EC                Enzyme                                 

tryptophan 5-monooxygenase;
L-tryptophan hydroxylase;
indoleacetic acid-5-hydroxylase;
tryptophan 5-hydroxylase;
tryptophan hydroxylase
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
L-tryptophan,tetrahydrobiopterin:oxygen oxidoreductase (5-hydroxylating)
L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin [RN:R07213]
(other) R01814
L-tryptophan [CPD:C00078];
tetrahydrobiopterin [CPD:C00272];
O2 [CPD:C00007]
5-hydroxy-L-tryptophan [CPD:C00643];
4a-hydroxytetrahydrobiopterin [CPD:C15522]
The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by a Ca2+-activated protein kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC (6,7-dihydropteridine reductase), or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
EC created 1972, modified 2003
ec00380  Tryptophan metabolism
ec00790  Folate biosynthesis
ec01100  Metabolic pathways
K00502  tryptophan 5-monooxygenase
HSA: 121278(TPH2) 7166(TPH1)
PTR: 466453(TPH1) 467070(TPH2)
PPS: 100977344(TPH2) 103782654(TPH1)
GGO: 101132108(TPH1) 101146582(TPH2)
PON: 100459809(TPH2) 103891844(TPH1)
NLE: 100588345(TPH2) 100601780(TPH1)
MCC: 664730(TPH2) 695363(TPH1)
MCF: 102124167(TPH2) 102145077(TPH1)
CSAB: 103238730(TPH2) 103239320(TPH1)
RRO: 104667637(TPH1) 104668095(TPH2)
RBB: 108526665(TPH2) 108528377(TPH1)
CJC: 100403096(TPH2) 100415029(TPH1)
SBQ: 101051709(TPH2) 104652952(TPH1)
MMU: 216343(Tph2) 21990(Tph1)
RNO: 24848(Tph1) 317675(Tph2)
CGE: 100763947(Tph2) 100767923(Tph1)
NGI: 103734460(Tph1) 103735331(Tph2)
HGL: 101710219(Tph1) 101714361(Tph2)
CCAN: 109675533 109679995(Tph1)
OCU: 100009100(TPH1) 100101558(TPH1) 100344397(TPH2)
TUP: 102481223(TPH2) 102487889(TPH1)
CFA: 481165(TPH2) 611956(TPH1)
AML: 100467699(TPH1) 100472165(TPH2)
UMR: 103656892(TPH2) 103679407(TPH1)
ORO: 101364741(TPH1) 101369839(TPH2)
FCA: 101082165(TPH2) 101098575(TPH1)
PTG: 102948910(TPH2) 102969936(TPH1)
AJU: 106967384(TPH2) 106977480(TPH1)
BTA: 100336620(TPH2) 781941(TPH1)
BOM: 102269915(TPH1) 102275621(TPH2)
BIU: 109558652(TPH2) 109569943(TPH1)
PHD: 102324712(TPH2) 102328991(TPH1)
CHX: 102174722(TPH2) 102184739(TPH1)
OAS: 101113620(TPH1) 101120314(TPH2)
SSC: 100511002(TPH1) 100627725(TPH2)
CFR: 102512650(TPH2) 102522464(TPH1)
CDK: 105086665(TPH1) 105095994(TPH2)
BACU: 102997866(TPH1) 103006656(TPH2)
LVE: 103083324(TPH1) 103087968(TPH2)
OOR: 101271217(TPH2) 101273510(TPH1)
ECB: 100009684(TPH2) 100056614(TPH1)
EPZ: 103559190(TPH1) 103561950(TPH2)
EAI: 106826108(TPH2) 106835485(TPH1)
MYB: 102241626(TPH2) 102244804(TPH1)
MYD: 102753485(TPH2) 102767513(TPH1)
HAI: 109387680(TPH2) 109388096(TPH1)
RSS: 109436423(TPH1) 109456565(TPH2)
PALE: 102882683(TPH1) 102891331(TPH2)
LAV: 100658860(TPH1) 100669911(TPH2) 104847369
MDO: 100011937(TPH2) 100020009(TPH1)
SHR: 100915442(TPH1) 100923184(TPH2) 111721271
OAA: 100090381(TPH1)
GGA: 395799(TPH1) 408026(TPH2)
MGP: 100303678(TPH2) 100549515(TPH1)
CJO: 107310284(TPH2) 107314681(TPH1)
APLA: 101793780(TPH2) 101797806(TPH1) 106015262
TGU: 100228542(TPH2) 100229598(TPH1)
GFR: 102036017(TPH2) 102041307(TPH1)
FAB: 101817911(TPH2) 101820220(TPH1)
PHI: 102103962(TPH2) 102106431(TPH1)
PMAJ: 107204683(TPH2) 107205260(TPH1)
CCW: 104685325(TPH1) 104698473(TPH2)
FPG: 101914983(TPH1) 101918183(TPH2)
FCH: 102052919(TPH2) 102057315(TPH1)
CLV: 102092014(TPH2) 102095810(TPH1)
EGZ: 104123206(TPH1) 104132957(TPH2)
AAM: 106488161(TPH2) 106497047(TPH1)
ASN: 102376121(TPH2) 102380987(TPH1)
AMJ: 102560538(TPH1) 102572294(TPH2)
PSS: 102445658(TPH2) 102460535(TPH1)
CMY: 102930035(TPH2) 102934830
CPIC: 101933912(TPH2) 101948172(TPH1)
ACS: 100562860(tph1) 100564918(tph2)
PVT: 110084890(TPH2) 110088804(TPH1)
GJA: 107115340(TPH2) 107115550(TPH1)
XLA: 108710258 108713144(tph2) 387560(tph1.L)
XTR: 100486097(tph2) 100497239(tph1)
NPR: 108785999(TPH1) 108788312(TPH2)
DRE: 352943(tph1a) 407712(tph2) 415103(tph1b)
IPU: 108259139(tph) 108263971 108274454(tph1)
TRU: 446047(tph1) 446048(tph2)
LCO: 104921438 104932027(tph1) 104938290(tph2)
MZE: 101480764(tph2) 101484460 101486409(tph1)
OLA: 101166957(tph2) 101170994 101175562(tph1)
XMA: 102216868(tph1) 102234879 102236889(tph2)
PRET: 103462259 103466377(tph2) 103466482(tph1)
NFU: 107381938 107388661(tph1) 107389098(tph2)
CSEM: 103379608(tph2) 103380212(tph1)
LCF: 108876698(tph1) 108891738(tph2)
HCQ: 109507516(tph1) 109518199(tph2) 109529786
BPEC: 110162577 110168313(tph2) 110169358(tph1)
ELS: 105018201(tph1) 105018238(tph2)
LCM: 102362567(TPH1) 102363250(TPH2)
CMK: 103174831(tph1) 103185330(tph2)
CIN: 100049066
SPU: 578903
APLC: 110981081
SKO: 100329006(tph-1)
DME: Dmel_CG9122(Trh)
DSI: Dsimw501_GD13494(Dsim_GD13494)
MDE: 101893101
AAG: 23687540
AME: 411200(Trh)
BIM: 100742465
BTER: 100647460
SOC: 105194454
AEC: 105145053
ACEP: 105619346
PBAR: 105430282
HST: 105182103
CFO: 105251016
LHU: 105678051
PGC: 109861523
NVI: 100123183
TCA: 655758
DPA: 109539121
NVL: 108562706
BMOR: 101740691
PMAC: 106717008
PRAP: 110999042
PXY: 105389797
API: 100158737
DNX: 107164769
ZNE: 110836317
FCD: 110856969
TUT: 107363777
TSP: Tsp_05203
CRG: 105336312
MYI: 110454322
OBI: 106875341
LAK: 106175748
SHX: MS3_06981
APRO: F751_2362
 » show all
1  [PMID:4402511]
Friedman PA, Kappelman AH, Kaufman S.
Partial purification and characterization of tryptophan hydroxylase from rabbit hindbrain.
J Biol Chem 247:4165-73 (1972)
2  [PMID:315449]
Hamon M, Bourgoin S, Artaud F, Glowinski J.
The role of intraneuronal 5-HT and of tryptophan hydroxylase activation in the control of 5-HT synthesis in rat brain slices incubated in K+-enriched medium.
J Neurochem 33:1031-42 (1979)
3  [PMID:5309585]
Ichiyama A, Nakamura S, Nishizuka Y, Hayaishi O.
Enzymic studies on the biosynthesis of serotonin in mammalian brain.
J Biol Chem 245:1699-709 (1970)
4  [PMID:5789774]
Jequier E, Robinson DS, Lovenberg W, Sjoerdsma A.
Further studies on tryptophan hydroxylase in rat brainstem and beef pineal.
Biochem Pharmacol 18:1071-81 (1969)
5  [PMID:12379098]
Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC.
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.
Biochemistry 41:12569-74 (2002)
Other DBs
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IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 9037-21-2

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