Tyrosine hydroxylase

mammalian protein found in Rattus norvegicus
Protein protein Q28557363
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Tyrosine hydroxylase

Summary

Tyrosine hydroxylase is a protein[1].

Key Facts

  • Tyrosine hydroxylase's instance of is recorded as protein[2].
  • Tyrosine hydroxylase's subclass of is recorded as protein[3].
  • Tyrosine hydroxylase's UniProt protein ID is recorded as P04177[4].
  • Tyrosine hydroxylase's part of is recorded as Aromatic amino acid monoxygenase, C-terminal domain superfamily[5].
  • Tyrosine hydroxylase's part of is recorded as Tyrosine 3-monooxygenase[6].
  • Tyrosine hydroxylase's part of is recorded as Aromatic amino acid hydroxylase superfamily[7].
  • Tyrosine hydroxylase's part of is recorded as Aromatic amino acid hydroxylase, C-terminal domain, protein family[8].
  • Tyrosine hydroxylase's part of is recorded as Tyrosine hydroxylase, conserved site, protein family[9].
  • Tyrosine hydroxylase's part of is recorded as Aromatic amino acid hydroxylase, iron/copper binding site, protein family[10].
  • Tyrosine hydroxylase's has part is recorded as Aromatic amino acid hydroxylase, iron/copper binding site[11].
  • Tyrosine hydroxylase's has part is recorded as Tyrosine hydroxylase, conserved site[12].
  • Tyrosine hydroxylase's has part is recorded as Aromatic amino acid hydroxylase, C-terminal[13].
  • Tyrosine hydroxylase's RefSeq protein ID is recorded as NP_036872[14].
  • Tyrosine hydroxylase's RefSeq protein ID is recorded as XP_038957248[15].
  • Tyrosine hydroxylase's RefSeq protein ID is recorded as XP_038957252[16].
  • Tyrosine hydroxylase's RefSeq protein ID is recorded as XP_038957255[17].
  • Tyrosine hydroxylase's molecular function is recorded as monooxygenase activity[18].
  • Tyrosine hydroxylase's molecular function is recorded as tyrosine 3-monooxygenase activity[19].
  • Tyrosine hydroxylase's molecular function is recorded as iron ion binding[20].
  • Tyrosine hydroxylase's molecular function is recorded as protein binding[21].
  • Tyrosine hydroxylase's molecular function is recorded as ferrous iron binding[22].
  • Tyrosine hydroxylase's molecular function is recorded as ferric iron binding[23].
  • Tyrosine hydroxylase's molecular function is recorded as oxidoreductase activity[24].
  • Tyrosine hydroxylase's molecular function is recorded as amino acid binding[25].
  • Tyrosine hydroxylase's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . Q905695. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . wikidata.org.
  9. [10] . wikidata.org.
  10. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Q20641742. Retrieved . wikidata.org.
  14. [15] . Q20641742. Retrieved . wikidata.org.
  15. [16] . Q20641742. Retrieved . wikidata.org.
  16. [17] . Q20641742. Retrieved . wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . A biochemical and functional protein complex involving dopamine synthesis and transport into synaptic vesicles.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: effects on enzyme stability and activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

📑 Cite this page

Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Tyrosine hydroxylase. Retrieved May 3, 2026, from https://4ort.xyz/entity/tyrosine-hydroxylase-q28557363
MLA “Tyrosine hydroxylase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tyrosine-hydroxylase-q28557363.
BibTeX @misc{4ortxyz_tyrosine-hydroxylase-q28557363_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Tyrosine hydroxylase}}, year = {2026}, url = {https://4ort.xyz/entity/tyrosine-hydroxylase-q28557363}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Tyrosine hydroxylase — https://4ort.xyz/entity/tyrosine-hydroxylase-q28557363 (retrieved 2026-05-03)

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