| Entry |
|
|---|
| Name |
tryptophan 5-monooxygenase;
L-tryptophan hydroxylase;
indoleacetic acid-5-hydroxylase;
tryptophan 5-hydroxylase;
tryptophan hydroxylase |
|---|
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With reduced pteridine as one donor, and incorporation of one atom
of oxygen into the other donor
 |
|---|
| 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
 |
|---|
| Substrate |
L-tryptophan [CPD:C00078];
tetrahydrobiopterin [CPD:C00272];
O2 [CPD:C00007] |
|---|
| Product |
5-hydroxy-L-tryptophan [CPD:C00643];
4a-hydroxytetrahydrobiopterin [CPD:C15522] |
|---|
| Cofactor |
Iron [CPD:C00023] |
|---|
| 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. |
|---|
| Pathway |
PATH: ec00380 Tryptophan metabolism
PATH: ec01063 Biosynthesis of alkaloids derived from shikimate
pathway
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00502 tryptophan 5-monooxygenase |
|---|
| Genes |
HSA: 121278(TPH2) 7166(TPH1)
PTR: 466453(SERGEF) 467070(TPH2)
MCC: 664730(TPH2) 695363(TPH1)
MMU: 216343(Tph2) 21990(Tph1)
RNO: 24848(Tph1) 317675(Tph2)
CFA: 481165(TPH2) 611956(SERGEF)
BTA: 618062 781941(SERGEF)
SSC: 100154806
ECB: 100009684(TPH2) 100056614
MDO: 100011937 100020009
OAA: 100090381
GGA: 395799(SERGEF) 408026(TPH2)
TGU: 100228542 100229598
XLA: 387560(tph1)
DRE: 352943(tph1a) 407712(tph2)
DAN: Dana_GF10077
DER: Dere_GG14621
DPE: Dper_GL24728
DSE: Dsec_GM14234
DSI: Dsim_GD13494
DYA: Dyak_GE20982
DMO: Dmoj_GI12709
AGA: AgaP_AGAP006020
CQU: CpipJ_CPIJ019741
AME: 411200
NVI: 100123183
TCA: 655758
API: 100158737
ISC: IscW_ISCW000796
TET: TTHERM_00997520
 |
|---|
| Structures |
PDB: 1MLW 3E2T 3HF6 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:4402511]
Friedman PA, Kappelman AH, Kaufman S.
Partial purification and characterization of tryptophan hydroxylase
from rabbit hindbrain.
J. Biol. Chem. 247 (1972) 4165-73.
Oryctolagus cuniculus |
|---|
Reference
Authors
Title
Journal
Organism
|
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 (1979) 1031-42.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
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 (1970) 1699-709.
Cavia porcellus |
|---|
Reference
Authors
Title
Journal
Organism
|
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 (1969) 1071-81.
Bos taurus [GN:bta] |
|---|
Reference
Authors
Title
Journal
Organism
|
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 (2002) 12569-74.
Homo sapiens [GN:hsa] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.16.4
IUBMB Enzyme Nomenclature: 1.14.16.4
ExPASy - ENZYME nomenclature database: 1.14.16.4
BRENDA, the Enzyme Database: 1.14.16.4
CAS: 9037-21-2 |
|---|
