BRENDA - Enzyme Database
show all sequences of 1.13.11.11

Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes

Yuasa, H.J.; Ball, H.J.; J. Exp. Zool. B 324, 128-140 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene 33737, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Monosiga brevicollis
gene BRAFLDRAFT_210874, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Branchiostoma floridae
gene C28H8.11, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Caenorhabditis elegans
gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Homo sapiens
gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Rattus norvegicus
gene TDOa, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Strongylocentrotus purpuratus
gene v1g157887, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Nematostella vectensis
gene vCG5163, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Drosophila melanogaster
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Branchiostoma floridae
additional information
-
additional information
Michaelis-Menten kinetics
Caenorhabditis elegans
additional information
-
additional information
Michaelis-Menten kinetics
Drosophila melanogaster
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
additional information
-
additional information
Michaelis-Menten kinetics
Monosiga brevicollis
additional information
-
additional information
Michaelis-Menten kinetics
Nematostella vectensis
additional information
-
additional information
Michaelis-Menten kinetics
Rattus norvegicus
additional information
-
additional information
Michaelis-Menten kinetics
Strongylocentrotus purpuratus
0.0825
-
L-tryptophan
pH 8.0, 37°C
Homo sapiens
0.221
-
L-tryptophan
pH 7.0, 37°C
Rattus norvegicus
0.277
-
L-tryptophan
pH 8.0, 37°C
Monosiga brevicollis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + O2
Rattus norvegicus
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Homo sapiens
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Drosophila melanogaster
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Nematostella vectensis
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Monosiga brevicollis
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Branchiostoma floridae
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Caenorhabditis elegans
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Strongylocentrotus purpuratus
-
N-formyl-L-kynurenine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Branchiostoma floridae
C3XXE6
-
-
Caenorhabditis elegans
Q09474
-
-
Drosophila melanogaster
P20351
-
-
Homo sapiens
P48775
-
-
Monosiga brevicollis
A9V766
-
-
Nematostella vectensis
A7RFF0
-
-
no activity in Brugia malayi
-
-
-
no activity in Saccharomyces cerevisiae
-
-
-
no activity in Schistosoma mansoni
-
-
-
Rattus norvegicus
P21643
-
-
Strongylocentrotus purpuratus
W4ZI02
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
743005
Rattus norvegicus
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Drosophila melanogaster
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Nematostella vectensis
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Monosiga brevicollis
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Branchiostoma floridae
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Caenorhabditis elegans
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Strongylocentrotus purpuratus
N-formyl-L-kynurenine
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Branchiostoma floridae
37
-
assay at
Caenorhabditis elegans
37
-
assay at
Drosophila melanogaster
37
-
assay at
Homo sapiens
37
-
assay at
Monosiga brevicollis
37
-
assay at
Nematostella vectensis
37
-
assay at
Rattus norvegicus
37
-
assay at
Strongylocentrotus purpuratus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Rattus norvegicus
8
-
-
Homo sapiens
8
-
-
Monosiga brevicollis
Cofactor
Cofactor
Commentary
Organism
Structure
heme
-
Nematostella vectensis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene 33737, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Monosiga brevicollis
gene BRAFLDRAFT_210874, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Branchiostoma floridae
gene C28H8.11, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Caenorhabditis elegans
gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Homo sapiens
gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Rattus norvegicus
gene TDOa, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Strongylocentrotus purpuratus
gene v1g157887, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Nematostella vectensis
gene vCG5163, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
Drosophila melanogaster
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
-
Nematostella vectensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Branchiostoma floridae
additional information
-
additional information
Michaelis-Menten kinetics
Caenorhabditis elegans
additional information
-
additional information
Michaelis-Menten kinetics
Drosophila melanogaster
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
additional information
-
additional information
Michaelis-Menten kinetics
Monosiga brevicollis
additional information
-
additional information
Michaelis-Menten kinetics
Nematostella vectensis
additional information
-
additional information
Michaelis-Menten kinetics
Rattus norvegicus
additional information
-
additional information
Michaelis-Menten kinetics
Strongylocentrotus purpuratus
0.0825
-
L-tryptophan
pH 8.0, 37°C
Homo sapiens
0.221
-
L-tryptophan
pH 7.0, 37°C
Rattus norvegicus
0.277
-
L-tryptophan
pH 8.0, 37°C
Monosiga brevicollis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + O2
Rattus norvegicus
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Homo sapiens
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Drosophila melanogaster
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Nematostella vectensis
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Monosiga brevicollis
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Branchiostoma floridae
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Caenorhabditis elegans
-
N-formyl-L-kynurenine
-
-
?
L-tryptophan + O2
Strongylocentrotus purpuratus
-
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
-
743005
Rattus norvegicus
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Homo sapiens
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Drosophila melanogaster
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Nematostella vectensis
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Monosiga brevicollis
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Branchiostoma floridae
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Caenorhabditis elegans
N-formyl-L-kynurenine
-
-
-
?
L-tryptophan + O2
-
743005
Strongylocentrotus purpuratus
N-formyl-L-kynurenine
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Branchiostoma floridae
37
-
assay at
Caenorhabditis elegans
37
-
assay at
Drosophila melanogaster
37
-
assay at
Homo sapiens
37
-
assay at
Monosiga brevicollis
37
-
assay at
Nematostella vectensis
37
-
assay at
Rattus norvegicus
37
-
assay at
Strongylocentrotus purpuratus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Rattus norvegicus
8
-
-
Homo sapiens
8
-
-
Monosiga brevicollis
General Information
General Information
Commentary
Organism
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Branchiostoma floridae
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Caenorhabditis elegans
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Drosophila melanogaster
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Homo sapiens
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Monosiga brevicollis
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Nematostella vectensis
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Rattus norvegicus
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Strongylocentrotus purpuratus
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) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Branchiostoma floridae
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Caenorhabditis elegans
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Drosophila melanogaster
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Homo sapiens
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Monosiga brevicollis
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Nematostella vectensis
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Rattus norvegicus
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
Strongylocentrotus purpuratus
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
-
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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
-
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
-
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-
-
-
-
-
-
-
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
-
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-
-
-
-
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
-
-
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-
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1
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2
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1
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-
-
-
-
-
-
-
-
-
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
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8
-
-
-
-
11
-
-
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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
-
-
-
-
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6
-
3
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-
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-
-
1
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8
-
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1
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-
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6
-
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-
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1
-
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8
-
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-
-
-
-
-
-
-
-
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
-
-
-