KEGG   ENZYME: 1.14.16.2
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
Sysname
L-tyrosine,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-tyrosine + a 5,6,7,8-tetrahydropteridine + O2 = L-dopa + a 4a-hydroxy-5,6,7,8-tetrahydropteridine [RN:R12541]
Reaction(KEGG)
R12541;
(other) R01815 R07212
Substrate
L-tyrosine [CPD:C00082];
5,6,7,8-tetrahydropteridine [CPD:C05650];
O2 [CPD:C00007]
Product
L-dopa [CPD:C00355];
4a-hydroxy-5,6,7,8-tetrahydropteridine [CPD:C22239]
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-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine.
History
EC 1.14.16.2 created 1972, modified 2003, modified 2019
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)
MCAL: 110298803(Th)
MPAH: 110327669(Th)
RNO: 25085(Th)
MUN: 110547270(Th)
NGI: 103738985(Th)
HGL: 101721615(Th)
CCAN: 109689795(Th)
TUP: 102482570(TH)
CFA: 403444(TH)
VVP: 112924141(TH)
AML: 100483681(TH)
UMR: 103671121(TH)
UAH: 113243914(TH)
ORO: 101384343(TH)
ELK: 111149999
FCA: 101090720(TH)
PTG: 102954972(TH)
PPAD: 109259420(TH)
AJU: 106971078(TH)
BTA: 280707(TH)
BOM: 102274970(TH)
BIU: 109554672(TH)
BBUB: 102395073(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)
DLE: 111184074(TH)
PCAD: 102996827(TH)
ECB: 100146648(TH)
EAI: 106824091(TH)
MYD: 102756871(TH)
MNA: 107539915(TH)
HAI: 109395916(TH)
DRO: 112317145(TH)
RAY: 107513264(TH)
MJV: 108402611(TH)
TMU: 101347132
MDO: 100021373
GGA: 395592(TH) 771761(THL)
MGP: 723977(TH)
NMEL: 110398023 110401820(TH)
APLA: 101794316 101794610(TH)
ACYG: 106035805 106042638(TH)
SCAN: 103819711 103826755(TH)
PMAJ: 107204189 107205413(TH)
CCAE: 111930777(TH) 111931331
ACUN: 113481167(TH) 113488615
PADL: 103920696(TH) 103924526
CPIC: 101937054(TH) 101942670
PMUR: 107289468 107294041(TH)
PMUA: 114599115(TH) 114605512
XLA: 100037248(th.S) 108710245 108713461(th.L)
XTR: 100488900(th) 100495856(th2)
DRE: 30384(th) 414844(th2)
PHYP: 113529896(th) 113532096
AMEX: 103023599(th) 103026162
TRU: 101078018(th) 446095
OLA: 101168664(th2) 101171548(th)
PRET: 103459397 103466160(th)
ALIM: 106515667(th) 106530261
AOCE: 111582533(th) 111586653
SLAL: 111661851(th) 111664688
BPEC: 110161487 110165894(th)
MALB: 109967816 109967893(th)
SALP: 111961998(th) 111982828
CIN: 493867(th)
SPU: 581094
SKO: 100329060(TH)
DME: Dmel_CG10118(ple)
DER: 6544948
DSE: 6611046
DSI: Dsimw501_GD13115(Dsim_GD13115)
DAN: 6493759
DSR: 110178770
DPE: 6601668
DMN: 108153568
DWI: 6645135
DAZ: 108614271
DNV: 108652194
DHE: 111600489
DVI: 6623552
MDE: 101896218
LCQ: 111683620
AAG: 23687518
AALB: 109413955
AME: 408930(TyHyd)
BIM: 100750025
BTER: 100646624
CCAL: 108629537
OBB: 114876902
SOC: 105194448
MPHA: 105838942
AEC: 105145056
ACEP: 105619344
PBAR: 105423652
VEM: 105567121
HST: 105182098
DQU: 106750925
CFO: 105248912
LHU: 105678075
PGC: 109861504
OBO: 105279021
PCF: 106786223
NVI: 100116056
CSOL: 105360534
MDL: 103574339
TCA: 654918(Th)
DPA: 109541904
ATD: 109599398
NVL: 108569991
BMOR: 100270767(Th)
BMAN: 114244521
PMAC: 106717258
PRAP: 110997603
HAW: 110377808
TNL: 113493935
PXY: 105380496(Th)
API: 100167369
DNX: 107161975
AGS: 114123079
RMD: 113554456
BTAB: 109044321
CLEC: 106664402
ZNE: 110829545
FCD: 110862051
PVM: 113810884
TUT: 107359687
DPTE: 113794892
CSCU: 111638578
CEL: CELE_B0432.5(cat-2)
CBR: CBG07026(Cbr-cat-2)
BMY: Bm1_46865
TSP: Tsp_12013
PCAN: 112566735
CRG: 105337798
MYI: 110459086
OBI: 106871451
SHX: MS3_00810
 » show all
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)
DOI:10.1038/302830a0
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)
DOI:10.1038/nsb0797-578
  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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