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Literature summary extracted from
- Analysis of reaction intermediates in tryptophan 2,3-dioxygenase a comparison with indoleamine 2,3-dioxygenase (2016), Biochemistry, 55, 6743-6750 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.11 | gene kynA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Xanthomonas campestris pv. campestris |
| 1.13.11.11 | gene TDO, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Homo sapiens |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.11 | additional information | - |
additional information | stopped-flow, pre-steady-state, and steady-state kinetics | Homo sapiens | |
| 1.13.11.11 | additional information | - |
additional information | stopped-flow, pre-steady-state, and steady-state kinetics | Xanthomonas campestris pv. campestris |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.11 | Fe2+ | ferryl heme, formation of ferrous-oxy TDO | Homo sapiens |  |
| 1.13.11.11 | Fe2+ | ferryl heme, formation of ferrous-oxy TDO | Xanthomonas campestris pv. campestris | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Xanthomonas campestris pv. campestris | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Xanthomonas campestris pv. campestris ATCC 33913 | - |
N-formyl-L-kynurenine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.11 | Homo sapiens | P48775 | - |
- |
| 1.13.11.11 | Xanthomonas campestris pv. campestris | Q8PDA8 | - |
- |
| 1.13.11.11 | Xanthomonas campestris pv. campestris ATCC 33913 | Q8PDA8 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.11 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Homo sapiens |
| 1.13.11.11 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Xanthomonas campestris pv. campestris |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | 5-fluoro-L-tryptophan + O2 | - |
Homo sapiens | 5-fluoro-N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | 5-fluoro-L-tryptophan + O2 | - |
Xanthomonas campestris pv. campestris | 5-fluoro-N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | 5-fluoro-L-tryptophan + O2 | - |
Xanthomonas campestris pv. campestris ATCC 33913 | 5-fluoro-N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | indole-3-pyruvic acid + O2 | - |
Homo sapiens | ? | - |
? | |
| 1.13.11.11 | indole-3-pyruvic acid + O2 | - |
Xanthomonas campestris pv. campestris | ? | - |
? | |
| 1.13.11.11 | indole-3-pyruvic acid + O2 | - |
Xanthomonas campestris pv. campestris ATCC 33913 | ? | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Xanthomonas campestris pv. campestris | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Xanthomonas campestris pv. campestris ATCC 33913 | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | 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 | Homo sapiens | ? | - |
? | |
| 1.13.11.11 | 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 | Xanthomonas campestris pv. campestris | ? | - |
? | |
| 1.13.11.11 | 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 | Xanthomonas campestris pv. campestris ATCC 33913 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | hTDO | - |
Homo sapiens |
| 1.13.11.11 | TDO | - |
Homo sapiens |
| 1.13.11.11 | TDO | - |
Xanthomonas campestris pv. campestris |
| 1.13.11.11 | XcTDO | - |
Xanthomonas campestris pv. campestris |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.11 | 25 | - |
assay at | Homo sapiens |
| 1.13.11.11 | 25 | - |
assay at | Xanthomonas campestris pv. campestris |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.11 | 8 | - |
assay at | Homo sapiens |
| 1.13.11.11 | 8 | - |
assay at | Xanthomonas campestris pv. campestris |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.11 | heme | ferryl heme | Homo sapiens | |
| 1.13.11.11 | heme | ferryl heme | Xanthomonas campestris pv. campestris | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | 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 |
| 1.13.11.11 | 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 |
| 1.13.11.11 | 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 |
| 1.13.11.11 | 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 |
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