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Information on EC 1.21.1.1 - iodotyrosine deiodinase
for references in articles please use BRENDA:EC1.21.1.1
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EC Tree 1 Oxidoreductases
1.21 Catalysing the reaction X-H + Y-H = X-Y
1.21.1 With NAD+ or NADP+ as acceptor
1.21.1.1 iodotyrosine deiodinase
IUBMB Comments
The enzyme activity has only been demonstrated in the direction of 3-deiodination. Present in a transmembrane flavoprotein. Requires FMN.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.21.1.1
- thyroid
- iodide
-
deiodination
- hypothyroidism
- diiodotyrosine
- thyroglobulin
-
dehalogenation
-
halotyrosines
-
iodothyronine
- nitroreductase
- goiter
-
bromo
-
chlorotyrosine
-
organification
- diagnostics
- synthesis
- medicine
Reaction Schemes
show+
2
+
2
=
+
2
+
2
Synonyms
iodotyrosine deiodinase, dehal1, sup-18, dehal1 protein, iodotyrosine dehalogenase 1, nadh oxidase/flavin reductase, dehal1b, sup-18 iyd, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.22.1.1
-
-
formerly
-
IYD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-iodo-L-tyrosine + NADP+ + iodide = 3,5-diiodo-L-tyrosine + NADPH + H+
(1b)
-
-
-
L-tyrosine + 2 NADP+ + 2 iodide = 3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
overall reaction
-
-
-
L-tyrosine + NADP+ + iodide = 3-iodo-L-tyrosine + NADPH + H+
(1a)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NADP+:L-tyrosine oxidoreductase (iodinating)
The enzyme activity has only been demonstrated in the direction of 3-deiodination. Present in a transmembrane flavoprotein. Requires FMN.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-iodophenol + NADP+ + iodide
?
Substrates: 2-iodophenol binds very weakly to the enzyme and is dehalogenated with a catalytic efficiency that is more than 4 orders of magnitude lower than that for 3-iodo-L-tyrosine
Products: -
Products: -
?
3-bromo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + Br-
-
Substrates: -
Products: -
Products: -
?
3-chloro-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + Cl-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + iodide
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 bromide
3,5-dibromo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds
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r
L-tyrosine + 2 NADP+ + 2 chloride
3,5-dichloro-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: chlorotyrosine reacts with the reduced enzyme approximately 20fold more slowly than bromo- and iodotyrosine and reveals a spectral intermediate that forms at approximately the same rate as the bromo- and iodotyrosine reactions
Products: -
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r
3,5-diiodo-L-tyrosine + dithionite
3-iodo-L-tyrosine + ? + I-
-
Substrates: solubilized enzyme preparations are active with dithionite, but not with NADPH. Particle-bound enzyme uses both dithionite and NADPH. At concentrations of substrate below 1 microM, 3,5-diiodo-L-tyrosine is more rapidly deiodinated than 3-iodo-L-tyrosine, which is reversed at concentrations greater than 5 microM
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Products: -
?
3,5-diiodo-L-tyrosine + dithionite
3-iodo-L-tyrosine + ? + I-
Substrates: -
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Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
-
Substrates: -
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Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
-
Substrates: solubilized enzyme preparations are active with dithionite, but not with NADPH. Particle-bound enzyme uses both dithionite and NADPH. At concentrations of substrate below 1 microM, 3,5-diiodo-L-tyrosine is more rapidly deiodinated than 3-iodo-L-tyrosine, which is reversed at concentrations greater than 5 microM
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Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
Substrates: substrate 3-iodo-L-tyrosine is preferred over 3,5-diiodotyrosine
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Products: -
?
3-bromo-L-tyrosine + NADP+ + bromide
3,5-dibromo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-bromo-L-tyrosine + NADP+ + bromide
3,5-dibromo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-chloro-L-tyrosine + NADP+ + chloride
3,5-dichloro-L-tyrosine + NADPH + H+
Substrates: -
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Products: -
?
3-chloro-L-tyrosine + NADP+ + chloride
3,5-dichloro-L-tyrosine + NADPH + H+
Substrates: low activity
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Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: -
Products: stepwise single electron transfer involving FMN, ferredoxin, and NADPH, overview. Ability of the substrate to provide multiple interactions with the isoalloxazine system ofFMN that are usually provided by protein side chains. Ligand binding acts to template the active site geometry and significantly stabilize the one-electron-reduced semiquinone form of FMN
Products: stepwise single electron transfer involving FMN, ferredoxin, and NADPH, overview. Ability of the substrate to provide multiple interactions with the isoalloxazine system ofFMN that are usually provided by protein side chains. Ligand binding acts to template the active site geometry and significantly stabilize the one-electron-reduced semiquinone form of FMN
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: via mono-iodotyrosine
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidize the reduced enzyme with nearly equivalent second-order rate constants despite the differing strength of their carbon-halogen bonds
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: via mono-iodotyrosine, the reaction might involve an additional ferredoxin reductase
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
r
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
Substrates: a synergy between substrate selectivity and catalytic activity is created by the enzyme. No activity with the substrate analog 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: a synergy between substrate selectivity and catalytic activity is created by the enzyme. No activity with the substrate analog 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
Substrates: analytical detection method for iodotyrosine, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: analytical detection method for iodotyrosine, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: fluorotyrosine is an inert substrate analogue
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme can act as a general dehalogenase, promoting reductive dehalogenation of 3-bromo- and 3-chloro-L-tyrosine, though not 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme can act as a general dehalogenase, promoting reductive dehalogenation of 3-bromo- and 3-chloro-L-tyrosine, though not 3-fluoro-L-tyrosine
Products: -
Products: -
?
additional information
?
-
-
Substrates: while L-iodotyrosines are almost completely dehalogenated, D-iodotyrosines, alpha-methyl-DL-iodotyrosines and 3,5-diiodo-4-hydroxyphenyl-DL-lactic acid are poor substrates for the deiodinase. No substrates are 3,5-diiodo-4-hydroxyphenyl-alpha-guanidyl propionic acid, 3,5-diiodo-4-hydroxyphenyl propionic acid, 3,5-diiodotyramine, 3-iodo-5-nitro-L-tyrosine and 3-iodo-L-phenylalanine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,5-diiodo-L-tyrosine + NADPH + H+
3-iodo-L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADPH + H+
L-tyrosine + NADP+ + I-
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-iodo-L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
Substrates: via mono-iodotyrosine
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + 2 NADP+ + 2 iodide
3,5-diiodo-L-tyrosine + 2 NADPH + 2 H+
-
Substrates: -
Products: -
Products: -
r
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3,5-diiodo-L-tyrosine + NADPH + H+
Substrates: overall reaction
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-tyrosine + NADP+ + iodide
3-iodo-L-tyrosine + NADPH + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
presence of a neutral flavin radical during the reaction. Radical is stable and persists at 4°C under aerobic conditions for many days
FMN
-
enzyme is reduced in two successive 1-electron oxidation-reduction steps. The oxidation-reduction potential of the couple semiquinone/fully reduced enzyme is -0.412 V at pH 7 and 25°C. The value for the oxidized/semiquinone couple is -0.190 V at pH 7 and 25°C
FMN
FMN binds non-covalently at the dimer interface established by a helix from each of the two identical subunits involving residues Ser102 and Ser128. Iodotyrosine deiodinase utilizes FMN to maintain iodide homeostasis by reductive deiodination of iodotyrosine. In the absence of an active site ligand, only the oxidized and two-electron-reduced forms of FMN are detected
FMN
the FMN-binding site of mammalian IYD is conserved in SUP-18, FMN appears to require catalytic activity to function
additional information
the cofactors form a redox electron transport chain, overview
-
additional information
-
the cofactors form a redox electron transport chain, overview
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
among polychlorinated biphenyls and polybrominated diphenyl ethers without a hydroxyl group tested, including their methoxylated metabolites, none is inhibitory
-
additional information
target for disruption of thyroid hormone homeostasis by environmental halogenated chemicals, e.g. food colorants, pharmaceuticals, agrochemicals, and antiparasitics, effects of environmental halogenated chemicals on iodotyrosine deiodinase activity, overview. Non-hydroxylated PCBs (e.g., 2,2',4,4'-tetrachlorobiphenyl) and PBDEs (e.g., 2,2',4,4'-tetrabromodiphenyl ether), nitrofen, trichlabendazole, miconazole and amiodarone lack IYD-inhibitory activity
-
additional information
-
target for disruption of thyroid hormone homeostasis by environmental halogenated chemicals, e.g. food colorants, pharmaceuticals, agrochemicals, and antiparasitics, effects of environmental halogenated chemicals on iodotyrosine deiodinase activity, overview. Non-hydroxylated PCBs (e.g., 2,2',4,4'-tetrachlorobiphenyl) and PBDEs (e.g., 2,2',4,4'-tetrabromodiphenyl ether), nitrofen, trichlabendazole, miconazole and amiodarone lack IYD-inhibitory activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
an evolutionarily conserved serine-cysteine-rich region in the C-terminal cytoplasmic domain of SUP-9 is required for its specific activation by SUP-18
-
additional information
-
an evolutionarily conserved serine-cysteine-rich region in the C-terminal cytoplasmic domain of SUP-9 is required for its specific activation by SUP-18
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital Hypothyroidism
Mutations in the iodotyrosine deiodinase gene and hypothyroidism.
Goiter
Genetics and phenomics of hypothyroidism and goiter due to iodotyrosine deiodinase (DEHAL1) gene mutations.
Goiter
Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects.
Goiter
[Quantitative aspects of iodine metabolism in one case of congenital iodotyrosine deiodinase defect (author's transl)]
Hyperthyroidism
A Nonradioactive DEHAL Assay for Testing Substrates, Inhibitors, and Monitoring Endogenous Activity.
Hypothyroidism
Genetic Evaluation of Congenital Hypothyroidism with Gland in situ Using Targeted Exome Sequencing.
Hypothyroidism
Genetics and phenomics of hypothyroidism and goiter due to iodotyrosine deiodinase (DEHAL1) gene mutations.
Hypothyroidism
Molecular characterization of iodotyrosine dehalogenase deficiency in patients with hypothyroidism.
Hypothyroidism
Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects.
Hypothyroidism
Towards the timely diagnosis of hypothyroidism caused by DEHAL1 gene defects.
Hypothyroidism
[Quantitative aspects of iodine metabolism in one case of congenital iodotyrosine deiodinase defect (author's transl)]
Intellectual Disability
Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects.
Intellectual Disability
Towards the timely diagnosis of hypothyroidism caused by DEHAL1 gene defects.
iodotyrosine deiodinase deficiency
Genetics and phenomics of hypothyroidism and goiter due to iodotyrosine deiodinase (DEHAL1) gene mutations.
iodotyrosine deiodinase deficiency
Towards the pre-clinical diagnosis of hypothyroidism caused by iodotyrosine deiodinase (DEHAL1) defects.
iodotyrosine deiodinase deficiency
Towards the timely diagnosis of hypothyroidism caused by DEHAL1 gene defects.
Thyroid Carcinoma, Anaplastic
Characterisation of DEHAL1 expression in thyroid pathologies.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
3-bromo-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.021
3-chloro-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.019
3,5-diiodo-L-tyrosine
enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication
0.04
3,5-diiodo-L-tyrosine
enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
0.44
3,5-diiodo-L-tyrosine
mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
0.004
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.0066
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.007
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.0073
3-iodo-L-tyrosine
pH and temperature not specified in the publication
0.008
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.014
3-iodo-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.019
3-iodo-L-tyrosine
pH not specified in the publication, temperature not specified in the publication
0.031
3-iodo-L-tyrosine
pH 7.6, temperature not specified in the publication, recombinant enzyme
additional information
additional information
Michaelis-Menten steady-state kinetics. Dissociation constants for different substrate analogues, overview
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics. Dissociation constants for different substrate analogues, overview
-
additional information
additional information
-
rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid, substrates chloro-, bromo-, and iodotyrosine bind with similar rate constants, overview. Standard two-state model, no intermediate complex accumulates during closure of the active site lid induced by substrate
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.069
3-bromo-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.05
3-chloro-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.12
3,5-diiodo-L-tyrosine
enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication
0.16
3,5-diiodo-L-tyrosine
enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
1.08
3,5-diiodo-L-tyrosine
mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
0.0102
3-iodo-L-tyrosine
pH and temperature not specified in the publication
0.07
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.09
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.12
3-iodo-L-tyrosine
pH not specified in the publication, temperature not specified in the publication
0.12
3-iodo-L-tyrosine
at pH 7.4, temperature not specified in the publication
0.208
3-iodo-L-tyrosine
pH 7.6, temperature not specified in the publication, recombinant enzyme
0.23
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
0.29
3-iodo-L-tyrosine
-
pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9000
3-bromo-L-tyrosine
at pH 7.4, temperature not specified in the publication
2400
3-chloro-L-tyrosine
at pH 7.4, temperature not specified in the publication
2.5
3,5-diiodo-L-tyrosine
mutant Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
3.83
3,5-diiodo-L-tyrosine
enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication
6
3,5-diiodo-L-tyrosine
enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication
6
3-iodo-L-tyrosine
pH not specified in the publication, temperature not specified in the publication