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Information on EC 1.21.99.4 - thyroxine 5'-deiodinase and Organism(s) Rattus norvegicus and UniProt Accession P70551
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1.21.99.4 thyroxine 5'-deiodinaseIUBMB 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.
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Word Map
- 1.21.99.4
- thyroid
- triiodothyronine
- hypothyroidism
- tsh
-
deiodination
- adipose
- pituitary
- selenium
-
euthyroidism
-
selenoproteins
- 3,5,3'-triiodothyronine
- thyrotropin
-
prohormone
-
thermogenesis
-
selenoenzyme
- propylthiouracil
-
photoperiodic
- hypothalamic
-
hypothalamic-pituitary-thyroid
- selenocysteine
-
thyroid-stimulating
-
thyrotropin-releasing
-
iopanoic
-
thermogenic
- iodotyrosine
-
hypophysiotropic
-
t3-dependent
-
polybrominated
-
extrathyroidal
-
hypothyroxinemia
- 3,3',5-triiodothyronine
-
thyroxine-binding
-
mediobasal
-
pbdes
-
5'-deiodination
-
iodine-deficient
- tanycytes
- tuberalis
-
debromination
-
selenocysteine-containing
-
trbeta
- methimazole
- thyrotoxicosis
-
hormone-activating
- thyroperoxidase
-
monocarboxylate
-
nonthyroidal
-
secis
- levothyroxine
- medicine
-
selenium-deficient
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5DI
-
-
-
-
5DII
-
-
-
-
5DIII
-
-
-
-
diiodothyronine 5'-deiodinase
-
-
-
-
DIOI
-
-
-
-
DIOII
-
-
-
-
DIOIII
-
-
-
-
iodothyronine outer ring monodeiodinase
-
-
-
-
L-thyroxine iodohydrolase (reducing)
-
-
-
-
thyroxine 5-deiodinase
-
-
-
-
Thyroxine deiodinase
-
-
-
-
Type 1 DI
-
-
-
-
Type 2 DI
-
-
-
-
Type 3 DI
-
-
-
-
Type-I 5'deiodinase
-
-
-
-
Type-II 5'deiodinase
-
-
-
-
Type-III 5'deiodinase
-
-
-
-
XL-15
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3,3',5-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor
isozyme type I, reaction mechanism, both 5-deiodinase isoforms and 5-deiodinase contain a selenocysteine residue at the active site
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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
70712-46-8
-
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'-triiodo-L-thyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
-
-
-
-
?
3,3',5'-triiodothyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
-
substrate for type 1 iodothyronine deiodinase
-
-
?
3,3',5-triiodo-L-thyronine sulfate + reduced electron acceptor
diiodothyronine + iodide + electron acceptor
-
-
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
isozymes type II and I, production of 3,3',5-triiodo-L-thyronine
hormonally inactive
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
-
-
from microsomal enzyme complex, 3,3',5-triiodo-L-thyronine is thyromimetically active
-
?
L-thyroxine + AH2
3,3',5-triiodothyronine + iodide + A + H+
in kidney and liver cells the enzyme can serve as an enzymic barrier to the entry of the prohormone thyroxine and the source of bioactive 3,3',5-triiodothyronine for the cell
-
-
?
L-thyroxine + electron acceptor
3,3',5-triiodothyronine + iodide + reduced electron acceptor
-
-
-
?
additional information
?
-
-
L-hormone analogues are preferentially deiodinated via the T4-5'-deiodination pathway, whereas D-analogues produce products via the T4-5-deiodination pathway
-
-
?
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
isozyme type I
-
-
?
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
isozyme type I: degradation of 3,3',5'-triiodo-L-thyronine
hormonally inactive
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
-
-
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
isozyme type II
hormonally active
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
addition of I125 labelled T4 to measure the production of T3, using paper chromatography
-
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
substrate for type 2 iodothyronine deiodinase
-
-
?
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 + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
-
isozyme type I
-
-
?
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
-
-
-
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
-
isozymes type II and I, production of 3,3',5-triiodo-L-thyronine
hormonally inactive
-
?
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
-
-
from microsomal enzyme complex, 3,3',5-triiodo-L-thyronine is thyromimetically active
-
?
L-thyroxine + AH2
3,3',5-triiodothyronine + iodide + A + H+
in kidney and liver cells the enzyme can serve as an enzymic barrier to the entry of the prohormone thyroxine and the source of bioactive 3,3',5-triiodothyronine for the cell
-
-
?
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
-
-
-
-
?
additional information
?
-
-
L-hormone analogues are preferentially deiodinated via the T4-5'-deiodination pathway, whereas D-analogues produce products via the T4-5-deiodination pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithioerythritol
-
can be substituted by dithiothreitol, isozyme type II, 5-20 mM, isozyme type I, 2-5 mM
additional information
-
no activity with glutathione or thioredoxin in vivo, isozyme type I
-
dithiothreitol
-
can be substituted by dithioerythritol, isozyme type II, 5-20 mM, isozyme type I, 2-5 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-2-(3,4-dihydroxybenzylidene)-4,6-dihydroxy-1-benzofuran-3(2H)-one
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
(2E)-2-(3,4-dihydroxybenzylidene)-6-hydroxy-1-benzofuran-3(2H)-one
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
(2E)-4,6-dihydroxy-2-(4-hydroxy-3-iodobenzylidene)-1-benzofuran-3(2H)-one
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
(2E)-4,6-dihydroxy-2-(4-hydroxybenzylidene)-1-benzofuran-3(2H)-one
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
(4-[(E)-(4,6-dihydroxy-3-oxo-1-benzofuran-2(3H)-ylidene)methyl]phenoxy)acetic acid
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
2-(3,4-dihydroxybenzyl)-4,6-dihydroxy-1-benzofuran-3(2H)-one
-
aurone derivative isolated from plant extract. Comparison with inhibition of 5-deiodinase EC 1.97.1.11
2-amino-3-[4-[(4-hydroxy-3,5-diiodophenyl)thio]-3,5-diiodophenyl]propanoic acid
-
comparison with 5-deiodinase EC 1.97.1.11
3,3',5,5'-tetraiodo-L-thyronine
-
hypoxia has no effect on inhibition of T4
3,5,3'-triiodo-5'-nitrothyronine
-
comparison with 5-deiodinase EC 1.97.1.11
3,5,5'-triiodo-2'-methylthyronine
-
comparison with 5-deiodinase EC 1.97.1.11
3,5-diiodo-3',5'-dinitrothyronine
-
comparison with 5-deiodinase EC 1.97.1.11
3,5-diiodo-4'-amino-3',5'-dimethylthyronine
-
comparison with 5-deiodinase EC 1.97.1.11
ethyl 4-(4-hydroxy-3,5-diiodobenzoyl)phenyl carbonate
-
comparison with 5-deiodinase EC 1.97.1.11
N-acetyl-3,5,3'-triiodo-5'-nitrothyronine
-
comparison with 5-deiodinase EC 1.97.1.11
N-acetyl-3,5-diiodo-3',5'-dinitrothyronine
-
comparison with 5-deiodinase EC 1.97.1.11
N-acetyl-3,5-diiodo-3'-bromo-5'-nitrothyronine
-
comparison with 5-deiodinase EC 1.97.1.11
[4-(4-hydroxy-3,5-diiodophenoxy)phenyl]acetic acid
-
comparison with 5-deiodinase EC 1.97.1.11
[4-(4-hydroxy-3,5-dinitrophenoxy)-3,5-diiodophenyl]acetic acid
-
comparison with 5-deiodinase EC 1.97.1.11
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)-3,5-diiodophenyl]acetic acid
-
comparison with 5-deiodinase EC 1.97.1.11
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)phenyl]acetic acid
-
comparison with 5-deiodinase EC 1.97.1.11
additional information
-
lipopolysaccharide-induced type 2 deiodinase activity is not inhibited by 1 mM 6-propyl-2-thiouracil
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
propranolol
propanolol does not prevent muscle Dio2 induction, but impairs a decrease of Dio2 in the brown adipose tissue and soleus after 10 days at 4°C
carbobenzoxy-L-leucyl-L-leucyl-L-leucinal
-
MG132, proteasome inhibitor, increases type 2 deiodinase
forskolin
-
increases mRNA expression and type 2 deiodinase activity, hypoxia stimulates forskolin induces activation of type 2 deiodinase
additional information
in red oxidative soleus muscle, isoform Dio2 activity increases 2.3fold after 3 days at 4°C together with the brown adipose tissue Dio2 activity, which increases 10fold. Soleus muscle and the brown adipose tissue Dio2 activities return to the control levels after 10 days of cold exposure, when an increase of 2.8fold in Dio2 activity is detected in white glycolytic gastrocnemius but not in red oxidative gastrocnemius fibers. Propranolol does not prevent muscle Dio2 induction, but it impairs the decrease of Dio2 in the brown adipose tissue and soleus after 10 days at 4°C. Serum total and free T3 is increased during cold exposure in rats
-
additional information
-
hypoxia activates type 2 deiodinase by a posttranslational mechanism, glucose depletion decrased hypoxia induced type 2 deiodinase activation, agents promoting hypoxia like desferrioxamine, dimethyloxalylglycine, diethylsuccinatecobalt chloride activate type 2 deiodinase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme G2A, duplicate determination give the values: 0.0015 mM and 0.0024 mM
0.002
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme S176A, duplicate determination give the values: 0.002 mM and 0.0024 mM
0.002
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme S176A, duplicate determination give the values: 0.0024 mM and 0.0024 mM
0.002
3,3',5-triiodo-L-thyronine sulfate
mutant enzymes, in which selenocysteine residues in the core catalytic center is replaced by cysteine
0.0022
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme S101A, duplicate determination give the values: 0.0022 mM and 3.2 mM
0.0024
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme G2A, duplicate determination give the values: 0.0015 mM and 0.0024 mM
0.0028
3,3',5-triiodo-L-thyronine sulfate
native enzyme from rat liver microsomes
0.0032
3,3',5-triiodo-L-thyronine sulfate
mutant enzyme S101A, duplicate determination give the values: 0.0022 mM and 0.0032 mM
additional information
additional information
mutant enzymes S101A/S176A and Y209F/Y217F show KM-values above 0.005 mM
-
additional information
additional information
-
review on enzyme isoforms type I and II and 5-deiodinase, type III
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(2E)-2-(3,4-dihydroxybenzylidene)-4,6-dihydroxy-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37°C
0.01
(2E)-2-(3,4-dihydroxybenzylidene)-6-hydroxy-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37°C
0.0005
(2E)-4,6-dihydroxy-2-(4-hydroxy-3-iodobenzylidene)-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37°C
0.001
(2E)-4,6-dihydroxy-2-(4-hydroxybenzylidene)-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37°C
0.005
(4-[(E)-(4,6-dihydroxy-3-oxo-1-benzofuran-2(3H)-ylidene)methyl]phenoxy)acetic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.008
2-(3,4-dihydroxybenzyl)-4,6-dihydroxy-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37°C
0.003
2-amino-3-[4-[(4-hydroxy-3,5-diiodophenyl)thio]-3,5-diiodophenyl]propanoate
Rattus norvegicus
-
-
0.0015
[4-(4-hydroxy-3,5-dinitrophenoxy)-3,5-diiodophenyl]acetic acid
Rattus norvegicus
-
pH 7.4, 37°C
0.0005
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)-3,5-diiodophenyl]acetate
Rattus norvegicus
-
pH 7.4, 37°C
0.0008
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)phenyl]acetic acid
Rattus norvegicus
-
pH 7.4, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
after 10 days of cold exposure an increase of 2.8fold in Dio2 activity is detected in white glycolytic gastrocnemius but not in red oxidative gastrocnemius fibers
in red oxidative soleus muscle, isoform Dio2 activity increases 2.3fold after 3 days at 4°C together with the brown adipose tissue Dio2 activity, which increases 10fold. Soleus muscle and the brown adipose tissue Dio2 activities return to the control levels after 10 days of cold exposure
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
membrane association is not essential for maintenance of functional activity
-
integral membrane protein. Once assembled the D1 holoenzyme is sorted to the plasma membrane in both kidney and liver cells, where it can serve as an enzymic barrier to the entry of the prohormone thyroxine and the source of bioactive 3,3',5-triiodothyronine for the cell
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in red oxidative soleus muscle, isoform Dio2 activity increases 2.3fold after 3 days at 4°C together with the brown adipose tissue Dio2 activity, which increases 10fold. Soleus muscle and the brown adipose tissue Dio2 activities return to the control levels after 10 days of cold exposure, when an increase of 2.8fold in Dio2 activity is detected in white glycolytic gastrocnemius but not in red oxidative gastrocnemius fibers. Propranolol does not prevent muscle Dio2 induction, but it impairs the decrease of Dio2 in the brown adipose tissue and soleus after 10 days at 4°C. Serum total and free T3 is increased during cold exposure in rats
physiological function
-
brain D2 is implicated in adaptative responses to infectious stress
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). IOD2_RAT
266
0
29871
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
heterogeneity is not caused by N-linked glycosylation, but probably by a combination of O-linked glycosylation and phosphorylation
phosphoprotein
heterogeneity is not caused by N-linked glycosylation, but probably by a combination of O-linked glycosylation and phosphorylation
additional information
-
both type I and type II enzyme as well as type III enzyme EC 1.97.1.11 are selenoproteins. All tissues studied maintain more than 50% deiodinase activity during prolonged selenium-deficiency. Only when selenium levels decrease by more than 80%, deiodinase activity markedly decreases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N94Q/N203Q
increase in Km-value for 3,3',5-triiodo-L-thyronine sulfate
S101A
Km-value for 3,3',5-triiodo-L-thyronine sulfate is nearly identical
S101A/S176A
increase in Km-value for 3,3',5-triiodo-L-thyronine sulfate
Y209F/Y217F
increase in Km-value for 3,3',5-triiodo-L-thyronine sulfate
additional information
mutant enzymes, in which selenocysteine residues in the core catalytic center is replaced by cysteine, shows a 10fold increase in Km-value for 3,3',5-triiodo-L-thyronine sulfate. Deletion of the endoplasmic reticulum (ER)-signal sequence and the membrane-spanning domain, amino acids 2-35, does not result in the production of a soluble type I-like enzyme. This mutant protein is inactive but is still membrane-bound
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, presence of 3 mM dithiothreitol, stable for at least 6 weeks, after 3 months, loss of55% of activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of mutant enzymes, in which selenocysteine residues in the core catalytic center is replaced by cysteine, in Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bacterial lipopolysaccharide induces type 2 iodothyronine deiodinase (D2) activity with a lag-time of 4-8 h and a maximum at 24 h at 0.001 mg /ml. Glucocorticoids (0.001 mM cortisol, 10 nM dexamethasone) enhance both the basal and LPS-stimulated D2 activity and mRNA accumulation. RU486 and sulfasalazine block the effects of lipopolysaccharide on both D2 activity and mRNA accumulation. In astrocytes, co-expression of p65 nuclear factor-kappaB with the 3.8 kb form of the rat dio2 promoter leads to a 7fold increase in the transcriptional activity
-
enzyme expression is significantly attenuated in all tissue homogenates of ovarectomized rats
-
increased local generation of triiodothyronine in prostate might be related to the differentiation, maturation that occurs at puberty, and, or, the energy expenditure associated with maintaining the secretory activity of the glandular epithelium
-
incubation (for 2-12 h at 37°C) of confluent primary cultures of astroglial cells, maintained in a chemically defined medium devoid of growth factors and hormones, with various concentrations of adenosine, AMP, ADP, ATP (highest activity at 0. 1 mM after 4 h), and a series of their analogues causes a marked induction of type 2 iodothyronine deiodinase activity (up to 30fold basal level). Preincubation of cells with all-trans-retinoic acid multiplies the inducing effect of the purines (up to 42fold increase of type 1 iodothyronine deiodinase); all-trans retinoic acid itself enhances the activity of type 2 iodothyronine deiodinase, and also of type 1 iodothyronine deiodinase, only a little
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
food restriction leads to reduced liver type 1 deiodinase activity, administration of 3,3,5,5-tetraiodo-L-thyronine restores type 1 deiodinase activity and promotes body protein loss
additional information
-
type 2 deiodinase is inactivated via WSB-1 mediated ubiquination but can be rescued from proteasomal degradation by USP-33 mediated deubiquination, expression of WSB-1 and USP-33 underlie cell specific posttranslational control of type 2 deiodinase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koehrle, J.; Auf'mkolk, M.; Rokos, H.; Hesch, R.D.; Cody, V.
Rat liver iodothyronine monodeiodinase. Evaluation of the iodothyronine ligand-binding site
J. Biol. Chem.
261
11613-11622
1986
Rattus norvegicus
Auf'mkolk, M.; Koehrle, J.; Hesch, R.D.; Cody, V.
Inhibition of rat liver iodothyronine deiodinase. Interaction of aurones with the iodothyronine ligand-binding site
J. Biol. Chem.
261
11623-11630
1986
Rattus norvegicus
Auf dem Brinke, D.; Hesch, R.D.; Khrle, J.
Re-examination of the subcellular localization of thyroxine 5-deiodination in rat liver
Biochem. J.
180
273-279
1979
Rattus norvegicus
Santini, F.; Chopra, I.J.; Hurd, R.E.; Solomon, D.H.; Chua Teco, G.N.
A study of the characteristics of the rat placental iodothyronine 5'-monodeiodinase: evidence that it is distinct from the rat hepatic iodothyronine 5'-monoiodinase
Endocrinology
130
2325-2332
1992
Rattus norvegicus
Bates, J.M.; Spate, V.L.; Morris, J.S.; St.Germain, D.L.; Galton, V.A.
Effects of selenium deficiency on tissue selenium content, deiodinase activity, and thyroid hormone economy in the rat during development
Endocrinology
141
2490-2500
2000
Rattus norvegicus
Koehrle, J.
Iodothyronine deiodinases
Methods Enzymol.
347
125-167
2002
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, vertebrata
Leonard, J.L.; Visser, T.J.; Leonard, D.M.
Characterization of the subunit structure of the catalytically active type I iodothyronine deiodinase
J. Biol. Chem.
276
2600-2607
2001
Rattus norvegicus (P24389)
Kuiper, G.G.; Klootwijk, W.; Visser, T.J.
Expression of recombinant membrane-bound type I iodothyronine deiodinase in yeast
J. Mol. Endocrinol.
34
865-878
2005
Rattus norvegicus (P24389)
Lamirand, A.; Mercier, G.; Ramauge, M.; Pierre, M.; Courtin, F.
Hypoxia stabilizes type 2 deiodinase activity in rat astrocytes
Endocrinology
148
4745-4753
2007
Rattus norvegicus
Fekete, C.; Freitas, B.C.; Zeoeld, A.; Wittmann, G.; Kadar, A.; Liposits, Z.; Christoffolete, M.A.; Singru, P.; Lechan, R.M.; Bianco, A.C.; Gereben, B.
Expression patterns of WSB-1 and USP-33 underlie cell-specific posttranslational control of type 2 deiodinase in the rat brain
Endocrinology
148
4865-4874
2007
Rattus norvegicus
Araujo, R.L.; de Andrade, B.M.; de Figueiredo, A.S.; da Silva, M.L.; Marassi, M.P.; Pereira, V.d.o.s..S.; Bouskela, E.; Carvalho, D.P.
Low replacement doses of thyroxine during food restriction restores type 1 deiodinase activity in rats and promotes body protein loss
J. Endocrinol.
198
119-125
2008
Rattus norvegicus
Lopez-Juarez, A.; Delgado, G.; Aceves, C.; Anguiano, B.
Type 1 deiodinase activity and generation of triiodothyronine (T3) in prostate of sexually active rats
Prostate
69
1651-1659
2009
Rattus norvegicus
Lamirand, A.; Ramauge, M.; Pierre, M.; Courtin, F.
Bacterial lipopolysaccharide induces type 2 deiodinase in cultured rat astrocytes
J. Endocrinol.
208
183-192
2012
Rattus norvegicus
Pavelka, S.
Radiometric enzyme assays: development of methods for extremely sensitive determination of types 1, 2 and 3 iodothyronine deiodinase enzyme activities
J. Radioanal. Nucl. Chem.
286
861-865
2010
Rattus norvegicus
-
Louzada, R.A.; Santos, M.C.; Cavalcanti-de-Albuquerque, J.P.; Rangel, I.F.; Ferreira, A.C.; Galina, A.; Werneck-de-Castro, J.P.; Carvalho, D.P.
Type 2 iodothyronine deiodinase is upregulated in rat slow- and fast-twitch skeletal muscle during cold exposure
Am. J. Physiol. Endocrinol. Metab.
307
E1020-E1029
2014
Rattus norvegicus (P70551)
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