| Entry |
|
|---|
| Name |
tyrosine 3-monooxygenase;
L-tyrosine hydroxylase;
tyrosine 3-hydroxylase;
tyrosine 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-tyrosine,tetrahydrobiopterin:oxygen oxidoreductase
(3-hydroxylating) |
|---|
| Reaction(IUBMB) |
L-tyrosine + tetrahydrobiopterin + O2 =
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
[RN:R07212] |
|---|
| Reaction(KEGG) |
R07212;
(other) R01815
 |
|---|
| Substrate |
L-tyrosine [CPD:C00082];
tetrahydrobiopterin [CPD:C00272];
O2 [CPD:C00007] |
|---|
| Product |
3,4-dihydroxy-L-phenylalanine [CPD:C00355];
4a-hydroxytetrahydrobiopterin [CPD:C15522] |
|---|
| Cofactor |
Iron [CPD:C00023] |
|---|
| Comment |
The active centre contains mononuclear iron(II). The enzyme is
activated by phosphorylation, catalysed by EC 2.7.11.27, [acetyl-CoA
carboxylase] 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: ec00350 Tyrosine metabolism
PATH: ec00950 Isoquinoline alkaloid biosynthesis
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00501 tyrosine 3-monooxygenase |
|---|
| Genes |
HSA: 7054(TH)
PTR: 450955(TH)
MMU: 21823(Th)
RNO: 25085(Th)
CFA: 403444(TH)
BTA: 280707(TH)
MDO: 100021373
GGA: 395592(TH)
TGU: 100219119
XLA: 100037248(th)
DRE: 30384(th)
BFO: BRAFLDRAFT_233334
SPU: 581094
DME: Dmel_CG10118(ple)
DPO: Dpse_GA10085
DAN: Dana_GF10892
DER: Dere_GG15029
DPE: Dper_GL13238
DYA: Dyak_GE20472
DGR: Dgri_GH15635
DMO: Dmoj_GI12682
AGA: AgaP_AGAP006023
CQU: CpipJ_CPIJ014156
AME: 408930(TyHyd)
NVI: 100116056
TCA: 654918(Th)
API: 100167369
CBR: CBG07026
BMY: Bm1_46865
 |
|---|
| Structures |
PDB: 1TOH 2TOH |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:6133218]
El Mestikawy S, Glowinski J, Hamon M.
Tyrosine hydroxylase activation in depolarized dopaminergic
terminals--involvement of Ca2+-dependent phosphorylation.
Nature. 302 (1983) 830-2.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:6033458]
Ikeda M, Levitt M, Udenfriend S.
Phenylalanine as substrate and inhibitor of tyrosine hydroxylase.
Arch. Biochem. Biophys. 120 (1967) 420-7.
Bos taurus [GN:bta], Cavia porcellus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:14216443]
NAGATSU T, LEVITT M, UDENFRIEND S.
TYROSINE HYDROXYLASE. THE INITIAL STEP IN NOREPINEPHRINE
BIOSYNTHESIS.
J. Biol. Chem. 239 (1964) 2910-7.
Bos taurus [GN:bta] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:2872947]
Pigeon D, Drissi-Daoudi R, Gros F, Thibault J.
[Copurification of tyrosine hydroxylase from rat pheochromocytoma by
protein kinase]
C. R. Acad. Sci. III. 302 (1986) 435-8.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
|
5 [PMID:9228951]
Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens
RC.
Crystal structure of tyrosine hydroxylase at 2.3 A and its
implications for inherited neurodegenerative diseases.
Nat. Struct. Biol. 4 (1997) 578-85. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.16.2
IUBMB Enzyme Nomenclature: 1.14.16.2
ExPASy - ENZYME nomenclature database: 1.14.16.2
BRENDA, the Enzyme Database: 1.14.16.2
CAS: 9036-22-0 |
|---|
