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Literature summary extracted from

  • Austin, C.J.; Mailu, B.M.; Maghzal, G.J.; Sanchez-Perez, A.; Rahlfs, S.; Zocher, K.; Yuasa, H.J.; Arthur, J.W.; Becker, K.; Stocker, R.; Hunt, N.H.; Ball, H.J.
    Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2 (2010), Amino Acids, 39, 565-578.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.11.52 cytochrome b5
-
Mus musculus
1.13.11.52 methylene blue
-
Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.52 isozyme IDO2 is expressed in KRX cells, isozyme IDO1 is expressed in Escherichia coli Rosetta cells Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.52 1-methyl-D-tryptophan poor non-competitive inhibitor of both IDO1 and IDO2 activity Mus musculus
1.13.11.52 1-methyl-L-tryptophan poor competitive inhibitor of isozyme IDO1 Mus musculus
1.13.11.52 nitric oxide nitric oxide can potentially inhibit isozyme IDO2 activity Mus musculus
1.13.11.52 norharman
-
Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.52 0.028
-
L-tryptophan recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 0.029
-
L-tryptophan recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 0.53
-
L-tryptophan recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 12
-
L-tryptophan recombinant isozyme IDO2, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.52 45000
-
isozymes IDO1 and IDO2, SDS-PAGE Mus musculus
1.13.11.52 45200
-
isozyme IDO2, calculated from amino acid sequence Mus musculus
1.13.11.52 45300
-
isozyme IDO1, calculated from amino acid sequence Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.52 D-tryptophan + O2 Mus musculus
-
N-formyl-D-kynurenine
-
?
1.13.11.52 L-tryptophan + O2 Mus musculus
-
N-formyl-L-kynurenine
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.52 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.52 5-hydroxy-L-tryptophan + O2
-
Mus musculus N-formyl-5-hydroxy-L-kynurenine
-
?
1.13.11.52 D-tryptophan + O2
-
Mus musculus N-formyl-D-kynurenine
-
?
1.13.11.52 L-tryptophan + O2
-
Mus musculus N-formyl-L-kynurenine
-
?

Subunits

EC Number Subunits Comment Organism
1.13.11.52 monomer 1 * 45000, isozymes IDO1 and IDO2, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
1.13.11.52 IDO1 isozyme Mus musculus
1.13.11.52 IDO2 isozyme Mus musculus
1.13.11.52 indoleamine 2,3-dioxygenase-1
-
Mus musculus
1.13.11.52 indoleamine 2,3-dioxygenase-2
-
Mus musculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.11.52 48 60 the melting temperature of the denaturation process for recombinant isozyme IDO1 is 60°C, with a possible second intermediate at 48°C, recombinant isozyme IDO2 denatures in a single step, with a melting temperature at 48°C Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.52 6 6.5 isozyme IDO1 Mus musculus
1.13.11.52 7.4 7.5 isozyme IDO2 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme recombinant isozymes IDO2 and IDO1 are ferric (Fe3+) type heme proteins Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.13.11.52 0.08
-
1-methyl-L-tryptophan recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 0.105
-
1-methyl-L-tryptophan recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 0.44
-
1-methyl-L-tryptophan recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 0.69
-
norharman recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 1.08
-
norharman recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 1.73
-
norharman recombinant isozyme IDO1, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 1.96
-
norharman recombinant isozyme IDO2, in the presence of 50 nM recombinant human cytochrome b5 and 50 nM NADPH cytochrome P450 reductase, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 2.75
-
1-methyl-L-tryptophan recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus
1.13.11.52 11.3
-
1-methyl-D-tryptophan recombinant isozyme IDO1, in the presence of 0.01 mM methylene blue, in 100 mM phosphate buffer, pH 7.4, at 37°C Mus musculus