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CATH Superfamily 1.10.800.10

Aromatic amino acid hydroxylase

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Aromatic amino acid hydroxylase
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 550: Aromatic amino acid hydroxylase 1

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Phenylalanine 4-monooxygenase. [EC: 1.14.16.1]
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin.
  • The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group.
  • This results in the hydrogen at C-4 migrating to C-3 and in part being retained, a process known as the NIH-shift.
  • 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.
  • Formerly EC 1.14.3.1 and EC 1.99.1.2.
 58 A0A024RBG4 A0A088RV41 A0A0G3VGS7 A0A170YZJ1 A4HGH5 A4I3K7 B0LQU2 B2L7T1 B2L7T2 B3M966
(48 more...)
Tryptophan 5-monooxygenase. [EC: 1.14.16.4]
L-tryptophan + tetrahydrobiopterin + O(2) = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
  • Activated by phosphorylation, catalyzed by a Ca(2+)-activated protein kinase.
  • 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.
 38 A0A0G3VJK8 A0A0J9RMW1 A0A0R3P6T9 A0A139XII3 A0A191B548 A0A191Y1Z8 B3M555 B3NJF1 B4KWR4 B4MM34
(28 more...)
Tyrosine 3-monooxygenase. [EC: 1.14.16.2]
L-tyrosine + tetrahydrobiopterin + O(2) = L-dopa + 4a-hydroxytetrahydrobiopterin.
  • 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.
 38 A0A061IDC3 A0A084W0Q1 A0A086J6L1 A0A086PJS0 A0A0G3VFY8 A0A0G3VI81 A0A0J9RQ65 A0A0Q9X3P9 A8X3V8 B3M9H5
(28 more...)
Camphor 5-monooxygenase. [EC: 1.14.15.1]
(+)-camphor + reduced putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H(2)O.
  • Also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy- 1,2-campholide.
 1 A0A1B2G376
Prephenate dehydratase. [EC: 4.2.1.51]
Prephenate = phenylpyruvate + H(2)O + CO(2).
  • This enzyme in the enteric bacteria also possesses EC 5.4.99.5 activity and converts chorismate into prephenate.
 1 A0A075AQ38
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