Any feedback?
Information on EC 1.21.99.3 - thyroxine 5-deiodinase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC1.21.99.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.21.99.3 thyroxine 5-deiodinaseIUBMB Comments
The enzyme activity has only been demonstrated in the direction of 5-deiodination. This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine.
Specify your search results
Word Map
- 1.21.99.3
- thyroid
- triiodothyronine
- hypothyroidism
- tsh
-
deiodination
- pituitary
-
euthyroidism
- 3,5,3'-triiodothyronine
- adipose
-
5'-deiodination
- propylthiouracil
- l-thyroxine
-
prohormone
- 3,3',5'-triiodothyronine
- thyrotropin
- selenocysteine
-
selenoproteins
-
selenoenzyme
-
iopanoic
- methimazole
-
dlk1-dio3
-
pituitary-thyroid
- 3,3'-diiodothyronine
- medicine
-
monodeiodination
-
extrathyroidal
-
se-deficient
-
t3-dependent
-
selenium-deficient
-
hypothalamic-pituitary-thyroid
- amiodarone
-
thyroidectomized
-
harderian
-
nonthyroidal
-
thyroxine-binding
-
thyrotropin-releasing
-
thermogenic
-
thyromimetically
-
inner-ring
- 6-n-propyl-2-thiouracil
-
thyroid-stimulating
-
thyrotoxicosis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
5'-deiodinase, type iii deiodinase, type 3 iodothyronine deiodinase, deiodinase 3, t4-5'-deiodinase, type iii iodothyronine deiodinase, dio3b, iodothyronine monodeiodinase, dio3a, deiodinase-3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
deiodinase, thyroxine 5-
-
-
-
-
diiodothyronine 5'-deiodinase
-
-
-
-
iodothyronine 5-deiodinase
-
-
-
-
iodothyronine inner ring monodeiodinase
-
-
-
-
type 3 deiodinase
type III iodothyronine deiodinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor
all 3 isozyme types contain a selenocysteine residue at the active site
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor
inner ring deiodination
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
3,3',5'-triiodo-L-thyronine,iodide:acceptor oxidoreductase (iodinating)
The enzyme activity has only been demonstrated in the direction of 5-deiodination. This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine.
CAS REGISTRY NUMBER
COMMENTARY
74506-30-2
-
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
3,3',5'-triido-L-thyronine + AH
3,3'-diiodothyronine + iodide + A + H+
-
-
-
-
?
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
D3 terminates thyroid hormone action by by inactivating T3
-
-
?
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
L-thyroxine + reduced acceptor
-
-
-
?
L-3',5'-diiodothyronine + AH2
L-5'-iodothyronine + iodide + A + H+
-
phenolic ring deiodination of 3',5'-T2 by Dio2
-
-
?
L-3,5,3',5'-tetraiodothyronine + AH2
L-3,5',3'-triiodothyronine + iodide + A + H+
-
i.e. thyroxine, reaction of isozyme Dio3
i.e. reverse triiodothyrosine
-
?
L-3-iodothyronine + AH2
L-thyronine + iodide + A + H+
-
tyrosyl ring deiodination of 3-iodothyronamine by isozyme Dio3
-
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
-
isozyme type III
-
?
L-thyroxine + reduced acceptor
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
-
-
-
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
-
hormonally inactive
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
best substrate
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
isozyme type III
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
isozyme type III
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
isozyme type III
hormonally inactive
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
selenocysteine residue in the active site is essential for efficient inner ring deiodination
i.e. 3,3'-diiodo-L-thyronine
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
hormonally inactive, i.e. 3,3'-diiodo-L-thyronine
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
i.e. 3,3'-diiodo-L-thyronine
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
preferred substrate
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
isozyme type III
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
isozyme type III
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
isozyme type III
hormonally inactive
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
5-deiodinase activity
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
5-deiodinase activity
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
5-deiodinase activity
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
5-deiodinase activity
hormonally inactive, enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
5-deiodinase activity
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
selenocysteine residue in the active site is absolutely essential for efficient inner ring deiodination
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
enzyme III performs the inactivation of 3,3',5,5'-tetraiodo-L-thyronine
hormonally inactive
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
enzyme performs the inactivation of 3,3',5,5'-tetraiodo-L-thyronine and plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
-
-
?
additional information
?
-
-
isozyme type III predominantly performs 5-deiodination reactions, while isozymes type I and type II perform 5'-deiodination reactions
-
-
?
additional information
?
-
-
isozyme type III is a oncofetal enzyme, regulation
-
-
?
additional information
?
-
-
thyroid hormone is essential for maintaining normal neurological functions both during development and in adult life
-
-
?
additional information
?
-
-
the enzyme is the major physiological inactivator of thyroid hormone. The presence of the enzyme at maternal-fetal interfaces is consistent with its role in modulating the thyroid status of the human fetus and its expression in endometrium suggests that local regulation of thyroid status is important in implantation
-
-
?
additional information
?
-
-
isozyme type III performs the inactivation of 3,3',5,5'-tetraiodo-L-thyronine and enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
-
-
?
additional information
?
-
-
selenium-level of cells influences the enzyme activity
-
-
?
additional information
?
-
-
thyronines and thyronamines are two groups of endogenous iodine-containing signaling molecules that are substrates of three deiodinase isozymes, which catalyze the sequential reductive removal of iodine from the respective precursor molecule. Development of a analytical method applying liquid chromatography/tandem mass spectrometry, overview
-
-
?
additional information
?
-
-
isozyme Dio1 exhibits both phenolic and tyrosyl ring deiodination activity while isozyme Dio2 catalyzes only deiodinations of the phenolic ring, isozyme Dio3 catalyzes only deiodinations of the tyrosyl ring. T3, 3,3'-T2, and 3,5-T2 are also not deiodinated by Dio1 from HepG2 lysates
-
-
?
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
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
L-thyroxine + reduced acceptor
-
-
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
-
isozyme type III
-
?
L-thyroxine + reduced acceptor
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
-
-
-
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
-
hormonally inactive
-
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
selenocysteine residue in the active site is essential for efficient inner ring deiodination
i.e. 3,3'-diiodo-L-thyronine
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
hormonally inactive, i.e. 3,3'-diiodo-L-thyronine
?
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
i.e. 3,3'-diiodo-L-thyronine
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
5-deiodinase activity
hormonally inactive, enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
5-deiodinase activity
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
selenocysteine residue in the active site is absolutely essential for efficient inner ring deiodination
enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
enzyme III performs the inactivation of 3,3',5,5'-tetraiodo-L-thyronine
hormonally inactive
-
?
additional information
?
-
-
isozyme type III is a oncofetal enzyme, regulation
-
-
?
additional information
?
-
-
thyroid hormone is essential for maintaining normal neurological functions both during development and in adult life
-
-
?
additional information
?
-
-
the enzyme is the major physiological inactivator of thyroid hormone. The presence of the enzyme at maternal-fetal interfaces is consistent with its role in modulating the thyroid status of the human fetus and its expression in endometrium suggests that local regulation of thyroid status is important in implantation
-
-
?
additional information
?
-
-
isozyme type III performs the inactivation of 3,3',5,5'-tetraiodo-L-thyronine and enzyme plays a critical role in regulating and maintaining the local 3,3',5-triiodo-L-thyronine content
-
-
?
additional information
?
-
-
thyronines and thyronamines are two groups of endogenous iodine-containing signaling molecules that are substrates of three deiodinase isozymes, which catalyze the sequential reductive removal of iodine from the respective precursor molecule. Development of a analytical method applying liquid chromatography/tandem mass spectrometry, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Se2+
the enzyme is a selenoenzyme encoded by the DIO3 gene. The DIO3 genomic structure contains a single exon and, at the 3'-UTR, a specific RNA structure, named SECIS (selenocysteine insertion element), that is crucial for the insertion of the selenocysteine residue and for maximal enzymatic catalytic efficiency. The DIO3 gene is imprinted, with preferential expression of the paternal allele. It belongs to a cluster of imprinted regions, at the DLK1-DIO3 locus
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3',5-triiodo-L-thyronine
-
substrate inhibition of isozyme type III, complete inhibition at 25 nM
additional information
-
no inhibition of 5-deiodinase activity by propylthiouracil
-
additional information
-
3,3',5-triiodo-L-thyronine sulfate has no effect on isozyme type III in hippocampus up to 100 nM
-
additional information
-
expression and function of the 5-deiodinase and 5-deiodinase isozymes are sensitive to thyroid hormone status, various cytokines and growth factors, severe illness, reactive oxygen species, a variety of hormones and signaling compounds, circadian rythm, and pharmacological agents, and therefore might be useful in sensor function of physiology and pathophysiology
-
additional information
-
decrease of deiodination about 50% in cells with knockdown of peroxiredoxin 3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression and function of 5-deiodinase are sensitive to thyroid hormone status, various cytokines and growth factors, severe illness, reactive oxygen species, a variety of hormones and signaling compounds, circadian rythm, and pharmacological agents
-
additional information
-
interaction with peroxiredoxin 3, rate-limiting role in regeneration of type 3 iodothyronine deiodinase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000028
3,3',5-triiodo-L-thyronine
native wild-type, pH 7.2, 37°C, in presence of 1 mM DTT
0.0000031
3,3',5-triiodo-L-thyronine
recombinant wild-type, pH 7.2, 37°C, in presence of 0.3 mM DTT
0.0000042
3,3',5-triiodo-L-thyronine
recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 0.3 mM DTT
0.0000035
L-thyroxine
recombinant wild-type, pH 7.2, 37°C, in presence of 3 mM DTT
0.000008
L-thyroxine
native wild-type, pH 7.2, 37°C, in presence of 10 mM DTT
0.000265
L-thyroxine
recombinant mutant SeC144C, pH 7.2, 37°C, in presence of 1 mM DTT
additional information
additional information
-
review on enzyme and 5-deiodinase isoforms type I and II
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
3,3',5,5'-tetraiodo-L-thyronine 5-deiodinase activity in brain carcinoma types
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
not: kidney, healthy adult liver, pituitary gland, thyroid gland
additional information
the enzyme is prevalently expressed in many fetal tissues, through the adult it is expressed in placenta, brain, and skin, and to a lesser extent in the pregnant uterus and pancreatic B-cells. The enzyme activity increases rapidly during the proliferative phase of hemangioma
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
type 3 deiodinase is the cause of consumptive hypothyroidism, a clinical entity which often requires close cooperation between clinical endocrinologists, pediatricians, and oncologists, pathology, detailed overview
physiological function
physiological function
the enzyme is active in local deiodination processes, it degrades T4 and T3 into inactive metabolites and is thus the major physiological thyroid hormone inactivator, overview. The enzyme plays a relevant role in pregnancy, the enzyme activity in the maternal-fetal unit locally converts most of the T4 derived from the mother into rT3. The enzyme is involved in consumptive hypothyroidism, overview. Pregnancy can be considered a physiological form of compensated consumptive hypothyroidism, in which the physiologically increased expression of the enzyme increases the inactivation rate of maternal T4 thereby enhancing the need for thyroid hormone
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). IOD3_HUMAN
304
1
33947
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
-
x * 65000, SDS-PAGE, overexpressed enzyme can homodimerize probably through disulfide bridges
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
x * 65000, SDS-PAGE, overexpressed enzyme can homodimerize probably through disulfide bridges
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SeC144A
site-directed mutagenesis, exchange of the selenocysteine residue in the highly conserved active site sequence, enzymatically inactive
SeC144C
site-directed mutagenesis, exchange of the selenocysteine residue in the highly conserved active site sequence, 5fold increased Km for 3,3',5-triiodo-L-thyronine and 100fold increased Km for 3,3',5,5'-tetraiodo-L-thyronine compared to the wild-type, 2-6fold reduced turnover
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of RNAi to knock down D3 in transient transfection experiments using G2N2C, Tb3A, and wild type keratinocytes
-
isozyme type III, expression of wild-type and active site mutants in COS cells, 50fold higher expression level for the mutants than for the wild-type enzyme
the enzyme is a selenoenzyme encoded by the DIO3 gene, localized on chromosome 14q32, in humans. The DIO3 genomic structure contains a single exon and, at the 3'-UTR, a specific RNA structure, named SECIS (selenocysteine insertion element), that is crucial for the insertion of the selenocysteine residue and for maximal enzymatic catalytic efficiency. The DIO3 gene is imprinted, with preferential expression of the paternal allele. It belongs to a cluster of imprinted regions, at the DLK1-DIO3 locus
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression and activity of type 3 iodothyronine deiodinase are elevated in infantile hepatic hemangioma
-
no influence of peroxiredoxin 3 on expression oftype 3 iodothyronine deiodinase
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
expression and function of the 5-deiodinase and 5-deiodinase isozymes are sensitive to thyroid hormone status, various cytokines and growth factors, severe illness, reactive oxygen species, a variety of hormones and signaling compounds, circadian rythm, and pharmacological agents, and therefore might be useful in sensor function of physiology and pathophysiology
medicine
-
sonic hedgehog pathway plays a critical role in hair follicle physiology and is constitutively active in basal cell carcinomas, induces D3 in proliferating keratinocytes and in BCCs through Gli2, reversing this T3 deficiency may be a therapeutic approach for BCCs and perhaps other D3-expressing tumors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Visser, T.J.; Schoenmakers, C.H.
Characteristics of type III iodothyronine deiodinase
Acta Med. Austriaca
19 Suppl 1
18-21
1992
Gallus gallus, Homo sapiens, Platyrrhini, Lithobates catesbeianus, Rattus norvegicus
Mori, K.; Yoshida, K.; Kayama, T.; Kaise, N.; Fukazawa, H.; Kiso, Y.; Kikuchi, K.; Aizawa, Y.; Abe, K.
Thyroxine 5-deiodinase in human brain tumors
J. Clin. Endocrinol. Metab.
77
1198-1202
1993
Homo sapiens
Santini, F.; Pinchera, A.; Ceccarini, G.; Castagna, M.; Rosellini, V.; Mammoli, C.; Montanelli, L.; Zucchi, V.; Chopra, I.J.; Chiovato, L.
Evidence for a role of the type III-iodothyronine deiodinase in the regulation of 3,5,3'-triiodothyronine content in the human central nervous system
Eur. J. Endocrinol.
144
577-583
2001
Homo sapiens
Koehrle, J.
Iodothyronine deiodinases
Methods Enzymol.
347
125-167
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, vertebrata
Kuiper, G.G.; Klootwijk, W.; Visser, T.J.
Substitution of cysteine for selenocysteine in the catalytic center of type III iodothyronine deiodinase reduces catalytic efficiency and alters substrate preference
Endocrinology
144
2505-2513
2003
Homo sapiens (P55073), Homo sapiens
Curcio-Morelli, C.; Gereben, B.; Zavacki, A.M.; Kim, B.W.; Huang, S.; Harney, J.W.; Larsen, P.R.; Bianco, A.C.
In vivo dimerization of types 1, 2, and 3 iodothyronine selenodeiodinases
Endocrinology
144
937-946
2003
Homo sapiens
Huang, S.A.; Dorfman, D.M.; Genest, D.R.; Salvatore, D.; Larsen, P.R.
Type 3 iodothyronine deiodinase is highly expressed in the human uteroplacental unit and in fetal epithelium
J. Clin. Endocrinol. Metab.
88
1384-1388
2003
Homo sapiens
Dentice, M.; Luongo, C.; Huang, S.; Ambrosio, R.; Elefante, A.; Mirebeau-Prunier, D.; Zavacki, A.M.; Fenzi, G.; Grachtchouk, M.; Hutchin, M.; Dlugosz, A.A.; Bianco, A.C.; Missero, C.; Larsen, P.R.; Salvatore, D.
Sonic hedgehog-induced type 3 deiodinase blocks thyroid hormone action enhancing proliferation of normal and malignant keratinocytes
Proc. Natl. Acad. Sci. USA
104
14466-14471
2007
Homo sapiens, Mus musculus
Aerts, G.; Arrojo E Drigo, R.; Van Herck, S.L.; Sammels, E.; Mirebeau-Prunier, D.; Gereben, B.; Zeoeld, A.; Harney, J.W.; Huang, S.A.; Mulcahey, M.A.; Van der Geyten, S.; Van den Bergh, G.; Arckens, L.; Darras, V.M.; Zavacki, A.M.
Knockdown of the type 3 iodothyronine deiodinase (D3) interacting protein peroxiredoxin 3 decreases D3-mediated deiodination in intact cells
Endocrinology
150
5171-5180
2009
Homo sapiens
Bessho, K.; Etani, Y.; Ichimori, H.; Miyoshi, Y.; Namba, N.; Yoneda, A.; Ooue, T.; Chihara, T.; Morii, E.; Aoki, T.; Murakami, M.; Mushiake, S.; Ozono, K.
Increased type 3 iodothyronine deiodinase activity in a regrown hepatic hemangioma with consumptive hypothyroidism
Eur. J. Pediatr.
169
215-221
2009
Homo sapiens
Piehl, S.; Heberer, T.; Balizs, G.; Scanlan, T.S.; Kohrle, J.
Development of a validated liquid chromatography/tandem mass spectrometry method for the distinction of thyronine and thyronamine constitutional isomers and for the identification of new deiodinase substrates
Rapid Commun. Mass Spectrom.
22
3286-3296
2008
Homo sapiens, Mus musculus
Luongo, C.; Trivisano, L.; Alfano, F.; Salvatore, D.
Type 3 deiodinase and consumptive hypothyroidism: a common mechanism for a rare disease
Front. Endocrinol. (Lausanne)
4
115
2013
Homo sapiens (P55073)
EXTERNAL LINKS (specific for EC-Number 1.21.99.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
