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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.14.16.2

Accepted Name
Tyrosine 3-monooxygenase.
Alternative Name(s)
L-tyrosine hydroxylase.
Tyrosine 3-hydroxylase.
Tyrosine hydroxylase.
Reaction catalysed
L-tyrosine + tetrahydrobiopterin + O(2) <=> L-dopa + 4a-hydroxytetrahydrobiopterin
Cofactor(s)
Fe cation.
Comment(s)
  • Activated by phosphorylation, catalyzed by EC 2.7.11.27.
  • The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7- dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96.
  • The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Cross-references
PROSITEPDOC00316
BRENDA1.14.16.2
EC2PDB1.14.16.2
ExplorEnz1.14.16.2
PRIAM enzyme-specific profiles1.14.16.2
KEGG Ligand Database for Enzyme Nomenclature1.14.16.2
IUBMB Enzyme Nomenclature1.14.16.2
IntEnz1.14.16.2
MEDLINEFind literature relating to 1.14.16.2
MetaCyc1.14.16.2
UniProtKB/Swiss-Prot
O42091, TY3H_ANGAN;  P17289, TY3H_BOVIN;  A8X3V8, TY3H_CAEBR;  
P90986, TY3H_CAEEL;  Q76IQ3, TY3H_CANLF;  P18459, TY3H_DROME;  
P07101, TY3H_HUMAN;  P24529, TY3H_MOUSE;  A0A060X6Z0, TY3H_ONCMY;  
P11982, TY3H_PHASP;  P04177, TY3H_RAT;  O17446, TY3H_SCHMA;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.16.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-