EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.11.52 | T254A | ternary complex molecular simulations. The mutation causes the opening of the loop 250-260 to loop 117-130, leading to a more dynamic and open distal pocket, accounting for the much lower substrate affinity (i.e. higher Km). On the other hand, the simulation data of the ferryl/L-indole 2,3-epoxide intermediate indicate that the T254A mutation also results in the opening of the loop 250-260 to loop 117-130. It leads to local reorganization of the H-bonding interactions surrounding the NH3+ group of the substrate, resulting in an open conformation, in which the H-bond between the NH3+ and the epoxide is temporarily lost | Xanthomonas campestris |
1.13.11.52 | T342A | site-directed mutagenesis, the mutation only slightly perturbs the global structural properties of the enzyme, but it totally abolishes the substrate stereoselectivity, substrate-free spectrum | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.52 | 0.119 | - |
L-tryptophan | pH 7.0, 25°C, mutant T342A | Homo sapiens | |
1.13.11.52 | 0.12 | - |
L-tryptophan | pH 7.0, 25°C, wild-type enzyme | Homo sapiens | |
1.13.11.52 | 0.159 | - |
D-tryptophan | pH 7.0, 25°C, mutant T342A | Homo sapiens | |
1.13.11.52 | 0.26 | - |
D-tryptophan | pH 7.0, 25°C, wild-type enzyme | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.52 | Fe2+ | heme-containing enzyme | Homo sapiens | |
1.13.11.52 | Fe2+ | heme-containing enzyme | Xanthomonas campestris |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.52 | L-tryptophan + O2 | Xanthomonas campestris | - |
N-formyl-L-kynurenine | - |
? | |
1.13.11.52 | L-tryptophan + O2 | Homo sapiens | human TDO displays a major specificity towards L-Trp, structural role of T342 in controlling the substrate stereoselectivity of the enzyme | N-formyl-L-kynurenine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.52 | Homo sapiens | - |
- |
- |
1.13.11.52 | Xanthomonas campestris | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.13.11.52 | liver | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.52 | D-tryptophan + O2 | low activity | Homo sapiens | N-formyl-D-kynurenine | - |
? | |
1.13.11.52 | L-tryptophan + O2 | - |
Xanthomonas campestris | N-formyl-L-kynurenine | - |
? | |
1.13.11.52 | L-tryptophan + O2 | human TDO displays a major specificity towards L-Trp, structural role of T342 in controlling the substrate stereoselectivity of the enzyme | Homo sapiens | N-formyl-L-kynurenine | - |
? | |
1.13.11.52 | L-tryptophan + O2 | highly preferred substrate, T342 plays a pivotal role in controlling the substrate stereoselectivity of hTDO | Homo sapiens | N-formyl-L-kynurenine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.52 | TDO | - |
Homo sapiens |
1.13.11.52 | TDO | - |
Xanthomonas campestris |
1.13.11.52 | tryptophan dioxygenase | - |
Homo sapiens |
1.13.11.52 | tryptophan dioxygenase | - |
Xanthomonas campestris |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.11.52 | 25 | - |
assay at | Homo sapiens |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.52 | 0.082 | - |
D-tryptophan | pH 7.0, 25°C, mutant T342A | Homo sapiens | |
1.13.11.52 | 0.101 | - |
L-tryptophan | pH 7.0, 25°C, mutant T342A | Homo sapiens | |
1.13.11.52 | 0.2 | - |
D-tryptophan | pH 7.0, 25°C, wild-type enzyme | Homo sapiens | |
1.13.11.52 | 2.24 | - |
L-tryptophan | pH 7.0, 25°C, wild-type enzyme | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.11.52 | 7 | - |
assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.52 | heme | - |
Homo sapiens | |
1.13.11.52 | heme | - |
Xanthomonas campestris |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.52 | additional information | molecular dynamics simulation studies, overview. Structural role of T342 in controlling the substrate stereoselectivity of the enzyme | Homo sapiens |
1.13.11.52 | additional information | Xanthomonas campestris TDO shows an H-bond between T254 and the ammonium group of the substrate is present in the L-Trp-bound enzyme, but not in the D-Trp bound enzyme, molecular dynamics simulation studies. T254 controls the substrate stereoselectivity of the enzyme by modulating the H-bonding interaction between the NH3-group and epoxide oxygen of the ferryl/indole 2,3-epoxide intermediate of the enzyme, and regulating the dynamics of two active site loops, loop250-260 and loop117-130, critical for substrate-binding, O2 and L-trp both are bound in the active site | Xanthomonas campestris |
1.13.11.52 | physiological function | the enzyme is responsible for L-Trp processing that ultimately leads to the biosynthesis of NAD+ and NADP+ | Homo sapiens |