BRENDA - Enzyme Database
show all sequences of 1.13.11.11

Analysis of reaction intermediates in tryptophan 2,3-dioxygenase a comparison with indoleamine 2,3-dioxygenase

Basran, J.; Booth, E.S.; Lee, M.; Handa, S.; Raven, E.L.; Biochemistry 55, 6743-6750 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene kynA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Xanthomonas campestris pv. campestris
gene TDO, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow, pre-steady-state, and steady-state kinetics
Homo sapiens
additional information
-
additional information
stopped-flow, pre-steady-state, and steady-state kinetics
Xanthomonas campestris pv. campestris
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
ferryl heme, formation of ferrous-oxy TDO
Homo sapiens
Fe2+
ferryl heme, formation of ferrous-oxy TDO
Xanthomonas campestris pv. campestris
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
-
-
?
L-tryptophan + O2
Xanthomonas campestris pv. campestris
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Xanthomonas campestris pv. campestris ATCC 33913
-
N-formyl-L-kynurenine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P48775
-
-
Xanthomonas campestris pv. campestris
Q8PDA8
-
-
Xanthomonas campestris pv. campestris ATCC 33913
Q8PDA8
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Xanthomonas campestris pv. campestris
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-fluoro-L-tryptophan + O2
-
741938
Homo sapiens
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
5-fluoro-L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
5-fluoro-L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Homo sapiens
?
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Xanthomonas campestris pv. campestris
?
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
?
-
-
-
?
L-tryptophan + O2
-
741938
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
N-formyl-L-kynurenine
-
-
-
?
additional information
no activity with D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Homo sapiens
?
-
-
-
-
additional information
no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Xanthomonas campestris pv. campestris
?
-
-
-
-
additional information
no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Xanthomonas campestris pv. campestris ATCC 33913
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Homo sapiens
25
-
assay at
Xanthomonas campestris pv. campestris
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
8
-
assay at
Xanthomonas campestris pv. campestris
Cofactor
Cofactor
Commentary
Organism
Structure
heme
ferryl heme
Homo sapiens
heme
ferryl heme
Xanthomonas campestris pv. campestris
Cloned(Commentary) (protein specific)
Commentary
Organism
gene kynA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Xanthomonas campestris pv. campestris
gene TDO, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
ferryl heme
Homo sapiens
heme
ferryl heme
Xanthomonas campestris pv. campestris
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow, pre-steady-state, and steady-state kinetics
Homo sapiens
additional information
-
additional information
stopped-flow, pre-steady-state, and steady-state kinetics
Xanthomonas campestris pv. campestris
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
ferryl heme, formation of ferrous-oxy TDO
Homo sapiens
Fe2+
ferryl heme, formation of ferrous-oxy TDO
Xanthomonas campestris pv. campestris
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
-
-
?
L-tryptophan + O2
Xanthomonas campestris pv. campestris
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Xanthomonas campestris pv. campestris ATCC 33913
-
N-formyl-L-kynurenine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Xanthomonas campestris pv. campestris
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-fluoro-L-tryptophan + O2
-
741938
Homo sapiens
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
5-fluoro-L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
5-fluoro-L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
5-fluoro-N-formyl-L-kynurenine
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Homo sapiens
?
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Xanthomonas campestris pv. campestris
?
-
-
-
?
indole-3-pyruvic acid + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
?
-
-
-
?
L-tryptophan + O2
-
741938
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
741938
Xanthomonas campestris pv. campestris ATCC 33913
N-formyl-L-kynurenine
-
-
-
?
additional information
no activity with D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Homo sapiens
?
-
-
-
-
additional information
no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Xanthomonas campestris pv. campestris
?
-
-
-
-
additional information
no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
741938
Xanthomonas campestris pv. campestris ATCC 33913
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Homo sapiens
25
-
assay at
Xanthomonas campestris pv. campestris
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Homo sapiens
8
-
assay at
Xanthomonas campestris pv. campestris
General Information
General Information
Commentary
Organism
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
Homo sapiens
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
Xanthomonas campestris pv. campestris
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
Homo sapiens
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
Xanthomonas campestris pv. campestris
General Information (protein specific)
General Information
Commentary
Organism
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
Homo sapiens
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
Xanthomonas campestris pv. campestris
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
Homo sapiens
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
Xanthomonas campestris pv. campestris
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
-
-
-
-
-
-
-
1
-
1
-
1
-
3
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
2
2
-
-
-
743358
Gonzalez Esquivel
Kynurenine pathway metabolite ...
Homo sapiens, Mus musculus, Xanthomonas campestris pv. campestris, Xanthomonas campestris pv. campestris ATCC 33913
Neuropharmacology
112
331-345
2017
2
-
-
-
-
-
3
2
-
-
-
-
-
7
-
-
-
-
-
29
-
-
4
2
-
-
-
-
-
-
-
3
-
-
-
2
-
-
5
-
-
-
-
3
-
3
-
-
-
-
-
-
-
-
-
31
-
-
4
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741938
Basran
Analysis of reaction intermed ...
Homo sapiens, Xanthomonas campestris pv. campestris, Xanthomonas campestris pv. campestris ATCC 33913
Biochemistry
55
6743-6750
2016
-
-
2
-
-
-
-
2
-
2
-
3
-
4
-
-
2
-
-
-
-
-
12
-
2
-
-
-
2
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
2
-
2
-
3
-
-
-
2
-
-
-
-
12
-
2
-
-
-
2
-
-
-
-
4
4
-
-
-
742986
Pantouris
Insights into the mechanism o ...
Homo sapiens
J. Enzyme Inhib. Med. Chem.
31
70-78
2016
-
1
-
-
-
-
2
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
743821
Lewis-Ballester
Molecular basis for catalysis ...
Homo sapiens
Sci. Rep.
6
35169
2016
-
-
1
1
1
-
-
1
-
1
-
1
-
2
-
-
-
1
-
1
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
1
-
1
-
1
-
-
-
-
-
1
-
-
2
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
743005
Yuasa
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
J. Exp. Zool. B
324
128-140
2015
-
-
8
-
-
-
-
11
-
-
-
8
-
14
-
-
-
-
-
-
-
-
8
-
8
-
-
-
3
-
-
1
-
-
-
-
-
8
1
-
-
-
-
-
-
11
-
-
-
8
-
-
-
-
-
-
-
-
8
-
8
-
-
-
3
-
-
-
-
8
8
-
-
-
743064
Wu
Identification of substituted ...
Homo sapiens
J. Med. Chem.
58
7807-7819
2015
-
1
1
-
-
-
21
-
-
-
-
1
-
1
-
-
1
-
-
2
-
-
1
-
1
-
-
-
1
-
-
1
-
-
20
-
1
1
1
-
-
-
20
21
-
-
-
-
-
1
-
-
-
1
-
2
-
-
1
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
742114
Maeta
Contributions of tryptophan 2 ...
Mus musculus, Mus musculus C57BL/6
Biosci. Biotechnol. Biochem.
78
878-881
2014
-
-
-
-
1
-
-
-
-
-
-
6
-
3
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
743760
Meng
Structural and functional ana ...
Homo sapiens
Proteins
82
3210-3216
2014
-
-
1
1
9
-
-
8
-
-
-
1
-
2
-
-
1
-
-
1
-
-
3
3
1
-
-
7
1
-
-
1
-
-
-
-
-
1
1
1
9
-
-
-
-
8
-
-
-
1
-
-
-
1
-
1
-
-
3
3
1
-
-
7
1
-
-
-
-
2
2
-
-
-