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
Tyrosine metabolism
Isoquinoline alkaloid biosynthesis
Metabolic pathways
Orthology
K00501  
tyrosine 3-monooxygenase
Genes
HSA: 
7054(TH)
PTR: 
450955(TH)
PPS: 
GGO: 
PON: 
NLE: 
MCC: 
721137(TH)
MCF: 
CJC: 
MMU: 
21823(Th)
RNO: 
25085(Th)
CGE: 
HGL: 
TUP: 
CFA: 
403444(TH)
AML: 
UMR: 
FCA: 
PTG: 
BTA: 
280707(TH)
BOM: 
PHD: 
CHX: 
OAS: 
CFR: 
BACU: 
LVE: 
ECB: 
MYD: 
PALE: 
MDO: 
OAA: 
GGA: 
MGP: 
APLA: 
TGU: 
FAB: 
PHI: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
PBI: 
XLA: 
XTR: 
DRE: 
30384(th)
TRU: 
101078018(th) 446095(2nd_copy)
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
CIN: 
493867(th)
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
CQU: 
AME: 
408930(TyHyd)
NVI: 
TCA: 
654918(Th)
BMOR: 
API: 
PHU: 
ISC: 
CBR: 
CBG07026(Cbr-cat-2)
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
SMM: 
 » 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 (1983) 830-2.
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 (1967) 420-7.
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 (1964) 2910-7.
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 (1986) 435-8.
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 (1997) 578-85.
  Sequence
[rno:25085]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9036-22-0

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