Information on EC 1.11.1.8 - iodide peroxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.11.1.8
-
RECOMMENDED NAME
GeneOntology No.
iodide peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O
show the reaction diagram
(1)
-
-
-
2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H2O
show the reaction diagram
(4)
-
-
-
[thyroglobulin]-3-iodo-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O
show the reaction diagram
(3)
-
-
-
[thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H2O
show the reaction diagram
(5)
-
-
-
[thyroglobulin]-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O
show the reaction diagram
(2)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
iodination
-
-
-
-
oxidation
-
-
-
-
peroxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
thyroid hormone biosynthesis
-
Tyrosine metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bromoperoxidase
-
-
DEHAL1
-
-
high-molecular weight-thyroid peroxidase
-
-
HMW-TPO
-
-
hrTPO
-
-
hTPO
-
-
iodide peroxidase-tyrosine iodinase
-
-
-
-
iodinase
-
-
-
-
iodoperoxidase (heme type)
-
-
-
-
iodotyrosine deiodase
-
-
-
-
iodotyrosine deiodinase
-
-
-
-
iodotyrosine deiodinase
-
-
monoiodotyrosine deiodinase
-
-
-
-
thyroid peroxidase
-
-
-
-
thyroid peroxidase
-
-
thyroid peroxidase
-
-
thyroperoxidase
-
-
-
-
thyroperoxidase
-
-
thyroperoxidase
-
-
TPO
-
-
TPOX
-
-
tyrosine iodinase
-
-
-
-
vanadium bromoperoxidase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9031-28-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
patients with hypothyroidism who have features suggestive of an iodotyrosine deiodinase defect for mutations in DEHAL1
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
two isoforms found
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
the enzyme catalyzes the transfer of iodine to thyroglobulin during thyroid hormone synthesis
physiological function
P09933
thyroid peroxidase is the key enzyme involved in thyroid hormone synthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
biochanin A + H2O2 + I-
6,8-diiodobiochanin A + H2O
show the reaction diagram
-
-
-
?
Br- + H2O2 + thymol blue
?
show the reaction diagram
-
ordered two-substrate mechanism
-
-
?
Br- + H2O2 + thymol blue
dibromothymolsulfonphthalein + ?
show the reaction diagram
-
-
-
-
?
diiodotyrosine + H2O2 + I-
?
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2 + H+
3,3'-dimethoxy-4,4'-biphenochinone + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2 + I-
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2 + I-
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
-
guaiacol + H2O2 + I-
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2 + I-
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
-
I- + H2O2
triiodide + ?
show the reaction diagram
-
-
-
-
?
I- + H2O2 + thymol blue
diiodothymolsulfonphthalein + ?
show the reaction diagram
-
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
highest activity if coupled with glucose-glucose oxidase reaction for H2O2 production
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
autoantigenin autoimmune thyroid disease
-
?
o-dianisidine
?
show the reaction diagram
-
-
-
-
?
tyrosine + H2O2 + I-
monoiodotyrosine + diiodotyrosine + H2O
show the reaction diagram
-
-
-
-
?
tyrosine + H2O2 + I-
monoiodotyrosine + diiodotyrosine + H2O
show the reaction diagram
-
-
ratio 1:4
?
monoiodotyrosine + H2O2 + I-
monoiodotyrosine + diiodotyrosine + H2O
show the reaction diagram
-
-
90% diiodotyrosine, 6% monoiodotyrosine, determined using radioactive I-
?
additional information
?
-
-
amino acids from TPO region 713-717 are the key residues, recognized by IDR/B-specific anti-TPO autoantibodies in autoimmune thyroid disease
-
-
-
additional information
?
-
-
several changes in ultracytochemical characteristics of the enzyme are associated with thyroid disease
-
-
-
additional information
?
-
-
hypothyroid dwarfism due to the missense mutation R479C of the thyroid peroxidase gene in the mouse
-
-
-
additional information
?
-
-
H353, D358, S359 and R361 are amino acid residues contributing to the binding of anti-TPO autoantibodies in the immunodominant regions
-
-
-
additional information
?
-
-
protein radical formation on thyroid peroxidase during turnover
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
-
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
biosynthesis of thyroid hormones
-
?
iodide + H2O2
iodine + H2O
show the reaction diagram
-
autoantigenin autoimmune thyroid disease
-
?
additional information
?
-
-
amino acids from TPO region 713-717 are the key residues, recognized by IDR/B-specific anti-TPO autoantibodies in autoimmune thyroid disease
-
-
-
additional information
?
-
-
several changes in ultracytochemical characteristics of the enzyme are associated with thyroid disease
-
-
-
additional information
?
-
-
hypothyroid dwarfism due to the missense mutation R479C of the thyroid peroxidase gene in the mouse
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
heme
-
enzyme contains heme
protoheme
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-Methyl-2-mercaptoimidazole
-
competitive with iodide
2,2',4,4'-tetrahydroxybenzophenone
-
inhibits enzyme activity by more than 60% from 0.00001 to 0.1 mM
3,4,5-hydroxybenzoic acid propyl ester
-
mixed type inhibition
3-methylchloranthracene
-
-
-
Aminotriazole
-
-
Aminotriazole
-
very strong
arsenic trioxide
-
0.1 ppm arsenic trioxide has no effect on TPO activity, incubation for 2 min in the presence of 1.0, 5.0, or 10 ppm arsenic trioxide inhibits TPO activity to 4%, 9%, and 9% of control, respectively. After 10 min incubation in the presence of 1.0 or 5.0 ppm arsenic trioxide, TPO activity returns to 92% and 54% of control, respectively, while the presence of 10 ppm arsenic trioxide further inhibits TPO activity to 1% of control
azide
-
very effective
azide
-
non competitive with H2O2
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
-
-
cyanide
-
competitive with H2O2
cysteine
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
fisetin
-
-
genistein
-
inhibits enzyme activity by about 40% at 0.001 and 0.01 mM
glutathione
-
-
glutathione
-
-
H2O2
-
above 0.00065 mM
H2O2
-
inactivation is prevented by iodide
heptachlor
-
weakly inhibits the enzyme activity by about 50% at 0.01 mM
histidine
-
-
Iodide
-
above 0.1 mM at pH 5, no inhibition at pH 7
kaempferol
-
-
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
-
enzyme activity is reduced by more than 70% by 0.1 and 1 mM
myricetin
-
non competitive with I-
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
Naringenin
-
non competitive with I-, competitive with H2O2
p-Aminobenzoic acid
-
-
perfluorooctane sulfonate
-
-
Perfluorooctanoic acid
-
slight inhibition at 0.01 mM
phenylalanine
-
-
propylthiouracil
-
-
quercetin
-
-
resorcinol
-
-
sulfathiazole
-
-
sunitinib
-
sunitinib is a tyrosine kinase inhibitor with antitumor and antiangiogenic effects. Its antithyroid effect appears to be inhibition of peroxidase
Thiocyanate
-
competitive with iodide
thiouracil
-
-
Thiourea
-
-
Thiourea
-
weak
tryptophan
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
methionine
-
complete inhibition at 0.05 mM, reversible by increasing I- concentration
additional information
-
no inhibition with sulfhydryl reacting reagents and p-chloromercuribenzoate
-
additional information
-
inhibited by hydrolyzed enzyme preparation, hydrolyzed bovine serum albumin and casein, guaiacol oxidation not significantly affected by amino acids
-
additional information
-
inhibited by quinones at concentration above 0.01 mM
-
additional information
-
CHO cells cultured in methimazole for days show a 58-82% reduction in high molecular weight-thyroid peroxidase isoforms at methimazole concentrations of 0.001-0.5 mM, whereas monomeric thyroid peroxidase expression is unchanged. A similar reduction in thyroid peroxidase expression (34-74%) is observed in CHO cells cultured in propylthiouracil (0.01-0.5 mM)
-
additional information
-
2,3,4-trihydroxybenzophenone, 2,4,4'-trihydroxybenzophenone, 4-hydroxybenzophenone, 2-hydroxy-4-methoxybenzophenone, chrysene, naphthalene, benzo(a)anthracene, phenanthrene, hexachlorobenzene, mirex, chlordane, and methylmercury have no effect on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
22
-
Br-
-
; in phosphate buffer (100 mM, pH 8.0), at 20°C
0.034
-
H2O2
-
-
0.18
-
I-
-
in phosphate buffer (100 mM, pH 8.0), at 20°C
0.25
-
I-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
71
-
Br-
-
; in phosphate buffer (100 mM, pH 8.0), at 20°C
75
-
I-
-
in phosphate buffer (100 mM, pH 8.0), at 20°C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0009
-
3,4,5-hydroxybenzoic acid propyl ester
-
-
0.001
0.008
azide
-
depending on substrate
0.009
-
cyanide
-
-
0.006
-
kaempferol
-
-
0.013
-
morin
-
-
0.001
-
myricetin
-
-
0.007
-
Naringenin
-
-
0.007
-
quercetin
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00197
-
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
0.00188
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
31
-
-
-
32
-
-
purified enzyme
138
-
-
purified enzyme with guaiacol as substrate
381
-
-
purified enzyme with guaiacol as substrate
464
-
-
with guaiacol as substrate
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
additional information
-
-
an accurate and sensitive colorimetric assay for the titration of haloperoxidase activities is developed. The method is based on the specific increase in absorbance at 620 nm that occurs on the halogenation of thymol blue. The quantitative determination of both iodo- and bromoperoxidase activities with the same assay is now possible
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
iodide oxidation
7.4
-
-
guaiacol oxidation
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
7.5
-
20% of activity at pH 2.5, 70% at pH 7.5
5
7
-
activity independent of pH
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
IL-1alpha/IFNgamma-induced down-regulation of thyroperoxidase is not affected by Th3 cytokines
Manually annotated by BRENDA team
-
IL-1alpha/IFNgamma-induced down-regulation of thyroperoxidase is not affected by Th3 cytokines
Manually annotated by BRENDA team
-
thyroid follicular cell, when thyrocytes are treated with IL-1alpha/IFNgamma thyroperoxidase expression is hindered, the viability of thyrocytes is not affected
Manually annotated by BRENDA team
-
thyroid follicular cell, some TPO-specific T cells and the majority of autoantibodies in humans develop in response to TPO presented by thyroid cells, rather than to TPO released by damaged thyrocytes
Manually annotated by BRENDA team
-
pathological tissue: Hashimoto‘s thyroiditis, Graves‘ disease, multinodular goiter, no activity in papillary carcinoma
Manually annotated by BRENDA team
-
of patients with diverse thyroid diseases
Manually annotated by BRENDA team
-
toxic diffuse goiter tissue samples obtained during thyroidectomies
Manually annotated by BRENDA team
-
TPO activities are similar between pre-pubertal and adult female rats. Estradiol administration does not change enzyme activity in pre-pubertal rats, while in intact adults activity is increased by low or high doses of estradiol
Manually annotated by BRENDA team
-
some TPO-specific T cells and the majority of autoantibodies in humans develop in response to TPO presented by thyroid cells, rather than to TPO released by damaged thyrocytes
Manually annotated by BRENDA team
-
lesion, negative correlation between thyroperoxidase and dual oxidase H2O2-generating activities
Manually annotated by BRENDA team
additional information
-
traces of activity in liver, kidney, heart, brain, ovary and muscle
Manually annotated by BRENDA team
additional information
-
papillary carcinoma are negative for TPO
Manually annotated by BRENDA team
additional information
-
recombinant TPO stably transfected into the human follicular thyroid carcinoma cell line FTC-238
Manually annotated by BRENDA team
additional information
-
genomic DNA is isolated from peripheral blood
Manually annotated by BRENDA team
additional information
-
smoking is negatively associated with the presence of thyroid peroxidase autoantibody in serum
Manually annotated by BRENDA team
additional information
-
not detected in dermal fibroblasts, HaCaT cells, and melanoma cell lines
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
integral membrane protein
Manually annotated by BRENDA team
-
integral membrane protein
Manually annotated by BRENDA team
-
of Graves‘ disease thyroid, enzyme is absent in the microvilli in multinodular goiter
Manually annotated by BRENDA team
-
Hashimoto‘s thyroiditis and oncocytic adenoma, are typically packed with mitochondria, display TPO reaction exclusivly in mitochondrial crisae
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. 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
-
mutant enzymes D574/L575del, G553C and G771R expressed to varying degree on the plasma membrane. Mutant R665W shows no cell surface localization
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
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
64000
-
-
gel filtration, analytical ultracentrifugation
71000
-
-
HPLC gel filtration
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
100000
-
-
SDS-PAGE, gel filtration
100000
-
-
SDS-PAGE, isoform 2
105000
-
-
SDS-PAGE
105000
-
-
SDS-PAGE, isoform 1
105000
-
-
SDS-PAGE
105000
-
-
double band of MW 97000; SDS-PAGE
135000
-
-
gel filtration, Triton solubilized enzyme
220000
240000
-
the high-molecular weight-thyroid peroxidase is in the 220000-240000 Da range, SDS-PAGE
additional information
-
-
different molecular weights found after different preparation procedures
additional information
-
-
conformational dominant epitopes on thyroid peroxidase recognized by human autoantibodies
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
-
2 * 110000, SDS-PAGE
homodimer
-
2 * 107600, calculated from SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
contains 10% carbohydrate, and four of the five potential glycosylation sites are actually occupied by oligosaccharide units in which mannose and glucosamine are either the sole sugars, or the main ones present
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
25
-
stable at room temperature at pH 4 for 40 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sensitive to pronase treatment
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-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
-
–18°C or -4°C, enzyme retains its immunoreactivity
-
-20°C, 4 years, no loss of activity
-
-20°C, 6-12 months, no loss of activity
-
-70°C, several months, no loss of activity of partially purified enzyme
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; ammonium sulfate precipitation and phenyl-Sepharose column chromatography
-
partial
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 Chinese hamster ovary (CHO) cells
-
stable expression of mutant enzymes at the surface of CHO cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thyroid-stimulating hormone (10 mUI/ml, for 24 h) does not affect TPO mRNA level
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
G533C
-
expressed to some extent on the cell surface, prolongation in kinetics, increasing interaction with calnexin
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
G771R
-
expressed to some extent on the cell surface, prolongation in kinetics, increasing interaction with calnexin
additional information
-
H353, D358, S359 and R361 are amino acid residues contributing to the binding of anti-TPO autoantibodies in the immunodominant regions
additional information
-
two patients with iodide organification defect caused by two compound heterozygous mutations, c.215delA/c.2422T-->C [p.Q72fsX86/p.C808R] and c.387delC/c.1159G-->A [p.N129fsX208/p.G387R], in the TPO gene and four patients with monoallelic TPO defect. Identification of the molecular basis of this disorder might be helpful for understanding the pathophysiology of congenital hypothyroidism
R479C
-
a novel hypothyroid dwarfism due to the missense mutation R479C of the thyroid peroxidase gene in the mouse
additional information
P09933
the single nucleotide polymorphism of A642G in the fourteenth exon of TPO gene is significantly associated with ham weight
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
development of an ELISA system for quantitative determination of TPO 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
medicine
-
amino acids from TPO region 713-717 are the key residues, recognized by IDR/B-specific anti-TPO autoantibodies in autoimmune thyroid disease. These data are of great importance to rationally design therapeutic peptides able to block undesired autoimmune responses
medicine
-
R646 and D707 together with R225 constitute a functional epitope within IDR-A, and that residues E604, D620, and D630, together with K627, constitute a functional epitope within IDR-B. The identification of key residues within the autoreactive epitopes will help in understanding the structural basis for the breakdown of immune tolerance to TPO in thyroid autoimmune disease
medicine
-
two patients with iodide organification defect caused by two compound heterozygous mutations, c.215delA/c.2422T-->C [p.Q72fsX86/p.C808R] and c.387delC/c.1159G-->A [p.N129fsX208/p.G387R], in the TPO gene and four patients with monoallelic TPO defect. Identification of the molecular basis of this disorder might be helpful for understanding the pathophysiology of congenital hypothyroidism
medicine
-
identification of TPO gene defects in a cohort of patients with thyroid dyshormonogenesis from Slovenia, Bosnia, and Slovakia. The high percentage of single allele mutations implies possible intronic or regulatory TPO gene mutations or monoallelic expression
medicine
-
identification of defects in DEHAL1 that produce a phenotype of severe hypothyroidism, goiter, excessive levels of iodotyrosine in serum and urine, and variable mental deficits derived from unrecognized hypothyroidism