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 incorporation of molecular oxygen (oxygenases);
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].
History
EC 1.13.11.52 created 2006
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)
MCF: 
102126825(IDO1) 102129002(IDO2)
MMU: 
15930(Ido1) 209176(Ido2)
RNO: 
66029(Ido1) 681319(Ido2)
CGE: 
100754111(Ido2) 100754402(Ido1)
HGL: 
101723386(Ido2) 101723745(Ido1)
TUP: 
102485305(IDO2) 102494474(IDO1)
CFA: 
475574(IDO1) 482846(IDO2)
AML: 
FCA: 
101096722(IDO2) 101096977(IDO1)
PTG: 
102959839(IDO2) 102969142(IDO1)
BTA: 
506281(IDO1) 513810(IDO2)
BOM: 
102264395(IDO1) 102267516(IDO2)
PHD: 
102314881(IDO2) 102344186(IDO1)
CHX: 
102184119(IDO1) 102184590(IDO2)
OAS: 
100196903(IDO1) 101120548(IDO2)
SSC: 
CFR: 
BACU: 
102998882(IDO1) 102999165(IDO2)
LVE: 
103068351(IDO2) 103068620(IDO1)
ECB: 
100056686(IDO2)
MYB: 
102256119(IDO1) 102256420(IDO2)
MYD: 
102755941(IDO2) 102756580(IDO1)
PALE: 
102878670(IDO2) 102896453(IDO1)
MDO: 
100032999(IDO1) 100033003(IDO2)
SHR: 
100926615(IDO1) 100926876(IDO2)
OAA: 
100085939(IDO2) 100086385(IDO1)
GGA: 
426785(INDOL1)
MGP: 
TGU: 
100219367(IDO2)
FAB: 
101810571(IDO2)
PHI: 
102102902(IDO2)
APLA: 
101791377(IDO2)
FPG: 
101914440(IDO2)
FCH: 
102055026(IDO2)
CLV: 
102086320(IDO2)
ASN: 
102376360(IDO2)
AMJ: 
102565729(IDO2)
PSS: 
102453712(IDO2) 102455437(IDO1)
CMY: 
102945834(IDO2) 102946062(IDO1)
ACS: 
PBI: 
103053378(IDO2)
XLA: 
100037099(ido1)
XTR: 
448488(ido1)
DRE: 
571967(ido1)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102364348(IDO2)
CMK: 
BFO: 
SPU: 
BMY: 
LOA: 
TSP: 
SMM: 
NVE: 
CRE: 
CVR: 
SCE: 
YJR078W(BNA2)
AGO: 
ERC: 
LTH: 
PPA: 
VPO: 
ZRO: 
TPF: 
TPHA_0B01500(TPHA0B01500)
TDL: 
TDEL_0C03080(TDEL0C03080)
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
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: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
TMS: 
PPL: 
DSQ: 
SHS: 
PCO: 
PSQ: 
ADL: 
FME: 
GTR: 
LBC: 
MPR: 
MRR: 
CCI: 
SCM: 
ABP: 
AGABI1DRAFT107428(AGABI1DRAFT_107428) AGABI1DRAFT34575(AGABI1DRAFT_34575) AGABI1DRAFT60207(AGABI1DRAFT_60207) AGABI1DRAFT85862(AGABI1DRAFT_85862)
ABV: 
AGABI2DRAFT135051(AGABI2DRAFT_135051) AGABI2DRAFT177539(AGABI2DRAFT_177539) AGABI2DRAFT177540(AGABI2DRAFT_177540) AGABI2DRAFT64740(AGABI2DRAFT_64740)
CPUT: 
SLA: 
UMA: 
PFP: 
PGR: 
MLR: 
WSE: 
MBR: 
TET: 
EHX: 
GTT: 
NOC: 
NHL: 
ELI: 
MAI: 
MAN: 
ASD: 
SCB: 
MMAR: 
GAU: 
GAU_3278(indO)
SACI: 
FGI: 
NDE: 
HRU: 
 » 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
  Sequence
[hsa:3620]
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
  Sequence
[mmu:15930]
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
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, Rattus norvegicus
  Sequence
[rno:66029]
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
  Sequence
[hsa:3620]
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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