Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.21.99.4 - thyroxine 5'-deiodinase and Organism(s) Homo sapiens and UniProt Accession P49895

for references in articles please use BRENDA:EC1.21.99.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active. The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics. For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P49895
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
deiodinase, type 2 deiodinase, type 3 deiodinase, iodothyronine 5'-deiodinase, type 2 iodothyronine deiodinase, type 1 deiodinase, thyroxine 5'-deiodinase, type i iodothyronine deiodinase, type ii iodothyronine deiodinase, type 1 iodothyronine deiodinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
type 1 iodothyronine deiodinase
-
type I iodothyronine deiodinase
-
types 1 iodothyronine selenodeiodinase
-
5DI
-
-
-
-
5DII
-
-
-
-
5DIII
-
-
-
-
D1 5'-deiodinase
-
-
D2 5'-deiodinase
-
-
deiodinase
-
-
diiodothyronine 5'-deiodinase
-
-
-
-
DIOI
-
-
-
-
DIOII
-
-
-
-
DIOIII
-
-
-
-
ID-2
-
-
ID-3
-
-
iodothyronine deiodinase D2
-
-
iodothyronine outer ring monodeiodinase
-
-
-
-
L-thyroxine iodohydrolase (reducing)
-
-
-
-
thyroxine 5-deiodinase
-
-
-
-
Thyroxine deiodinase
-
-
-
-
type 1 5'-deiodinase
-
-
type 1 deiodinase
-
-
Type 1 DI
-
-
-
-
type 1 iodothyronine deiodinase
-
-
type 2 5'-deiodinase
-
-
type 2 deiodinase
Type 2 DI
-
-
-
-
type 2 iodothyronine deiodinase
type 3 deiodinase
-
-
Type 3 DI
-
-
-
-
type I iodothyronine deiodinase
-
-
type II iodothyronine deiodinase
-
Type-I 5'deiodinase
-
-
-
-
Type-II 5'deiodinase
-
-
-
-
Type-III 5'deiodinase
-
-
-
-
types 2 iodothyronine selenodeiodinase
-
XL-15
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
deiodination
-
-
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, which renders the thyroid hormone more active. The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics. For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
CAS REGISTRY NUMBER
COMMENTARY hide
70712-46-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
activation and deactivation of thyroid hormone
-
-
r
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
show the reaction diagram
3,3',5'-triiodothyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
3,3',5-triiodothyronine + AH2
diiodothyronine + iodide + A + H+
show the reaction diagram
rT3 ORD activity
-
-
?
L-3,5',3'-triiodothyronine + AH2
L-3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
5'-deionination by isozyme Dio1
-
-
?
L-3,5'-diiodothyronine + AH2
L-3-iodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
L-3,5,3',5'-tetraiodothyronine + AH2
L-3,5,3'-triiodothyronine + iodide + A + H+
show the reaction diagram
-
i.e. thyroxine
triiodothyrosine, a small 3,3'-T2 peak also occurs
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,3',5-triiodothyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + reduced acceptor
3,3',5-triiodo-L-thyronine + iodide + acceptor + H+
show the reaction diagram
reverse triiodothyronine + AH2
diiodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
r
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
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
activation and deactivation of thyroid hormone
-
-
r
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
show the reaction diagram
-
isozyme type I
-
-
?
3,3',5'-triiodothyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
-
-
from microsomal enzyme complex, 3,3',5-triiodo-L-thyronine is thyromimetically active
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + reduced acceptor
3,3',5-triiodo-L-thyronine + iodide + acceptor + H+
show the reaction diagram
-
-
-
-
?
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 hide
LITERATURE
IMAGE
dithioerythritol
-
-
dithiothreitol
glutathione
-
20 mM glutathione is used in assay conditions
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,3',5'-triiodo-L-thyronine
-
-
aurothioglucose
gold thioglucose
-
iodoacetate
-
iopanoic acid
-
both isozyme type I and type II
propylthiouracil
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Bu)2cAMP
forskolin
-
significantly stimulates deiodinating activity in TT cells
Se2+
-
severe selenium deficiency leads to a decrease in activity of isozyme type I in liver, kidney, and several other organs, but not in the thyroid gland, the central nervous system, and several other endrocrine organs
additional information
-
expression and function of the 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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
3,3',5'-triiodothyronine
0.003 - 0.57
L-3,5',3'-triiodothyronine
0.0000000017 - 0.0066
L-thyroxine
0.00000101 - 0.0000098
reverse triiodothyronine
0.00003
thyroxine
-
additional information
additional information
-
review on enzyme isoforms type I and II and 5-deiodinase, type III
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000000041
-
medullary thyroid carcinoma
0.00000000043
-
normal thyroid tissue
0.0000000058
-
normal tissues
0.0000000286
-
normal tissues
0.0000000429
-
McCune-Albright syndrome patients
0.0000000543
-
toxic adenoma patient
0.0000000714
-
toxic adenoma patient
0.0000001857
-
McCune-Albright syndrome patients
0.000001
-
healthy control
0.0000025
-
patient with mutation in thyroglobulin gene
0.0001
-
isoenzyme type I
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
activity assay
7.4
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
hepatocellular carcinoma
Manually annotated by BRENDA team
-
isozyme type I
Manually annotated by BRENDA team
-
isozyme Dio3
Manually annotated by BRENDA team
expression of type 2 iodothyronine deiodinase D2, which converts T4 to T3, and TR1 in HUVECs
Manually annotated by BRENDA team
-
isozyme type I
Manually annotated by BRENDA team
-
thyroid tissue samples are collected from five patients, three affected by toxic nodule, and from areas of normal thyroid parenchyma from five patients undergoing total thyroidectomy for thyroid cancer
Manually annotated by BRENDA team
additional information
-
severe selenium deficiency leads to a decrease in activity of isozyme type I in liver, kidney, and several other organs, but not in the thyroid gland, the central nervous system, and several other endrocrine organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
convert prohormone T4 to biologicalliy active T3
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IOD1_HUMAN
249
1
28924
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
x * 55000, SDS-PAGE, overexpressed enzyme can homodimerize probably through disulfide bridges. Monomeric form is also catalytically active
62000
x * 62000, SDS-PAGE, overexpressed enzyme can homodimerize probably through disulfide bridges. Monomeric form is also catalytically active
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
?
-
x * 28000, SDS-PAGE
dimer
additional information
-
substrate binding unit type I 31 kD
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A131C
similar Km-values for L-thyroxine and 3,3',5-triiodothyronine as the wild-type enzyme. Mutation improves the interaction with the reducing cofactor dithiothreitol
A131S
similar Km-values for L-thyroxine and 3,3',5-triiodothyronine as the wild-type enzyme. Mutation improves the interaction with the reducing cofactor dithiothreitol
P135S
-
the mutant type 2 iodothyronine deiodinase has many type 1 iodothyronine deiodinase-like properties, a Km (L-thyroxine) in the micromolar range, ping-pong kinetics with dithiothreitol, and sensitivity to 6n-propylthiouracil in vitro. When the P135S mutant is expressed in HEK-293 cells and exposed to 2-200 pM free L-thyroxine, the rate of L-thyroxine to 3,5,3'-triiodo-L-thyronine conversion is identical with type 2 iodothyronine deiodinase and conversion is insensitive to 6n-propylthiouracil. Using glutathione as a cofactor in vitro results in a marked decrease in the Km (L-thyroxine) (as also occurs for type 1 iodothyronine deiodinase), it shows sequential kinetics with L-thyroxine and is sensitive to 6n-propylthiouracil but is resistant when HEK-293 cytosol is used as a cofactor
SeC133A
inactive mutant enzyme
SeC133C
SeC133C/A131C
mutant enzyme with more than 1000fold increase in Km-value for L-thyroxine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sephadex LH20 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
different splicing variants of DOI1 are cloned into the vector pGEM-T for sequencing, 11 variants are identified
expression in HEK-293 cells
transfection in HEK 293 cells
expression in COS cells
expression in HEK-293 cells
into a D10 vector
-
isozyme type I, mapping on chromosome 1p32-p33, DNA sequence analysis
-
the P135S mutant enzyme is expressed in HEK-293 cells
-
transfection in HEK 293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3,5,3'-triiodothyronine decreases mRNA levels in TT cell, addition of thyroxine or 3,3',5'-triiodothyronine decreases the deiodinating activity
-
5'-deiodinase is increased in McCune-Albright syndrome-associated hyperthyroidism pathogenesis
-
an increase in enzyme expression is observed in Liver X receptor alpha-stimulated cells
-
growth hormone significantly increases iodothyronine deiodinase D2 expression at the mRNA level in HTC/C3 cells
-
substrate-dependent down-regulation, WSB-1-mediated ubiquitination inactivates the enzyme and targets it for proteasomal degradation, TEB4 interacts with the enzyme and mediates loss of activity and protein
-
the enzymatic activity of type 1 iodothyronine deiodinase is low in liver hemangioma
-
there is no significant difference between the thyroidal type 2 iodothyronine deiodinase mRNA level in patients with with 3,5,3'-triiodothyronine-predominant Graves' disease and that in patients with common type-Graves' disease
-
thyroidal type 1 iodothyronine deiodinase mRNA level and activity in patients with 3,5,3'-triiodothyronine-predominant Graves' disease is significantly higher than that in patients with common type-Graves' disease
-
ubiquitinated enzyme can be reactivated and rescued from proteosomal degradation by the von Hippel-Lindau protein-interacting deubiquitinating enzyme-1, TEB4 knockdown increases activity and protein level of iodothyronine deiodinase 2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, J.; Koenig, R.J.
Regulation of hepatocyte thyroxine 5'-deiodinase by T3 and nuclear receptor coactivators as a model of the sick euthyroid syndrome
J. Biol. Chem.
275
38296-38301
2000
Homo sapiens, Mus musculus, Rattus sp.
Manually annotated by BRENDA team
Garcia-Macias, J.F.; Molinero, P.; Guerrero, J.M.; Osuna, C.
Expression of type II thyroxine 5'-deiodinase from rat harderian gland in Xenopus laevis oocytes
FEBS Lett.
354
110-112
1994
Homo sapiens, Rattus sp.
Manually annotated by BRENDA team
Santini, F.; Chopra, I.J.; Hurd, R.E.; Chua Teco, G.N.
A study of the characteristics of hepatic iodothyronine 5'-monodeiodinase in various vertebrate species
Endocrinology
131
830-834
1992
Bos taurus, Cavia porcellus, Gallus gallus, Ovis aries, Homo sapiens, Mus musculus, Rattus sp., Sus scrofa
Manually annotated by BRENDA team
Koehrle, J.
Iodothyronine deiodinases
Methods Enzymol.
347
125-167
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, vertebrata
Manually annotated by BRENDA team
Steinsapir, J.; Bianco, A.C.; Buettner, C.; Harney, J.; Larsen, P.R.
Substrate-induced down-regulation of human type 2 deiodinase (hD2) is mediated through proteasomal degradation and requires interaction with the enzyme's active center
Endocrinology
141
1127-1135
2000
Homo sapiens (Q92813), Homo sapiens
Manually annotated by BRENDA team
Buettner, C.; Harney, J.W.; Larsen, P.R.
The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase
Endocrinology
141
4606-4612
2000
Homo sapiens (Q92813), Homo sapiens
Manually annotated by BRENDA team
Kuiper, G.G.; Klootwijk, W.; Visser, T.J.
Substitution of cysteine for a conserved alanine residue in the catalytic center of type II iodothyronine deiodinase alters interaction with reducing cofactor
Endocrinology
143
1190-1198
2002
Homo sapiens (Q92813), Homo sapiens
Manually annotated by BRENDA team
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 (P49895), Homo sapiens (Q92813), Homo sapiens
Manually annotated by BRENDA team
Curcio, C.; Baqui, M.M.; Salvatore, D.; Rihn, B.H.; Mohr, S.; Harney, J.W.; Larsen, P.R.; Bianco, A.C.
The human type 2 iodothyronine deiodinase is a selenoprotein highly expressed in a mesothelioma cell line
J. Biol. Chem.
276
30183-30187
2001
Homo sapiens (Q92813), Homo sapiens
Manually annotated by BRENDA team
Kanou, Y.; Hishinuma, A.; Tsunekawa, K.; Seki, K.; Mizuno, Y.; Fujisawa, H.; Imai, T.; Miura, Y.; Nagasaka, T.; Yamada, C.; Ieiri, T.; Murakami, M.; Murata, Y.
Thyroglobulin gene mutations producing defective intracellular transport of thyroglobulin are associated with increased thyroidal type 2 iodothyronine deiodinase activity
J. Clin. Endocrinol. Metab.
92
1451-1457
2007
Homo sapiens
Manually annotated by BRENDA team
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 (P49895), Homo sapiens (Q92813)
Manually annotated by BRENDA team
Celi, F.S.; Coppotelli, G.; Chidakel, A.; Kelly, M.; Brillante, B.A.; Shawker, T.; Cherman, N.; Feuillan, P.P.; Collins, M.T.
The role of type 1 and type 2 5-deiodinase in the pathophysiology of the 3,5,3-triiodothyronine toxicosis of McCune-Albright syndrome
J. Clin. Endocrinol. Metab.
93
2383-2389
2008
Homo sapiens
Manually annotated by BRENDA team
Zavacki, A.M.; Arrojo E Drigo, R.; Freitas, B.C.; Chung, M.; Harney, J.W.; Egri, P.; Wittmann, G.; Fekete, C.; Gereben, B.; Bianco, A.C.
The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase
Mol. Cell. Biol.
29
5339-5347
2009
Homo sapiens
Manually annotated by BRENDA team
Meyer, E.L.; Goemann, I.M.; Dora, J.M.; Wagner, M.S.; Maia, A.L.
Type 2 iodothyronine deiodinase is highly expressed in medullary thyroid carcinoma
Mol. Cell. Endocrinol.
289
16-22
2008
Homo sapiens
Manually annotated by BRENDA team
Piekielko-Witkowska, A.; Master, A.; Wojcicka, A.; Boguslawska, J.; Brozda, I.; Tanski, Z.; Nauman, A.
Disturbed expression of type 1 iodothyronine deiodinase splice variants in human renal cancer
Thyroid
19
1105-1113
2009
Homo sapiens (P49895), Homo sapiens
Manually annotated by BRENDA team
Goto, K.; Sonoda, D.; Shimada, K.; Sase, S.; Kawashima, T.
Modeling of the 5'-deiodination of thyroxine by iodothyronine deiodinase: Chemical corroboration of a selenenyl iodide intermediate
Angew. Chem.
49
545-547
2010
Homo sapiens
Manually annotated by BRENDA team
Manna, D.; Mugesh, G.
A chemical model for the inner-ring deiodination of thyroxine by iodothyronine deiodinase
Angew. Chem.
49
9246-9249
2010
Homo sapiens
-
Manually annotated by BRENDA team
Kornasiewicz, O.; Debski, M.; Stepnowska, M.; Sza?as, A.; Bar-Andziak, E.; Krawczyk, M.
The enzymatic activity of type 1 iodothyronine deiodinase (D1) is low in liver hemangioma: a preliminary study
Arch. Immunol. Ther. Exp.
58
77-80
2010
Homo sapiens
Manually annotated by BRENDA team
Goemann, I.; Gereben, B.; Harney, J.; Zhu, B.; Maia, A.; Larsen, P.
Substitution of serine for proline in the active center of type 2 iodothyronine deiodinase substantially alters its in vitro biochemical properties with dithiothreitol but not its function in intact cells
Endocrinology
151
821-829
2010
Homo sapiens
Manually annotated by BRENDA team
Ito, M.; Toyoda, N.; Nomura, E.; Takamura, Y.; Amino, N.; Iwasaka, T.; Takamatsu, J.; Miyauchi, A.; Nishikawa, M.
Type 1 and type 2 iodothyronine deiodinases in the thyroid gland of patients with 3,5,3'-triiodothyronine-predominant Graves' disease
Eur. J. Endocrinol.
164
95-100
2011
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kornasiewicz, O.; Debski, M.; Grat, M.; Lenartowicz, B.; Stepnowska, M.; Szalas, A.; Bar-Andziak, E.; Krawczyk, M.
Enzymatic activity of type 1 iodothyronine deiodinase in selected liver tumors
Arch. Med. Sci.
10
801-805
2014
Homo sapiens (P49895), Homo sapiens
Manually annotated by BRENDA team
Aoki, T.; Tsunekawa, K.; Araki, O.; Ogiwara, T.; Nara, M.; Sumino, H.; Kimura, T.; Murakami, M.
Type 2 iodothyronine deiodinase activity is required for rapid stimulation of PI3K by thyroxine in human umbilical vein endothelial cells
Endocrinology
156
4312-4324
2015
Homo sapiens (Q9C0K2), Homo sapiens
Manually annotated by BRENDA team
Yamauchi, I.; Sakane, Y.; Yamashita, T.; Hirota, K.; Ueda, Y.; Kanai, Y.; Yamashita, Y.; Kondo, E.; Fujii, T.; Taura, D.; Sone, M.; Yasoda, A.; Inagaki, N.
Effects of growth hormone on thyroid function are mediated by type 2 iodothyronine deiodinase in humans
Endocrine
59
353-363
2018
Homo sapiens
Manually annotated by BRENDA team
Poplawski, P.; Rybicka, B.; Boguslawska, J.; Rodzik, K.; Visser, T.J.; Nauman, A.; Piekielko-Witkowska, A.
Induction of type 1 iodothyronine deiodinase expression inhibits proliferation and migration of renal cancer cells
Mol. Cell. Endocrinol.
442
58-67
2017
Homo sapiens
Manually annotated by BRENDA team
Sakane, Y.; Kanamoto, N.; Yamauchi, I.; Tagami, T.; Morita, Y.; Miura, M.; Sone, M.; Yasoda, A.; Kimura, T.; Nakao, K.; Inagaki, N.
Regulation of type 1 iodothyronine deiodinase by LXRalpha
PLoS ONE
12
e0179213
2017
Homo sapiens
Manually annotated by BRENDA team
Poplawski, P.; Wisniewski, J.; Rijntjes, E.; Richards, K.; Rybicka, B.; Kohrle, J.; Piekielko-Witkowska, A.
Restoration of type 1 iodothyronine deiodinase expression in renal cancer cells downregulates oncoproteins and affects key metabolic pathways as well as anti-oxidative system
PLoS ONE
12
e0190179
2017
Homo sapiens
Manually annotated by BRENDA team