EC Explorer

[browse EC tree] - [search]

EC 1.13.11.52 Details

show Brenda entry

EC number

1.13.11.52

Accepted name

indoleamine 2,3-dioxygenase

Reaction

(1) D-tryptophan + O₂ = N-formyl-D-kynurenine;;(2) L-tryptophan + O₂ = N-formyl-L-kynurenine

Other name(s)

IDO (ambiguous), tryptophan pyrrolase (ambiguous), D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)

Systematic name

D-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)

CAS registry number

9014-51-1

Comment

A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [2,6]. Superoxide radicals can replace O₂ as oxygen donor [4,7].

History

created 2006

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.1. undefined

1.13.11 With incorporation of two atoms of oxygen

1.13.11.1 catechol 1,2-dioxygenase

1.13.11.2 catechol 2,3-dioxygenase

1.13.11.3 protocatechuate 3,4-dioxygenase

1.13.11.4 gentisate 1,2-dioxygenase

1.13.11.5 homogentisate 1,2-dioxygenase

1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase

1.13.11.7 created 1965 as EC 1.13.1.7, transferred 1972 to EC 1.13.11.7, deleted 1980

1.13.11.8 protocatechuate 4,5-dioxygenase

1.13.11.9 2,5-dihydroxypyridine 5,6-dioxygenase

1.13.11.10 7,8-dihydroxykynurenate 8,8a-dioxygenase

1.13.11.11 tryptophan 2,3-dioxygenase

1.13.11.12 linoleate 13S-lipoxygenase

1.13.11.13 ascorbate 2,3-dioxygenase

1.13.11.14 2,3-dihydroxybenzoate 3,4-dioxygenase

1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenase

1.13.11.16 3-carboxyethylcatechol 2,3-dioxygenase

1.13.11.17 indole 2,3-dioxygenase

1.13.11.18 persulfide dioxygenase

1.13.11.19 cysteamine dioxygenase

1.13.11.20 cysteine dioxygenase

1.13.11.21 created 1972, deleted 2001

1.13.11.22 caffeate 3,4-dioxygenase

1.13.11.23 2,3-dihydroxyindole 2,3-dioxygenase

1.13.11.24 quercetin 2,3-dioxygenase

1.13.11.25 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase

1.13.11.26 peptide-tryptophan 2,3-dioxygenase

1.13.11.27 4-hydroxyphenylpyruvate dioxygenase

1.13.11.28 2,3-dihydroxybenzoate 2,3-dioxygenase

1.13.11.29 stizolobate synthase

1.13.11.30 stizolobinate synthase

1.13.11.31 arachidonate 12-lipoxygenase

1.13.11.32 2-nitropropane dioxygenase

1.13.11.33 arachidonate 15-lipoxygenase

1.13.11.34 arachidonate 5-lipoxygenase

1.13.11.35 pyrogallol 1,2-oxygenase

1.13.11.36 chloridazon-catechol dioxygenase

1.13.11.37 hydroxyquinol 1,2-dioxygenase

1.13.11.38 1-hydroxy-2-naphthoate 1,2-dioxygenase

1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase

1.13.11.40 arachidonate 8-lipoxygenase

1.13.11.41 2,4′-dihydroxyacetophenone dioxygenase

1.13.11.42 indoleamine-pyrrole 2,3-dioxygenase

1.13.11.43 lignostilbene αβ-dioxygenase

1.13.11.44 linoleate diol synthase

1.13.11.45 linoleate 11-lipoxygenase

1.13.11.46 4-hydroxymandelate synthase

1.13.11.47 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

1.13.11.48 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

1.13.11.49 chlorite O₂-lyase

1.13.11.50 acetylacetone-cleaving enzyme

1.13.11.51 9-cis-epoxycarotenoid dioxygenase

1.13.11.52 indoleamine 2,3-dioxygenase

1.13.11.53 acireductone dioxygenase (Ni²⁺-requiring)

1.13.11.54 acireductone dioxygenase [iron(II)-requiring]

1.13.11.55 sulfur oxygenase/reductase

1.13.11.56 1,2-dihydroxynaphthalene dioxygenase

1.13.11.57 gallate dioxygenase

1.13.11.58 linoleate 9S-lipoxygenase

1.13.11.59 torulene dioxygenase

1.13.11.60 linoleate 8R-lipoxygenase

1.13.11.61 linolenate 9R-lipoxygenase

1.13.11.62 linoleate 10R-lipoxygenase

1.13.11.63 β-carotene 15,15′-dioxygenase

1.13.11.64 5-nitrosalicylate dioxygenase

1.13.11.65 carotenoid isomerooxygenase

1.13.11.66 hydroquinone 1,2-dioxygenase

1.13.11.67 8′-apo-β-carotenoid 14′,13′-cleaving dioxygenase

1.13.11.68 9-cis-β-carotene 9′,10′-cleaving dioxygenase

1.13.11.69 carlactone synthase

1.13.11.70 all-trans-10′-apo-β-carotenal 13,14-cleaving dioxygenase

1.13.11.71 carotenoid-9′,10′-cleaving dioxygenase

1.13.11.72 2-hydroxyethylphosphonate dioxygenase

1.13.11.73 methylphosphonate synthase

1.13.11.74 2-aminophenol 1,6-dioxygenase

1.13.11.75 all-trans-8′-apo-β-carotenal 15,15′-oxygenase

1.13.11.76 2-amino-5-chlorophenol 1,6-dioxygenase

1.13.11.77 oleate 10S-lipoxygenase

1.13.11.78 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)

1.13.11.79 aerobic 5,6-dimethylbenzimidazole synthase

1.13.11.80 (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase

1.13.11.81 7,8-dihydroneopterin oxygenase

1.13.11.82 8′-apo-carotenoid 13,14-cleaving dioxygenase

1.13.11.83 4-hydroxy-3-prenylphenylpyruvate oxygenase

1.13.11.84 crocetin dialdehyde synthase

1.13.11.85 exo-cleaving rubber dioxygenase

1.13.11.86 5-aminosalicylate 1,2-dioxygenase

1.13.11.87 endo-cleaving rubber dioxygenase

1.13.11.88 isoeugenol monooxygenase

1.13.11.89 (hydroxymethyl)phosphonate dioxygenase

1.13.11.90 [1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming)

1.13.11.91 3-mercaptopropionate dioxygenase

1.13.11.92 fatty acid α-dioxygenase

1.13.11.93 2-oxoadipate dioxygenase/decarboxylase

1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

1.13.99 Miscellaneous

1.13.99.1 inositol oxygenase

1.13.99.2 created 1972, deleted 1992

1.13.99.3 tryptophan 2′-dioxygenase

1.13.99.4 created 1989, deleted 1992

1.13.99.5 created 1999, deleted 2001

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)