KEGG   ENZYME: 1.14.16.2Help
Entry
EC 1.14.16.2                Enzyme                                 

Name
tyrosine 3-monooxygenase;
L-tyrosine hydroxylase;
tyrosine 3-hydroxylase;
tyrosine 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-tyrosine,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-tyrosine + tetrahydrobiopterin + O2 = L-dopa + 4a-hydroxytetrahydrobiopterin [RN:R07212]
Reaction(KEGG)
R07212;
(other) R01815
Show
Substrate
L-tyrosine [CPD:C00082];
tetrahydrobiopterin [CPD:C00272];
O2 [CPD:C00007]
Product
L-dopa [CPD:C00355];
4a-hydroxytetrahydrobiopterin [CPD:C15522]
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.
History
EC 1.14.16.2 created 1972, modified 2003
Pathway
ec00350  Tyrosine metabolism
ec00790  Folate biosynthesis
ec00950  Isoquinoline alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00501  tyrosine 3-monooxygenase
Genes
HSA: 7054(TH)
PTR: 450955(TH)
PPS: 100967895(TH)
GGO: 101135345(TH)
PON: 100454349(TH)
NLE: 100591963(TH)
MCC: 721137(TH)
MCF: 102134074(TH)
CSAB: 103238895(TH)
RRO: 104677105(TH)
RBB: 108539190(TH)
CJC: 100393454(TH)
SBQ: 101037795(TH)
MMU: 21823(Th)
RNO: 25085(Th)
CGE: 100760127(Th)
NGI: 103738985(Th)
HGL: 101721615(Th)
CCAN: 109689795(Th)
TUP: 102482570(TH)
CFA: 403444(TH)
AML: 100483681(TH)
UMR: 103671121(TH)
ORO: 101384343(TH)
FCA: 101090720(TH)
PTG: 102954972(TH)
AJU: 106971078(TH)
BTA: 280707(TH)
BOM: 102274970(TH)
BIU: 109554672(TH)
PHD: 102343816(TH)
CHX: 102179849(TH)
OAS: 101120619(TH)
SSC: 110259705(TH)
CFR: 102508286(TH)
CDK: 105106406(TH)
BACU: 103020745(TH)
LVE: 103086024(TH)
OOR: 101278256(TH)
ECB: 100146648(TH)
EPZ: 103545553
EAI: 106824091(TH)
MYB: 102254096(TH)
MYD: 102756871(TH)
HAI: 109395916(TH)
RSS: 109435669(TH)
LAV: 100665276(TH)
TMU: 101347132
MDO: 100021373
OAA: 100075982
GGA: 395592(TH) 771761(THL)
MGP: 100546438 723977(TH)
APLA: 101794316 101794610(TH)
ACYG: 106035805 106042638(TH)
PMAJ: 107204189 107205413(TH)
CCAE: 111930777(TH) 111931331
CPIC: 101937054(TH) 101942670
XLA: 100037248(th.S) 108710245 108713461(th.L)
DRE: 30384(th)
AMEX: 103023599(th) 103026162
TRU: 101078018(th) 446095(2nd_copy)
OLA: 101168664(th2) 101171548(th)
PRET: 103459397 103466160(th)
BPEC: 110161487 110165894(th)
MALB: 109967816 109967893(th)
CIN: 493867(th)
SPU: 581094
SKO: 100329060(TH)
DME: Dmel_CG10118(ple)
DSI: Dsimw501_GD13115(Dsim_GD13115)
MDE: 101896218
AAG: 23687518
AME: 408930(TyHyd)
BIM: 100750025
BTER: 100646624
SOC: 105194448
AEC: 105145056
ACEP: 105619344
PBAR: 105423652
HST: 105182098
DQU: 106750925
CFO: 105248912
LHU: 105678075
PGC: 109861504
PCF: 106786223
NVI: 100116056
MDL: 103574339
TCA: 654918(Th)
DPA: 109541904
NVL: 108569991
BMOR: 100270767(Th)
PMAC: 106717258
PRAP: 110997603
HAW: 110377808
PXY: 105380496(Th)
API: 100167369
DNX: 107161975
CLEC: 106664402
ZNE: 110829545
FCD: 110862051
TUT: 107359687
CEL: CELE_B0432.5(cat-2)
CBR: CBG07026(Cbr-cat-2)
BMY: Bm1_46865
TSP: Tsp_12013
CRG: 105337798
MYI: 110459086
OBI: 106871451
SHX: MS3_00810
 » show all
Taxonomy
Reference
1  [PMID:6133218]
  Authors
El Mestikawy S, Glowinski J, Hamon M.
  Title
Tyrosine hydroxylase activation in depolarized dopaminergic terminals--involvement of Ca2+-dependent phosphorylation.
  Journal
Nature 302:830-2 (1983)
Reference
2  [PMID:6033458]
  Authors
Ikeda M, Levitt M, Udenfriend S.
  Title
Phenylalanine as substrate and inhibitor of tyrosine hydroxylase.
  Journal
Arch Biochem Biophys 120:420-7 (1967)
DOI:10.1016/0003-9861(67)90259-7
Reference
3  [PMID:14216443]
  Authors
NAGATSU T, LEVITT M, UDENFRIEND S.
  Title
TYROSINE HYDROXYLASE. THE INITIAL STEP IN NOREPINEPHRINE BIOSYNTHESIS.
  Journal
J Biol Chem 239:2910-7 (1964)
Reference
4  [PMID:2872947]
  Authors
Pigeon D, Drissi-Daoudi R, Gros F, Thibault J.
  Title
[Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase]
  Journal
C R Acad Sci III 302:435-8 (1986)
Reference
5  [PMID:9228951]
  Authors
Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC.
  Title
Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases.
  Journal
Nat Struct Biol 4:578-85 (1997)
  Sequence
[rno:25085]
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

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