Information on EC 1.21.99.3 - thyroxine 5-deiodinase

Word Map on EC 1.21.99.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.21.99.3
-
RECOMMENDED NAME
GeneOntology No.
thyroxine 5-deiodinase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
thyroid hormone metabolism I (via deiodination)
-
-
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 hide
74506-30-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
chondrichthye
UNIPROT
Manually annotated by BRENDA team
strain Hybro
-
-
Manually annotated by BRENDA team
isozyme type III
SwissProt
Manually annotated by BRENDA team
pine snake
UniProt
Manually annotated by BRENDA team
isozyme type III
-
-
Manually annotated by BRENDA team
isozyme type III; tadpole
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
physiological role of thyroid hormones in the regulation of insulin secretion, overview. type 3 iodothyronine deiodinase-mediated thyroid hormone inactivation is thought to participate in glucose-stimulated insulin secretion from beta cellsA cAMP pathway mediates the pretranslational regulation of D3 expression in MIN6 cells
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,3',5'-triido-L-thyronine + AH
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
3,3',5'-triido-L-thyronine + iodide + A + H+
L-thyroxine + AH2
show the reaction diagram
-
assay at pH 7.2
-
-
?
3,3',5'-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
show the reaction diagram
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
L-thyroxine + reduced acceptor
show the reaction diagram
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
show the reaction diagram
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
-
-
?
3,3',5-triiodo-L-thyronine + AH2
?
show the reaction diagram
-
assay at pH 7.0, 37C
-
-
?
3,3',5-triiodo-L-thyronine sulfate + AH2
3,3'-diiodo-L-thyronine sulfate + iodide + A + H+
show the reaction diagram
3,5,3'-triiodo-L-thyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
3,5,3'-triiodo-L-thyronine + AH2
?
show the reaction diagram
-
-
-
?
3,5,3'-triiodothyronine + AH2
3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
radioactive and unlabeled T3,in presence of 1 6-N-propylthiouracil, the products of deiodination are quantified by HPLC
-
-
?
L-3',5'-diiodothyronine + AH2
L-5'-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, reaction of isozyme Dio3
i.e. reverse triiodothyrosine
-
?
L-3,5,3'-triiodothyronine + AH2
L-3,3'-diiodothyronine + iodide + A + H+
show the reaction diagram
-
5-deionination by isozyme Dio1
-
-
?
L-3-iodothyronine + AH2
L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,3',5'-triido-L-thyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+
L-thyroxine + reduced acceptor
show the reaction diagram
3,3',5-triiodo-L-thyronine + AH2
3,3'-diiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,3',5'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,3',5-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
L-thyroxine + AH2
3,5,3'-triiodo-L-thyronine + iodide + A + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
dithiothreitol
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Se
-
selenoenzyme
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
selenium
-
selenoprotein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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 1.97.1.10
(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 1.97.1.10
(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 1.97.1.10
(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 1.97.1.10
(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 1.97.1.10
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 1.97.1.10
3',4',4,6-tetrahydroxyaurone
-
inhibition kinetics; very potent naturally occuring plant-derived inhibitor, conformation study
-
3',5'-diiodothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,3',5'-triiodo-L-thyronine
3,3',5'-triiodothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,3',5,5'-tetraiodo-L-thyronine
3,3',5-triiodo-L-thyronine
3,3'-diiodo-L-thyronine
-
product inhibition, 82% at 0.001 mM
3,5,3'-triiodo-5'-nitrothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5,5'-triiodo-2'-methylthyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5-diiodo-2'-hydroxythyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5-diiodo-3',5'-dinitrothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5-diiodo-3'-hydroxythyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5-diiodo-4'-amino-3',5'-dimethylthyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
3,5-diiodo-L-thyronine
4',4,6-trihydroxyaurone
-
cofactor competitive mechanism, displacement of thyroxine from the binding site of thyroxine-binding prealbumin; inhibition kinetics; very potent naturally occuring plant-derived inhibitor
6-n-propyl-2-thiouracil
type 3 iodothyronine deiodinase is unaffected by PTU
6-Propyl-2-thiouracil
-
aurothioglucose
bromoacetyl-triiodothyronine
-
-
cycloheximide
-
isozyme type III, slight decrease of activity in vivo
ellagic acid
-
-
growth hormone
upregulates the 5-deiodinase mRNA expression in the tail, but downregulates it in the liver
-
iodoacetate
recombinant and native isozyme type III
iopanoic acid
luteolin-7-beta-glucoside
-
-
N-acetyl-3,5,3'-triiodo-5'-nitrothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
N-acetyl-3,5-diiodo-3',5'-dinitrothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
N-acetyl-3,5-diiodo-3'-bromo-5'-nitrothyronine
-
comparison with 5'-deiodinase EC 1.97.1.10
N-bromoacetyl-3,3',5-triiodo-L-thyronine
Phospholipids
prolactin
inhibits the 3,3',5-triiodo-L-thyronine-dependent upregulation of thyroid hormone receptor beta mRNA expression in the tail; inhibits the regression of the tail fin; upregulates the 5-deiodinase mRNA expression in the tail, but downregulates it in the liver
-
propylthiouracil
slight inhibition of recombinant and native isozyme type III
rosmarinic acid
-
-
sodium iodate
-
95% inhibition at 1 mM
Tetraiodothyroacetic acid
-
comparison with 5'-deiodinase EC 1.97.1.10
triiodothyronine
-
-
[4-(4-hydroxy-3,5-diiodophenoxy)phenyl]acetic acid
-
comparison with 5'-deiodinase EC 1.97.1.10
[4-(4-hydroxy-3,5-dinitrophenoxy)-3,5-diiodophenyl]acetic acid
-
comparison with 5'-deiodinase EC 1.97.1.10
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)-3,5-diiodophenyl]acetic acid
-
comparison with 5'-deiodinase EC 1.97.1.10
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)phenyl]acetic acid
-
comparison with 5'-deiodinase EC 1.97.1.10
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoylphorbol-13-acetate
-
induction of isozyme type III from brain astrocytes
3,3',5-triiodo-L-thyronine
-
induces enzyme
acidic fibroblast growth factor
-
actinomycin D
-
induction of isozyme type III from brain astrocytes
basic fibroblast growth factor
-
45fold induction of isozyme type III 5-deiodinase activity in vitro
-
cAMP
-
induction of isozyme type III from brain astrocytes
Epidermal growth factor
fibroblast growth factor
-
induces enzyme
-
growth hormone
slightly upregulates the 5-deiodinase mRNA expression in the tail, but strongly downregulates it in the liver
-
insulin-like growth factor I
-
slight induction of isozyme type III 5-deiodinase activity in vitro
-
Phospholipids
-
no influence on the kinetic parameters of 5-deiodinase activity of isozyme type III in placenta, but essential for activity
platelet-derived growth factor
-
slight induction of isozyme type III 5-deiodinase activity in vitro
-
prolactin
upregulates the 5-deiodinase mRNA expression in the tail, but downregulates it in the liver
-
retinoic acid
-
induction of isozyme type III from brain astrocytes
Se2+
-
required, depletion reversibly reduces the activity of isozyme type III by 3-10fold in cultured brain astrocytes
Vasopressin
-
slight induction of isozyme type III 5-deiodinase activity in vitro
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001 - 0.000011
3,3',5'-triiodo-L-thyronine
0.000001 - 0.0000225
3,3',5-triiodo-L-thyronine
0.0000094 - 0.0000098
3,5,3'-triiodo-L-thyronine
0.003 - 0.57
L-3,5',3'-triiodothyronine
0.0000035 - 0.000265
L-thyroxine
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014 - 0.00017
4',4,6-trihydroxyaurone
4.8
6-Propyl-2-thiouracil
at 30C, at pH 7.0, with 50 mM dithiothreitol
0.000005
N-bromoacetyl-3,3',5-triiodo-L-thyronine
-
isozyme type III; pH 7.2, 37C
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
(2E)-2-(3,4-dihydroxybenzylidene)-4,6-dihydroxy-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37C
0.0005
(2E)-4,6-dihydroxy-2-(4-hydroxy-3-iodobenzylidene)-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37C
0.001
(2E)-4,6-dihydroxy-2-(4-hydroxybenzylidene)-1-benzofuran-3(2H)-one
Rattus norvegicus
-
pH 7.4, 37C
0.005
(4-[(E)-(4,6-dihydroxy-3-oxo-1-benzofuran-2(3H)-ylidene)methyl]phenoxy)acetic acid
Rattus norvegicus
-
pH 7.4, 37C
0.0025
3',5'-diiodothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.006
3,5,3'-triiodo-5'-nitrothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.005
3,5,5'-triiodo-2'-methylthyronine
Rattus norvegicus
-
pH 7.4, 37C
0.01
3,5-diiodo-3',5'-dinitrothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.014
3,5-diiodo-3'-hydroxythyronine
Rattus norvegicus
-
pH 7.4, 37C
0.017
3,5-diiodo-4'-amino-3',5'-dimethylthyronine
Rattus norvegicus
-
pH 7.4, 37C
0.43
aurothioglucose
Rattus norvegicus
-
pH 7.4, 37C
0.001
N-acetyl-3,5,3'-triiodo-5'-nitrothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.006
N-acetyl-3,5-diiodo-3',5'-dinitrothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.003
N-acetyl-3,5-diiodo-3'-bromo-5'-nitrothyronine
Rattus norvegicus
-
pH 7.4, 37C
0.002
Tetraiodothyroacetic acid
Rattus norvegicus
-
pH 7.4, 37C
0.0003
[4-(4-hydroxy-3,5-diiodophenoxy)phenyl]acetic acid
Rattus norvegicus
-
pH 7.4, 37C
0.001
[4-(4-hydroxy-3,5-dinitrophenoxy)-3,5-diiodophenyl]acetic acid
Rattus norvegicus
-
pH 7.4, 37C
0.0008
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)-3,5-diiodophenyl]acetate
Rattus norvegicus
-
pH 7.4, 37C
0.001
[4-(4-hydroxy-3-iodo-5-nitrophenoxy)phenyl]acetic acid
Rattus norvegicus
-
pH 7.4, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000005
-
placental tissue
0.00000024
-
3,3',5-triiodo-L-thyronine 5-deiodination activity, isozyme type III, posterior pituitary gland
0.0000006
-
hemangioma tissue
0.000042
-
isozyme type III, brown adipocyte cell culture, in presence of 10% newborn calf serum, substrate 3,3',5-triiodo-L-thyronine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
isozyme type III, 3,3',5-triiodo-L-thyronine 5-deiodinase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
in presence of ammonium sulfate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cell culture; isozyme type III
Manually annotated by BRENDA team
-
cell culture; isozyme type III
Manually annotated by BRENDA team
-
5-deiodinase activity
Manually annotated by BRENDA team
-
cell culture; isozyme type III
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
-
isozyme Dio3
Manually annotated by BRENDA team
-
of fetal vessels
Manually annotated by BRENDA team
gene expression
Manually annotated by BRENDA team
-
human keratinocyte cell line
Manually annotated by BRENDA team
-
isozyme Dio1
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
larval, primary
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
premetamorphic
Manually annotated by BRENDA team
-
malignant
Manually annotated by BRENDA team
-
isozyme Dio2
Manually annotated by BRENDA team
-
healthy and infarcted
Manually annotated by BRENDA team
organ culture of tadpole tail tips
Manually annotated by BRENDA team
-
isozyme type III
Manually annotated by BRENDA team
of tadpole tail tips
Manually annotated by BRENDA team
-
epithelium
Manually annotated by BRENDA team
-
of nonpregnant human uteri
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme type III
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, isozyme type III, SDS-PAGE
31000
-
x * 31000, SDS-PAGE
32000
x * 32000, isozyme type III, SDS-PAGE
37000
-
2 * 37000, epitope-tagged recombinant protein,SDS-PAGE
50000 - 55000
-
FLAG-tagged recombinant protein, PAGE
65000
-
x * 65000, SDS-PAGE, overexpressed enzyme can homodimerize probably through disulfide bridges
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of the catalytic domain of mouse deiodinase Dio3, to 1.9 A resolution. The catalytic Sec170 is positioned in the loop connecting beta1 to alpha1. It points toward an elongated cleft that likely represents the iodothyronine binding site. The deiodination step follows a selenolate inline attack on the iodine delta-hole weakening the carbon-iodine bond. The abstracted iodonium is replaced by a proton approaching from the opposite side of the ring. The proton is conveyed to the 5-position of the iodothyronine along a triad His219, Glu200, and Ser167, with residues Tyr197 and Thr169 participating in the organization of an intricate H-bond network
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
30 min, inactivation of 5-deiodinase
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, 3fold
-
recombinant from COS-1 cells
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, isozyme type III, an in-frame TGA codon encodes a selenocysteine residue, contains a putative Sec insertion sequence element at 3' UTR, functional expression in COS-1 cells
expressed in Xenopus laevis oocytes
expression in oocytes from Xenopus laevis
expression of RNAi to knock down D3 in transient transfection experiments using G2N2C, Tb3A, and wild type keratinocytes
-
expression of RNAi to knock down type 3 deiodinase 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
isozyme type III, via RT-PCR from cerebellum mRNA, expression in bacteria
-
screening of neonatal skin cDNA library, DNA sequence determination and analysis, isozyme type III, an in-frame TGA codon encodes a selenocysteine residue, functional translation in Xenopus laevis oocytes, catalytis properties of recombinant and native enzyme are identical
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
transfection in HEK 293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decrease postnatally, persisted into adulthood at low levels
expression and activity of type 3 iodothyronine deiodinase are elevated in infantile hepatic hemangioma
-
glucagon-like peptide-1 stimulates type 3 iodothyronine deiodinase expression in Min6 cells in a dose-dependent manner through a GLP-1 receptor-cAMP-PKA-medicated mechanism, and this effect is inhibited by the protein kinase A inhibitor H-89. Exendin-4, a GLP-1 receptor agonist, and forskolin also stimulates type 3 deiodinase expression in MIN6 cells. A cAMP pathway mediates the pretranslational regulation of D3 expression in MIN6 cells
-
high expressio levels in embryos
increase of type 3 deiodinase levels in spinal cord inflammatory lesions, induction of type 3 deiodinase levels in proinflammatory or immunomodulatory monocytes
-
incubation (for 8 h at 37C) of confluent primary cultures of astroglial cells with 0.1 mM ATP causes a 7fold induction of type 3 iodothyronine deiodinase activity. The activity of type 3 iodothyronine deiodinase significantly raises by the influence of 0.001 mM all-trans retinoic acid during preincubation for 2-3 days
-
no influence of peroxiredoxin 3 on expression oftype 3 iodothyronine deiodinase
-
the enzyme activity is increased in kidney, muscle, and liver up to 4fold during fasting
-
the mRNA expression and activity of the zebrafish deiodinase-3 gene is increased locally 1 and 3 days after partial fin amputation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
E200T
-
inactive
S167A
-
about 10% residual activity
Sec170C
-
mutation in active site, crystallization data
T169A
-
inactive
T169S
-
60% of wild-type activity
Y197F
-
inactive
additional information
-
generation of enzyme knockout mice
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
delipidation of microsomes during purification results in loss of enzyme activity. Full recovering of activity is achieved by recombining phospholipids and protein, partial recovery may be achieved by addition of exogenous phospholipids to protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine