BRENDA - Enzyme Database
show all sequences of 1.13.11.11

Substrate binding primes human tryptophan 2,3-dioxygenase for ligand binding

Nienhaus, K.; Hahn, V.; Huepfel, M.; Nienhaus, G.U.; J. Phys. Chem. B 121, 7412-7420 (2017)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
reaction and ligand binding kinetics, two hTDO conformations exist that bind CO in a bimolecular reaction, but with very different rates, kinetic calculations, overview
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
ferric heme
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + O2
Homo sapiens
-
N-formyl-L-kynurenine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P48775
-
-
Reaction
Reaction
Commentary
Organism
L-tryptophan + O2 = N-formyl-L-kynurenine
catalytic mechanism, modeling. hTDO exists as two discrete species with markedly different ligand binding properties. The active site environment of the slowly rebinding species is structurally very heterogeneous and ligand access to greatly hindered. Binding of the L-Trp substrate stabilizes the faster-binding species, which features a well-structured active site and offers facile access of the ligand to the heme iron. This mechanism ensures that the ternary complex forms mainly by first binding the L-Trp substrate, which primes the active site for the subsequent binding of O2, which ensures efficient enzyme action
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
743153
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
additional information
enzyme-CO binding analysis, overview
743153
Homo sapiens
?
-
-
-
-
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
heme
ferric heme
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
ferric heme
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
reaction and ligand binding kinetics, two hTDO conformations exist that bind CO in a bimolecular reaction, but with very different rates, kinetic calculations, overview
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
ferric heme
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + O2
Homo sapiens
-
N-formyl-L-kynurenine
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
743153
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
additional information
enzyme-CO binding analysis, overview
743153
Homo sapiens
?
-
-
-
-
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
additional information
the active site of the enzyme is highly dynamic
Homo sapiens
physiological function
the human heme enzyme tryptophan 2,3-dioxygenase (hTDO) catalyzes the insertion of dioxygen into its cognate substrate, L-tryptophan (L-Trp)
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
additional information
the active site of the enzyme is highly dynamic
Homo sapiens
physiological function
the human heme enzyme tryptophan 2,3-dioxygenase (hTDO) catalyzes the insertion of dioxygen into its cognate substrate, L-tryptophan (L-Trp)
Homo sapiens
Other publictions for EC 1.13.11.11
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743153
Nienhaus
Substrate binding primes huma ...
Homo sapiens
J. Phys. Chem. B
121
7412-7420
2017
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1
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1
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1
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3
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1
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1
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1
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1
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1
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1
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1
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2
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1
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743358
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331-345
2017
2
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3
2
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7
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29
-
-
4
2
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3
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2
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5
-
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3
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3
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31
-
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4
4
-
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2016
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2
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2
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4
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2
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12
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2
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2
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2
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2
2
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2
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2
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3
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2
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-
12
-
2
-
-
-
2
-
-
-
-
4
4
-
-
-
742986
Pantouris
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Homo sapiens
J. Enzyme Inhib. Med. Chem.
31
70-78
2016
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1
-
-
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2
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1
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1
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1
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1
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1
1
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743821
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6
35169
2016
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-
1
1
1
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-
1
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1
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1
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2
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1
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2
1
1
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1
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1
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1
1
1
1
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1
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1
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1
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2
1
1
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Efficient tryptophan-cataboli ...
Branchiostoma floridae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Monosiga brevicollis, Nematostella vectensis, no activity in Brugia malayi, no activity in Saccharomyces cerevisiae, no activity in Schistosoma mansoni, Rattus norvegicus, Strongylocentrotus purpuratus
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324
128-140
2015
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8
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11
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8
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14
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8
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8
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3
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1
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8
1
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11
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8
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8
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3
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8
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743064
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Homo sapiens
J. Med. Chem.
58
7807-7819
2015
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1
1
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21
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1
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1
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1
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2
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1
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1
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1
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1
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20
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1
1
1
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20
21
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1
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1
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2
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1
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1
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1
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3
3
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742114
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2014
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1
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6
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8
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6
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8
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3
3
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Homo sapiens
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82
3210-3216
2014
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1
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9
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8
-
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-
1
-
2
-
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1
-
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1
-
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3
3
1
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7
1
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1
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1
1
1
9
-
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8
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1
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1
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1
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3
3
1
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7
1
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2
2
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