| Entry |
|
|---|
| Name |
tryptophan 2,3-dioxygenase;
tryptophan pyrrolase (ambiguous);
tryptophanase;
tryptophan oxygenase;
tryptamine 2,3-dioxygenase;
tryptophan peroxidase;
indoleamine 2,3-dioxygenase (ambiguous);
indolamine 2,3-dioxygenase (ambiguous);
L-tryptophan pyrrolase;
TDO;
L-tryptophan 2,3-dioxygenase |
|---|
| 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
 |
|---|
| Sysname |
L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing) |
|---|
| Reaction(IUBMB) |
L-tryptophan + O2 = N-formyl-L-kynurenine [RN:R00678] |
|---|
| Reaction(KEGG) |
R00678
 |
|---|
| Substrate |
L-tryptophan [CPD:C00078];
O2 [CPD:C00007] |
|---|
| Product |
N-formyl-L-kynurenine [CPD:C02700] |
|---|
| Cofactor |
Heme [CPD:C00032] |
|---|
| Comment |
A protohemoprotein. In mammals, the enzyme appears to be located
only in the liver. This enzyme, together with EC 1.13.11.52,
indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting
step in the kynurenine pathway, the major pathway of tryptophan
metabolism [5]. The enzyme is specific for tryptophan as substrate,
but is far more active with L-tryptophan than with D-tryptophan [2]. |
|---|
| Pathway |
PATH: ec00380 Tryptophan metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00453 tryptophan 2,3-dioxygenase |
|---|
| Genes |
HSA: 6999(TDO2)
PTR: 736252(TDO2)
MMU: 56720(Tdo2)
RNO: 64206(Tdo2)
CFA: 475476(TDO2)
BTA: 530397(TDO2)
ECB: 100069524
MDO: 100023852
OAA: 100075117
GGA: 422409(TDO2)
TGU: 100220652
XLA: 495495
XTR: 548450
DRE: 100008541(tdo2a) 334082(tdo2b)
BFO: BRAFLDRAFT_210874
CIN: 100181631
SPU: 593764
DME: Dmel_CG2155(v)
DPO: Dpse_GA15272
DAN: Dana_GF20476(Dana_v)
DER: Dere_GG18380
DPE: Dper_GL18243
DSE: Dsec_GM11443
DSI: Dsim_GD16993(Dsim_v)
DYA: Dyak_GE15897(Dyak_v)
DGR: Dgri_GH12679
DMO: Dmoj_GI16256
AGA: AgaP_AGAP002721
AAG: AaeL_AAEL000428
CQU: CpipJ_CPIJ002864
AME: 410828
NVI: 100114839
TCA: 654844(V)
ISC: IscW_ISCW024183
CEL: C28H8.11
CBR: CBG09046
NVE: NEMVE_v1g157887
HMG: 100210202
TAD: TRIADDRAFT_25841
CME: CMT104C
MBR: MONBRDRAFT_33737
DDI: DDB_0231363(tdo)
PLU: plu1434
SPE: Spro_3022
XCC: XCC0432 XCC1210
XCB: XC_0446 XC_3032
XCA: xccb100_0466(tdo)
XCV: XCV0478
XAC: XAC0448
XOO: XOO4075
XOM: XOO_3850
XOP: PXO_04220
SML: Smlt4336
SMT: Smal_3745
PAE: PA2579(kynA)
PAU: PA14_30750
PAP: PSPA7_2637(kynA)
PAG: PLES_27151
PFL: PFL_0753
PFS: PFLU5198
SWD: Swoo_1403
PAT: Patl_0410
AMC: MADE_02822
KKO: Kkor_1547
RSO: RS01755(RSp0694) RSc0758
RPI: Rpic_0708
RPF: Rpic12D_0774
REU: Reut_A0807
REH: H16_A2816(tdo1) H16_B1418(tdo2)
RME: Rmet_2651
CTI: RALTA_A2305
BMA: BMA0351
BMV: BMASAVP1_A0650(kynA)
BML: BMA10229_A2485(kynA)
BMN: BMA10247_0098(kynA)
BPS: BPSL0846
BPM: BURPS1710b_1053
BPL: BURPS1106A_0895(kynA)
BPD: BURPS668_0892(kynA)
BPR: GBP346_A0819(kynA)
BTE: BTH_I0709
BVI: Bcep1808_2701
BUR: Bcep18194_A5910
BCN: Bcen_1968
BCH: Bcen2424_2579
BCM: Bcenmc03_2603
BCJ: BCAL2792
BAM: Bamb_2627
BAC: BamMC406_2498
BMU: Bmul_0718
BMJ: BMULJ_02542(kynA)
BXE: Bxe_A0733
BPH: Bphy_0506
BPY: Bphyt_3229
BGL: bglu_1g29400
BPE: BP1233
BPA: BPP1848
BBR: BB3260
BPT: Bpet3151
BAV: BAV2407
POL: Bpro_3590
PNA: Pnap_3020
AAV: Aave_1155
DAC: Daci_2161 Daci_2170
DIA: Dtpsy_2440
VAP: Vapar_1447 Vapar_5416
CTT: CtCNB1_3657
BBA: Bd1810
ADE: Adeh_3165
ACP: A2cp1_3356
ANK: AnaeK_3282
MXA: MXAN_7400
SCL: sce8412
HOH: Hoch_0225
MLO: mlr0620
BJA: blr4158
BRA: BRADO1529
BBT: BBta_6511
CCR: CC_2886
CCS: CCNA_02980
CAK: Caul_5244
PZU: PHZ_c2930
SIL: SPOA0409
SIT: TM1040_2226
JAN: Jann_2084
MMR: Mmar10_1469
SAL: Sala_1391
ELI: ELI_14140
RCE: RC1_2780
BAN: BA2751
BAR: GBAA2751
BAA: BA_3277
BAT: BAS2565
BAH: BAMEG_1844(kynA)
BAI: BAA_2815(kynA)
BCE: BC2757
BCA: BCE_2785
BCZ: BCZK2486
BCR: BCAH187_A2806(kynA)
BCB: BCB4264_A2764(kynA)
BCU: BCAH820_2759(kynA)
BCG: BCG9842_B2528(kynA)
BCQ: BCQ_2598
BCX: BCA_2835(kynA)
BCY: Bcer98_1901
BTK: BT9727_2521
BTL: BALH_2476
BWE: BcerKBAB4_2557
BCL: ABC0653
OIH: OB0754
GTN: GTNG_3168
ESI: Exig_0180
EAT: EAT1b_1504
BBE: BBR47_27130
RHA: RHA1_ro01801
RER: RER_09930
ROP: ROP_14750
SCO: SCO3646(SCH10.24c)
SMA: SAV_4526(tdo)
SGR: SGR_3414
ART: Arth_1431
AAU: AAur_2058(kynA)
ACH: Achl_1436
RSA: RSal33209_2215
BCV: Bcav_0960
KSE: Ksed_02210
NCA: Noca_1224
TFU: Tfu_0921
SRO: Sros_6248 Sros_6949
NML: Namu_0590
KRA: Krad_1864
SEN: SACE_4055
SVI: Svir_18450
AMI: Amir_0266 Amir_2024
STP: Strop_3531
SAQ: Sare_0539 Sare_3906
CAI: Caci_1080 Caci_7896
CHU: CHU_1409
CPI: Cpin_1013
PHE: Phep_0260
GFO: GFO_1393(tdo2) GFO_3168
FJO: Fjoh_0731
FPS: FP0228
RBI: RB2501_07855
GVI: glr2058
NPU: Npun_F3126
HAU: Haur_1517
DRA: DR_A0339
DGE: Dgeo_2857
DDR: Deide_2p01440
 |
|---|
| Structures |
PDB: 1YW0 2NOX 3BK9 3E08 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:6600455]
Uchida K, Shimizu T, Makino R, Sakaguchi K, Iizuka T, Ishimura Y,
Nozawa T, Hatano M.
Magnetic and natural circular dichroism of L-tryptophan
2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of
ferric and ferrous high spin forms.
J. Biol. Chem. 258 (1983) 2519-25.
Rattus norvegicus [GN:rno], Pseudomonas acidovorans |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:8806758]
Ren S, Liu H, Licad E, Correia MA.
Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia
coli: structural and functional characterization of the purified
enzyme.
Arch. Biochem. Biophys. 333 (1996) 96-102.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:8349662]
Leeds JM, Brown PJ, McGeehan GM, Brown FK, Wiseman JS.
Isotope effects and alternative substrate reactivities for
tryptophan 2,3-dioxygenase.
J. Biol. Chem. 268 (1993) 17781-6.
Rattus norvegicus [GN:rno], Pseudomonas acidovorans |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:10719243]
Dang Y, Dale WE, Brown OR.
Comparative effects of oxygen on indoleamine 2,3-dioxygenase and
tryptophan 2,3-dioxygenase of the kynurenine pathway.
Free. Radic. Biol. Med. 28 (2000) 615-24.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:12766158]
Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.
Asp274 and his346 are essential for heme binding and catalytic
function of human indoleamine 2,3-dioxygenase.
J. Biol. Chem. 278 (2003) 29525-31.
Homo sapiens [GN:hsa] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.13.11.11
IUBMB Enzyme Nomenclature: 1.13.11.11
ExPASy - ENZYME nomenclature database: 1.13.11.11
BRENDA, the Enzyme Database: 1.13.11.11
CAS: 9014-51-1 |
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