KEGG   ENZYME: 1.13.11.52Help
Entry
EC 1.13.11.52               Enzyme                                 
Name
indoleamine 2,3-dioxygenase;
IDO (ambiguous);
tryptophan pyrrolase (ambiguous)
Class
Oxidoreductases;
Acting on single donors with O2 as oxidant and incorporation of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2;
With incorporation of two atoms of oxygen
BRITE hierarchy
Sysname
D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Reaction(IUBMB)
(1) D-tryptophan + O2 = N-formyl-D-kynurenine [RN:R07362];
(2) L-tryptophan + O2 = N-formyl-L-kynurenine [RN:R00678]
Reaction(KEGG)
Substrate
D-tryptophan [CPD:C00525];
O2 [CPD:C00007];
L-tryptophan [CPD:C00078]
Product
N-formyl-D-kynurenine [CPD:C15605];
N-formyl-L-kynurenine [CPD:C02700]
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].
Pathway
Tryptophan metabolism
Metabolic pathways
Orthology
K00463  
indoleamine 2,3-dioxygenase
Genes
HSA: 
169355(IDO2) 3620(IDO1)
PTR: 
464134(IDO1) 472744(IDO2)
PPS: 
100969906(IDO2) 100970596(IDO1)
GGO: 
101131712(IDO1) 101134018(IDO2)
PON: 
100435160(IDO2) 100436652(IDO1)
MCC: 
574370(IDO1) 707424(IDO2)
MMU: 
15930(Ido1) 209176(Ido2)
RNO: 
66029(Ido1) 681319(Ido2)
CFA: 
475574(IDO1) 482846(IDO2)
AML: 
FCA: 
101096722(IDO2) 101096977(IDO1)
BTA: 
506281(IDO1)
SSC: 
100519341 100519877(IDO1)
ECB: 
100050681 100056686(IDO2)
MDO: 
100032999(IDO1) 100033003(IDO2)
SHR: 
100926615(IDO1) 100926876(IDO2)
OAA: 
100085939(IDO2) 100086385(IDO1)
GGA: 
426785(INDOL1)
MGP: 
100548413
TGU: 
100219367(IDO2)
ACS: 
100560005
XLA: 
100037099(ido1)
XTR: 
448488(ido1)
DRE: 
571967(ido1)
TRU: 
101074760
OLA: 
101167965
BFO: 
BRAFLDRAFT_126354
SPU: 
577419
BMY: 
Bm1_01790
SMM: 
Smp_133900
NVE: 
NEMVE_v1g244579
CRE: 
CHLREDRAFT_170294
SCE: 
YJR078W(BNA2)
AGO: 
AGOS_ACR188C
ERC: 
Ecym_4655
LTH: 
KLTH0C05412g
PPA: 
PAS_chr1-4_0083
VPO: 
Kpol_520p15
ZRO: 
ZYRO0F13376g
TPF: 
TPHA_0B01500(TPHA0B01500)
TDL: 
TDEL_0C03080(TDEL0C03080)
DHA: 
DEHA2G12188g
PIC: 
PICST_87443(BNA2)
PGU: 
PGUG_04309
LEL: 
LELG_04075
CAL: 
CaO19.583
CTP: 
CTRG_05778
CDU: 
CD36_51480
COT: 
CORT_0F00140
YLI: 
YALI0F26455g
CLU: 
CLUG_01155
NCR: 
NCU01402
SMP: 
SMAC_08377 SMAC_08948 SMAC_08990
PAN: 
PODANSg2504 PODANSg762 PODANSg7893
TTT: 
THITE_2106420 THITE_2110987
MTM: 
MYCTH_2300294 MYCTH_2303249 MYCTH_2307600
MGR: 
MGG_00755 MGG_14348
FGR: 
FG02657.1 FG04828.1 FG09040.1
NHE: 
NECHADRAFT_70501 NECHADRAFT_70795 NECHADRAFT_85363
VAL: 
VDBG_00295 VDBG_04314 VDBG_09667
SSL: 
SS1G_00858 SS1G_08222 SS1G_10307
BFU: 
BC1G_03469 BC1G_09032
ANI: 
AN1858.2 AN2509.2 AN9108.2
NFI: 
NFIA_063050 NFIA_106220 NFIA_114740
AFM: 
AFUA_3G14250 AFUA_4G09830 AFUA_7G02010
AOR: 
AOR_1_1074084(AO090020000618) AOR_1_2200154(AO090003001248) AOR_1_980074(AO090038000578)
ANG: 
ANI_1_1150184(An04g07210) ANI_1_530084(An09g04250) ANI_1_90104(An12g00660)
AFV: 
AFLA_025840 AFLA_071180 AFLA_098110
ACT: 
ACLA_041740 ACLA_049060 ACLA_065510
PCS: 
Pc13g15680 Pc21g12230 Pc22g11860
CIM: 
CIMG_00126 CIMG_07803
CPW: 
CPC735_041970 CPC735_060120
PBL: 
PAAG_05853 PAAG_06866
URE: 
UREG_00231 UREG_02134
ABE: 
ARB_03636 ARB_04584 ARB_05733
TVE: 
TRV_00864 TRV_01957 TRV_04509
AJE: 
HCAG_01148 HCAG_04432
PNO: 
SNOG_02815 SNOG_10574 SNOG_10794
PTE: 
PTT_07650 PTT_08299 PTT_13994
ZTR: 
MYCGRDRAFT_52885 MYCGRDRAFT_73635 MYCGRDRAFT_75056
TML: 
GSTUM_00005398001 GSTUM_00007145001
PPL: 
POSPLDRAFT_102140
LBC: 
LACBIDRAFT_157851 LACBIDRAFT_253793 LACBIDRAFT_256000 LACBIDRAFT_257063 LACBIDRAFT_306113
MPR: 
MPER_12716
CCI: 
CC1G_02499 CC1G_12399
SCM: 
SCHCODRAFT_17654 SCHCODRAFT_33516 SCHCODRAFT_61392
UMA: 
UM03728.1
PGR: 
PGTG_09355
MBR: 
MONBRDRAFT_23639 MONBRDRAFT_31854
TET: 
TTHERM_00035520
NOC: 
Noc_1709
NHL: 
Nhal_1432
ELI: 
ELI_06040
MAI: 
MICA_2463
MAN: 
A11S_2397
ASD: 
AS9A_2778
SCB: 
SCAB_15261
GAU: 
GAU_3278(indO)
SACI: 
Sinac_2518
NDE: 
NIDE0784
HRU: 
Halru_2529
 » show all
Taxonomy
Reference
1  [PMID:6065097]
  Authors
Yamamoto S, Hayaishi O.
  Title
Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes.
  Journal
J. Biol. Chem. 242 (1967) 5260-6.
  Organism
Oryctolagus cuniculus
Reference
2  [PMID:2428037]
  Authors
Yasui H, Takai K, Yoshida R, Hayaishi O.
  Title
Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 6622-6.
  Organism
Homo sapiens [GN:hsa]
Reference
3  [PMID:2419335]
  Authors
Takikawa O, Yoshida R, Kido R, Hayaishi O.
  Title
Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase.
  Journal
J. Biol. Chem. 261 (1986) 3648-53.
  Organism
Mus musculus [GN:mmu]
Reference
4  [PMID:194886]
  Authors
Hirata F, Ohnishi T, Hayaishi O.
  Title
Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex.
  Journal
J. Biol. Chem. 252 (1977) 4637-42.
  Organism
Rattus norvegicus [GN:rno]
Reference
5  [PMID:10719243]
  Authors
Dang Y, Dale WE, Brown OR.
  Title
Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway.
  Journal
Free. Radic. Biol. Med. 28 (2000) 615-24.
  Organism
Homo sapiens [GN:hsa], Rattus norvegicus [GN:rno]
Reference
6  [PMID:12766158]
  Authors
Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.
  Title
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
  Journal
J. Biol. Chem. 278 (2003) 29525-31.
  Organism
Homo sapiens [GN:hsa]
Reference
7  [PMID:10731095]
  Authors
Thomas SR, Stocker R.
  Title
Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway.
  Journal
Redox. Rep. 4 (1999) 199-220.
Reference
8  [PMID:2334706]
  Authors
Sono M.
  Title
Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase.
  Journal
Biochemistry. 29 (1990) 1451-60.
  Organism
Oryctolagus cuniculus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9014-51-1
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