol.
17
165-174
1996
Homo sapiens
Manually annotated by BRENDA team
Gardas, A.; Lewartowska, A.; Sutton, B.J.; Pasieka, Z.; McGregor, M.; Banga, J.P.
Human thyroid peroxidase (TPO) isoforms, TPO-1 and TPO-2: Analysis of protein expression in Graves' thyroid tissue
J. Clin. Endocrinol. Metab.
82
3752-3756
1997
Homo sapiens
Manually annotated by BRENDA team
Guo, J.; McLachlan, S.M.; Hutchison, S.; Rapoport, B.
The greater glycan content of recombinant human thyroid peroxidase of mammalian than of insect cell origin facilitates purification to homogeneity of enzymically protein remaining soluble at high concentration
Endocrinology
139
999-1005
1998
Homo sapiens
Manually annotated by BRENDA team
Gardas, A.; Sutton, B.J.; Piotrowska, U.; Pasieka, Z.; Barnett, P.S.; Huang, G.; McGregor, A.M.; Banga, J.P.
Distinct immunological and biochemical properties of thyroid peroxidase purified from human thyroid glands and recombinant protein produced in insect cells
Biochim. Biophys. Acta
1433
229-239
1999
Homo sapiens
Manually annotated by BRENDA team
Gut, P.; Grennan Jones, F.; Sullivan, A.; Ziemnicka, K.; Smith, S.; Jaskolski, D.; Furmaniak, J.; Rees Smith, B.
Recombinant human thyroid peroxidase produced in insect cells has similar properties to native human thyroid peroxidase
Thyroid
10
543-550
2000
Homo sapiens
Manually annotated by BRENDA team
Carvalho, D.P.; Ferreira, A.C.; Coelho, S.M.; Moraes, J.M.; Camacho, M.A.; Rosenthal, D.
Thyroid peroxidase activity is inhibited by amino acids
Braz. J. Med. Biol. Res.
33
355-361
2000
Homo sapiens
Manually annotated by BRENDA team
Grintsevich, E.E.; Senchuk, V.V.; Puchkaev, A.V.; Metelitza, D.I.
Propyl gallate inhibition of iodide and tetramethylbenzidine oxidation catalyzed by human thyroid peroxidase
Biochemistry (Moscow)
65
924-932
2000
Homo sapiens
Manually annotated by BRENDA team
Sentchouk, V.V.; Grintsevich, E.E.
Oxidation of benzidine and its derivatives by thyroid peroxidase
Biochemistry
69
201-207
2004
Homo sapiens
Manually annotated by BRENDA team
Masini-Repiso, A.M.; Bonaterra, M.; Spitale, L.; Di Fulvio, M.; Bonino, M.I.; Coleoni, A.H.; Orgnero-Gaisan, E.
Ultrastructural localization of thyroid peroxidase, hydrogen peroxide-generating sites, and monoamine oxidase in benign and malignant thyroid diseases
Hum. Pathol.
35
436-446
2004
Homo sapiens
Manually annotated by BRENDA team
Bresson, D.; Pugniere, M.; Roquet, F.; Rebuffat, S.A.; N-Guyen B.; Cerutti, M.; Guo, J.; McLachlan, S.M.; Rapoport, B.; Estienne, V.; Ruf, J.; Chardes, T.; Peraldi-Roux, S.
Directed mutagenesis in region 713-720 of human thyroperoxidase assigns 713KFPED717 residues as being involved in the B domain of the discontinuous immunodominant region recognized by human autoantibodies
J. Biol. Chem.
279
39058-39067
2004
Homo sapiens
Manually annotated by BRENDA team
Umeki, K.; Kawano, J.i.; Yamamoto, I.; Aratake, Y.; Kotani, T.
Comparative analysis and characterization of mutated thyroid peroxidases with disturbance expressed on the cell surface
Mol. Cell. Endocrinol.
223
77-84
2004
Homo sapiens
Manually annotated by BRENDA team
Tsyganova, O.V.; Kiseleva, E.P.; Vashkevich, I.I.; Pryadko, A.G.; Sviridov, O.V.
Characteristics of immunoaffinity chromatography and a new method for isolation of human thyroid peroxidase from subcellular fractions of thyroid gland
Appl. Biochem. Microbiol.
42
210-219
2006
Homo sapiens
-
Manually annotated by BRENDA team
Ruf, J.; Carayon, P.
Structural and functional aspects of thyroid peroxidase
Arch. Biochem. Biophys.
445
269-277
2006
Homo sapiens, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Ferreira, A.C.; Neto, J.C.; da Silva, A.C.; Kuster, R.M.; Carvalho, D.P.
Inhibition of thyroid peroxidase by Myrcia uniflora flavonoids
Chem. Res. Toxicol.
19
351-355
2006
Homo sapiens
Manually annotated by BRENDA team
Bresson, D.; Rebuffat, S.A.; Nguyen, B.; Banga, J.P.; Gardas, A.; Peraldi-Roux, S.
New insights into the conformational dominant epitopes on thyroid peroxidase recognized by human autoantibodies
Endocrinology
146
2834-2844
2005
Homo sapiens
Manually annotated by BRENDA team
Dubska, M.; Banga, J.P.; Plochocka, D.; Hoser, G.; Kemp, E.H.; Sutton, B.J.; Gardas, A.; Gora, M.
Structural insights into autoreactive determinants in thyroid peroxidase composed of discontinuous and multiple key contact amino acid residues contributing to epitopes recognized by patients autoantibodies
Endocrinology
147
5995-6003
2006
Homo sapiens
Manually annotated by BRENDA team
Ehrenshaft, M.; Mason, R.P.
Protein radical formation on thyroid peroxidase during turnover as detected by immuno-spin trapping
Free Radic. Biol. Med.
41
422-430
2006
Homo sapiens
Manually annotated by BRENDA team
Rebuffat, S.A.; Bresson, D.; Nguyen, B.; Peraldi-Roux, S.
The key residues in the immunodominant region 353-363 of human thyroid peroxidase were identified
Int. Immunol.
18
1091-1099
2006
Homo sapiens
Manually annotated by BRENDA team
Nakagawa, T.; Maruyama, K.; Takeyama, H.; Matsunaga, T.
Determination of microsatellite repeats in the human thyroid peroxidase (TPOX) gene using an automated gene analysis system with nanoscale engineered biomagnetite
Biosens. Bioelectron.
22
2276-2281
2007
Homo sapiens
Manually annotated by BRENDA team
Rivolta, C.M.; Louis-Tisserand, M.; Varela, V.; Gruneiro-Papendieck, L.; Chiesa, A.; Gonzalez-Sarmiento, R.; Targovnik, H.M.
Two compound heterozygous mutations (c.215delA/c.2422T-->C and c.387delC/c.1159G-->A) in the thyroid peroxidase gene responsible for congenital goitre and iodide organification defect
Clin. Endocrinol. (Oxf.)
67
238-246
2007
Homo sapiens
Manually annotated by BRENDA team
Schmutzler, C.; Bacinski, A.; Gotthardt, I.; Huhne, K.; Ambrugger, P.; Klammer, H.; Schlecht, C.; Hoang-Vu, C.; Grueters, A.; Wuttke, W.; Jarry, H.; Koehrle, J.
The ultraviolet filter benzophenone 2 interferes with the thyroid hormone axis in rats and is a potent in vitro inhibitor of human recombinant thyroid peroxidase
Endocrinology
148
2835-2844
2007
Homo sapiens
Manually annotated by BRENDA team
Poncin, S.; Lengele, B.; Colin, I.M.; Gerard, A.C.
Differential interactions between Th1/Th2, Th1/Th3, and Th2/Th3 cytokines in the regulation of thyroperoxidase and dual oxidase expression, and of thyroglobulin secretion in thyrocytes in vitro
Endocrinology
149
1534-1542
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Avbelj, M.; Tahirovic, H.; Debeljak, M.; Kusekova, M.; Toromanovic, A.; Krzisnik, C.; Battelino, T.
High prevalence of thyroid peroxidase gene mutations in patients with thyroid dyshormonogenesis
Eur. J. Endocrinol.
156
511-519
2007
Homo sapiens
Manually annotated by BRENDA team
Ginabreda, M.G.; Cardoso, L.C.; Nobrega, F.M.; Ferreira, A.C.; Goncalves, M.D.; Vaisman, M.; Carvalho, D.P.
Negative correlation between thyroperoxidase and dual oxidase H2O2-generating activities in thyroid nodular lesions
Eur. J. Endocrinol.
158
223-227
2008
Homo sapiens
Manually annotated by BRENDA team
Pedersen, I.B.; Laurberg, P.; Knudsen, N.; J?rgensen, T.; Perrild, H.; Ovesen, L.; Rasmussen, L.B.
Smoking is negatively associated with the presence of thyroglobulin autoantibody and to a lesser degree with thyroid peroxidase autoantibody in serum: a population study
Eur. J. Endocrinol.
158
367-373
2008
Homo sapiens
Manually annotated by BRENDA team
Wong, E.; Rosen, L.S.; Mulay, M.; Vanvugt, A.; Dinolfo, M.; Tomoda, C.; Sugawara, M.; Hershman, J.M.
Sunitinib induces hypothyroidism in advanced cancer patients and may inhibit thyroid peroxidase activity
Thyroid
17
351-355
2007
Homo sapiens
Manually annotated by BRENDA team
McLachlan, S.M.; Rapoport, B.
Thyroid peroxidase as an autoantigen
Thyroid
17
939-948
2007
Homo sapiens
Manually annotated by BRENDA team
Simm, D.; Pfarr, N.; Pohlenz, J.; Prawitt, D.; Doerr, H.G.
Two novel mutations in the human thyroid peroxidase (TPO) gene: genetics and clinical findings in four children
Acta Paediatr.
98
1057-1061
2009
Homo sapiens
Manually annotated by BRENDA team
Palazzolo, D.L.; Jansen, K.P.
The minimal arsenic concentration required to inhibit the activity of thyroid peroxidase activity in vitro
Biol. Trace Elem. Res.
126
49-55
2008
Homo sapiens
Manually annotated by BRENDA team
Savin, S.; Cvejic, D.; Isic, T.; Paunovic, I.; Tatic, S.; Havelka, M.
Thyroid peroxidase and galectin-3 immunostaining in differentiated thyroid carcinoma with clinicopathologic correlation
Hum. Pathol.
39
1656-1663
2008
Homo sapiens
Manually annotated by BRENDA team
McDonald, D.O.; Pearce, S.H.
Thyroid peroxidase forms thionamide-sensitive homodimers: relevance for immunomodulation of thyroid autoimmunity
J. Mol. Med.
87
971-980
2009
Homo sapiens
Manually annotated by BRENDA team
Cianfarani, F.; Baldini, E.; Cavalli, A.; Marchioni, E.; Lembo, L.; Teson, M.; Persechino, S.; Zambruno, G.; Ulisse, S.; Odorisio, T.; DArmiento, M.
TSH receptor and thyroid-specific gene expression in human skin
J. Invest. Dermatol.
130
93-101
2010
Homo sapiens
Manually annotated by BRENDA team
Song, M.; Kim, Y.J.; Park, Y.K.; Ryu, J.C.
Changes in thyroid peroxidase activity in response to various chemicals
J. Environ. Monit.
14
2121-2126
2012
Homo sapiens
Manually annotated by BRENDA team
Godlewska, M.; Gora, M.; Buckle, A.M.; Porebski, B.T.; Kemp, E.H.; Sutton, B.J.; Czarnocka, B.; Banga, J.P.
A redundant role of human thyroid peroxidase propeptide for cellular, enzymatic, and immunological activity
Thyroid
24
371-382
2014
Homo sapiens
Manually annotated by BRENDA team
Palazzolo, D.L.; Ely, E.A.
Arsenic trioxide and reduced glutathione act synergistically to augment inhibition of thyroid peroxidase activity in vitro
Biol. Trace Elem. Res.
165
110-117
2015
Homo sapiens
Manually annotated by BRENDA team
Maruta, J.; Hashimoto, H.; Yamashita, H.; Noguchi, H.; Noguchi, S.; Kobayashi, T.K.; Tsuneoka, H.; Takahashi, M.
Value of thyroid specific peroxidase and Ki-67 stains in preoperative cytology for thyroid follicular tumors
Diagn. Cytopathol.
43
202-209
2015
Homo sapiens
Manually annotated by BRENDA team
Kaur, P.; Patil, H.; Bhanushali, P.; Badgujar, S.; Gupta, A.
Purification of recombinant human thyroid peroxidase (hTPO) from AD293 mammalian cells
Int. J. Biol. Macromol.
106
87-94
2018
Homo sapiens
Manually annotated by BRENDA team
Belforte, F.S.; Targovnik, A.M.; Gonzalez-Lebrero, R.M.; Osorio Larroche, C.; Citterio, C.E.; Gonzalez-Sarmiento, R.; Miranda, M.V.; Targovnik, H.M.; Rivolta, C.M.
Kinetic characterization of human thyroperoxidase. Normal and pathological enzyme expression in Baculovirus system a molecular model of functional expression
Mol. Cell. Endocrinol.
404
9-15
2015
Homo sapiens (P07202), Homo sapiens
Manually annotated by BRENDA team
Godlewska, M.; Arczewska, K.; Rudzinska, M.; Lyczkowska, A.; Krasuska, W.; Hanusek, K.; Ruf, J.; Kiedrowski, M.; Czarnocka, B.
Thyroid peroxidase (TPO) expressed in thyroid and breast tissues shows similar antigenic properties
PLoS ONE
12
e0179066
2017
Homo sapiens
Manually annotated by BRENDA team
Caballero, Y.; Lopez-Tomassetti, E.M.; Favre, J.; Santana, J.R.; Cabrera, J.J.; Hernandez, J.R.
The value of thyroperoxidase as a prognostic factor for differentiated thyroid cancer - a long-term follow-up study
Thyroid Res.
8
12
2015
Homo sapiens
Manually annotated by BRENDA team
Rahnama, R.; Mahmoudi, A.R.; Kazemnejad, S.; Salehi, M.; Ghahiri, A.; Soltanghoraee, H.; Vafaei, S.; Rezaei, A.; Zarnani, A.H.
Thyroid peroxidase in human endometrium and placenta a potential target for anti-TPO antibodies
Clin. Exp. Med.
21
79-88
2021
Homo sapiens (P07202), Homo sapiens
Manually annotated by BRENDA team
Williams, D.E.; Le, S.N.; Hoke, D.E.; Chandler, P.G.; Gora, M.; Godlewska, M.; Banga, J.P.; Buckle, A.M.
Structural studies of thyroid peroxidase show the monomer interacting with autoantibodies in thyroid autoimmune disease
Endocrinology
161
1-16
2020
Homo sapiens (P07202)
Manually annotated by BRENDA team
Godlewska, M.; Krasuska, W.; Czarnocka, B.
Biochemical properties of thyroid peroxidase (TPO) expressed in human breast and mammary-derived cell lines
PLoS ONE
13
e0193624
2018
Homo sapiens (P07202), Homo sapiens
Manually annotated by BRENDA team
Lou, Y.; Ji, G.; Liu, Q.; Wang, P.; Zhang, R.; Zhang, Y.; Liu, X.
Secretory expression and scale-up production of recombinant human thyroid peroxidase via baculovirus/insect cell system in a wave-type bioreactor
Protein Expr. Purif.
149
7-12
2018
Homo sapiens (P07202), Homo sapiens
Manually annotated by BRENDA team
Dong, H.; Godlewska, M.; Wade, M.G.
A rapid assay of human thyroid peroxidase activity
Toxicol. In Vitro
62
104662
2020
Homo sapiens (P07202), Homo sapiens
Manually annotated by BRENDA team