KEGG   ENZYME: 1.14.16.4Help
Entry
EC 1.14.16.4                Enzyme                                 

Name
tryptophan 5-monooxygenase;
L-tryptophan hydroxylase;
indoleacetic acid-5-hydroxylase;
tryptophan 5-hydroxylase;
tryptophan hydroxylase
Class
Oxidoreductases;
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
Sysname
L-tryptophan,tetrahydrobiopterin:oxygen oxidoreductase (5-hydroxylating)
Reaction(IUBMB)
L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin [RN:R07213]
Reaction(KEGG)
R07213;
(other) R01814
Show
Substrate
L-tryptophan [CPD:C00078];
tetrahydrobiopterin [CPD:C00272];
O2 [CPD:C00007]
Product
5-hydroxy-L-tryptophan [CPD:C00643];
4a-hydroxytetrahydrobiopterin [CPD:C15522]
Comment
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 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34 (6,7-dihydropteridine reductase), or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
History
EC 1.14.16.4 created 1972, modified 2003
Pathway
Tryptophan metabolism
Metabolic pathways
Orthology
K00502  
tryptophan 5-monooxygenase
Genes
HSA: 
121278(TPH2) 7166(TPH1)
PTR: 
466453(TPH1) 467070(TPH2)
PPS: 
100977344(TPH2) 100982654(SERGEF)
GGO: 
101132108(TPH1) 101146582(TPH2)
PON: 
100459809(TPH2)
NLE: 
100588345(TPH2) 100601780(TPH1)
MCC: 
664730(TPH2) 695363(TPH1)
MCF: 
102124167(TPH2) 102145077(TPH1)
CJC: 
100403096(TPH2) 100415029(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)
OCU: 
100009100(TPH1) 100101558(TPH1) 100344397(TPH2)
TUP: 
102481223(TPH2) 102487889(TPH1)
CFA: 
481165(TPH2) 611956(TPH1)
AML: 
UMR: 
103656892(TPH2) 103679407(TPH1)
FCA: 
101082165(TPH2) 101098575(TPH1)
PTG: 
102948910(TPH2) 102969936(TPH1)
BTA: 
BOM: 
102269915(TPH1) 102275621(TPH2)
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)
BACU: 
102997866(TPH1) 103006656(TPH2)
LVE: 
103083324(TPH1) 103087968(TPH2)
ECB: 
100009684(TPH2) 100056614(TPH1)
MYB: 
102241626(TPH2) 102244804(TPH1)
MYD: 
102753485(TPH2) 102767513(TPH1)
PALE: 
102882683(TPH1) 102891331(TPH2)
MDO: 
100011937(TPH2) 100020009(TPH1)
SHR: 
OAA: 
100090381(TPH1)
GGA: 
395799(TPH1) 408026(TPH2)
MGP: 
APLA: 
TGU: 
100228542(TPH2) 100229598(TPH1)
FAB: 
101817911(TPH2) 101820220(TPH1)
PHI: 
102103962(TPH2) 102106431(TPH1)
FPG: 
101914983(TPH1) 101918183(TPH2)
FCH: 
102052919(TPH2) 102057315(TPH1)
CLV: 
102092014(TPH2) 102095810(TPH1)
ASN: 
AMJ: 
PSS: 
102445658(TPH2) 102460535(TPH1)
CMY: 
ACS: 
100562860(tph1) 100564918(tph2)
PBI: 
XLA: 
387560(tph1)
XTR: 
DRE: 
352943(tph1a) 407712(tph2) 415103(tph1b)
TRU: 
446047(tph1) 446048(tph2)
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
103174831(tph1) 103185330(tph2)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
CQU: 
AME: 
411200(Trh)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
LOA: 
TSP: 
HRO: 
LGI: 
 » show all
Taxonomy
Reference
1  [PMID:4402511]
  Authors
Friedman PA, Kappelman AH, Kaufman S.
  Title
Partial purification and characterization of tryptophan hydroxylase from rabbit hindbrain.
  Journal
J. Biol. Chem. 247 (1972) 4165-73.
Reference
2  [PMID:315449]
  Authors
Hamon M, Bourgoin S, Artaud F, Glowinski J.
  Title
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.
  Journal
J. Neurochem. 33 (1979) 1031-42.
Reference
3  [PMID:5309585]
  Authors
Ichiyama A, Nakamura S, Nishizuka Y, Hayaishi O.
  Title
Enzymic studies on the biosynthesis of serotonin in mammalian brain.
  Journal
J. Biol. Chem. 245 (1970) 1699-709.
Reference
4  [PMID:5789774]
  Authors
Jequier E, Robinson DS, Lovenberg W, Sjoerdsma A.
  Title
Further studies on tryptophan hydroxylase in rat brainstem and beef pineal.
  Journal
Biochem. Pharmacol. 18 (1969) 1071-81.
Reference
5  [PMID:12379098]
  Authors
Wang L, Erlandsen H, Haavik J, Knappskog PM, Stevens RC.
  Title
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin.
  Journal
Biochemistry. 41 (2002) 12569-74.
  Sequence
[hsa:7166]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9037-21-2

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