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Information on EC 1.11.1.8 - iodide peroxidase and Organism(s) Sus scrofa and UniProt Accession P09933
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1.11.1.8 iodide peroxidaseIUBMB 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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Word Map
- 1.11.1.8
- thyroglobulin
- tsh
- autoimmune
- hypothyroidism
- autoantibody
- thyroxin
- women
- graves
-
tpoabs
- hashimoto
- thyrotropin
-
thyroid-stimulating
- pregnancy
-
subclinical
-
euthyroidism
- triiodothyronine
- goiter
-
follicular
-
overt
- thyrocytes
-
anti-tpo
-
antithyroid
-
symporter
-
organification
-
trimester
- levothyroxine
- autoantigens
-
thyroid-specific
-
frtl-5
- guaiacol
- methimazole
- lactoperoxidase
-
radioiodine
- propylthiouracil
-
goitrous
- thyrotoxicosis
-
antibody-negative
-
multinodular
- analysis
-
peroxidase-catalyzed
-
hypothalamic-pituitary-thyroid
-
ophthalmopathy
-
gadas
-
tsh-induced
-
anti-thyroglobulin
- medicine
-
thyroid-associated
-
tsh-stimulated
- chloroperoxidase
- synthesis
- nodosum
- haloperoxidases
-
thyrotoxic
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide(3 overall reactions are displayed. Show all (5)>>)
Synonyms
thyroid peroxidase, thyroperoxidase, bromoperoxidase, vanadium bromoperoxidase, iodide peroxidase, hrtpo, iodinase, hmw-tpo, tyrosine iodinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
iodide peroxidase-tyrosine iodinase
-
-
-
-
iodinase
-
-
-
-
iodoperoxidase (heme type)
-
-
-
-
thyroid peroxidase
-
-
-
-
thyroperoxidase
-
-
-
-
tyrosine iodinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
iodination
-
-
-
-
peroxidation
-
-
-
-
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
9031-28-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
iodide + H2O2
iodine + H2O
-
highest activity if coupled with glucose-glucose oxidase reaction for H2O2 production
-
?
iodide + H2O2
iodine + H2O
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
-
iodination and coupling reactions of proteins
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
iodide + H2O2
iodine + H2O
-
iodination and coupling reactions of proteins
-
?
iodide + H2O2
iodine + H2O
-
iodination and coupling reactions of proteins
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
rutin
competitive, rutin and quercetin as well as rutin and rosmarinic acid act additively
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cumin ethanol extract
activating, and also acts as effective lipoxygenase inhibitor
-
green coffee ethanol extract
activating, and also acts as effective lipoxygenase inhibitor
-
green tea ethanol extract
activating, and also acts as effective lipoxygenase inhibitor
-
mustard ethanol extract
activating, and also acts as effective lipoxygenase inhibitor
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
traces of activity in liver, kidney, heart, brain, ovary and muscle
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
thyroid peroxidase is the key enzyme involved in thyroid hormone synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PERT_PIG
926
2
100443
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
different molecular weights found after different preparation procedures
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the single nucleotide polymorphism of A642G in the fourteenth exon of TPO gene is significantly associated with ham weight
additional information
-
the single nucleotide polymorphism of A642G in the fourteenth exon of TPO gene is significantly associated with ham weight
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coval, M.L.; Taurog, A.
Purification and iodinating activity of hog thyroid peroxidase
J. Biol. Chem.
242
5510-5523
1967
Sus scrofa
Neary, J.T.; Soodak, M.; Maloof, F.
Iodination by thyroid peroxidase
Methods Enzymol.
107
445-475
1984
Bos taurus, Rattus norvegicus, Sus scrofa
Ohtaki, S.; Nakagawa, H.; Nakamura, S.; Nakamura, M.; Yamazaki, I.
Characterization of hog thyroid peroxidase
J. Biol. Chem.
260
441-448
1985
Sus scrofa
Divi, R.L.; Doerge, D.R.
Inhibition of thyroid peroxidase by dietary flavonoids
Chem. Res. Toxicol.
9
16-23
1996
Sus scrofa
Sugawara, M.; Sugawara, Y.; Wen, K.; Giulivi, C.
Generation of oxygen free radicals in thyroid cells and inhibition of thyroid peroxidase
Exp. Biol. Med.
227
141-146
2002
Sus scrofa
Ruf, J.; Carayon, P.
Structural and functional aspects of thyroid peroxidase
Arch. Biochem. Biophys.
445
269-277
2006
Homo sapiens, Mus musculus, Sus scrofa
Wang, Y.; Zhao, X.; Jiang, X.; Hua, X.; Xu, N.
Molecular characterization of thyroid peroxidase gene in porcine (Sus scrofa)
J. Genet. Genomics
37
381-388
2010
Sus scrofa (P09933), Sus scrofa
Habza-Kowalska, E.; Gawlik-Dziki, U.; Dziki, D.
Mechanism of action and interactions between thyroid peroxidase and lipoxygenase inhibitors derived from plant sources
Biomolecules
9
663
2019
Sus scrofa (P09933)
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