EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O2
EC 18.104.22.168 - Tyrosine 3-monooxygenase
IntEnz Enzyme Nomenclature
18201 [IUBMB](6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(6R)-L-erythro-5,6,7,8-tetrahydrobiopterinName origin: UniProt - CHECKED (C)Formula: C9H15N5O3
Charge: 0ChEBI compound status: CHECKED (C)L-tyrosineL-tyrosineName origin: UniProt - CHECKED (C)Formula: C9H11NO3
Charge: 0ChEBI compound status: CHECKED (C)O2O2Name origin: UniProt - CHECKED (C)Formula: O2
Charge: 0ChEBI compound status: CHECKED (C)<?>4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterinName origin: UniProt - CHECKED (C)Formula: C9H15N5O4
Charge: 0ChEBI compound status: CHECKED (C)
The active centre contains mononuclear iron(II). The enzyme is activated by phosphorylation, catalysed by EC 22.214.171.124, [aceteyl-CoA caboxylase]kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 126.96.36.199, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 188.8.131.52 (6,7-dihydropteridine reductase), or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Links to other databases
Tyrosine hydroxylase activation in depolarized dopaminergic terminals -involvement of Ca2+-dependent phosphorylation.Nature (Lond.) 302: 830-832 (1983). [PMID: 6133218]
Phenylalanine as substrate and inhibitor of tyrosine hydroxylase.Arch. Biochem. Biophys. 120: 420-427 (1967). [PMID: 6033458]
Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis.J. Biol. Chem. 239: 2910-2917 (1964).
Copurification of tyrosine-hydroxylase from rat pheochromocytoma, with a protein-kinase activity.C.R. Acad. Sci. Paris, Ser. 3, 302: 435-438 (1986). [PMID: 2872947]
Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases.Nat. Struct. Biol. 4: 578-585 (1997). [PMID: 9228951]
[EC 184.108.40.206 created 1972, modified 2003]