Tyrosine hydroxylase

TH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTH, Th, DYT14, DYT5b, TYH, tyrosine hydroxylase, Tyrosine hydroxylase
External IDsOMIM: 191290; MGI: 98735; HomoloGene: 307; GeneCards: TH; OMA:TH - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000360
NM_199292
NM_199293

NM_009377

RefSeq (protein)

NP_000351
NP_954986
NP_954987
NP_954986.2
NP_954987.2

NP_033403

Location (UCSC)Chr 11: 2.16 – 2.17 MbChr 7: 142.45 – 142.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA).[5][6] It does so using molecular oxygen (O2), as well as iron (Fe2+) and tetrahydrobiopterin as cofactors. L-DOPA is a precursor for dopamine, which, in turn, is a precursor for the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline). Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines. In humans, tyrosine hydroxylase is encoded by the TH gene,[6] and the enzyme is present in the central nervous system (CNS), peripheral sympathetic neurons and the adrenal medulla.[6] Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs).

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000180176Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000214Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kaufman S (1995). "Tyrosine hydroxylase". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 70. pp. 103–220. doi:10.1002/9780470123164.ch3. ISBN 978-0-470-12316-4. PMID 8638482.
  6. ^ a b c Nagatsu T (1995). "Tyrosine hydroxylase: human isoforms, structure and regulation in physiology and pathology". Essays in Biochemistry. 30: 15–35. PMID 8822146.