Pathways & interactions
Aromatic amino acid monoxygenase, C-terminal domain superfamily (IPR036329)
Short name: Aro-AA_hydroxylase_C_sf
- Aromatic amino acid hydroxylase (IPR001273)
- Phenylalanine-4-hydroxylase, monomeric form (IPR005960)
- Phenylalanine-4-hydroxylase, tetrameric form (IPR005961)
- Tyrosine 3-monooxygenase (IPR005962)
- Tryptophan 5-monooxygenase (IPR005963)
- Aromatic amino acid hydroxylase, iron/copper binding site (IPR018301)
- Tyrosine 3-monooxygenase-like (IPR019773)
- Aromatic amino acid hydroxylase, C-terminal (IPR019774)
- Aromatic amino acid hydroxylase superfamily (IPR036951)
- Tyrosine 3-monooxygenase, catalytic domain (IPR041903)
- Tryptophan 5-hydroxylase, catalytic domain (IPR041904)
- Eukaryotic phenylalanine-4-hydroxylase, catalytic domain (IPR041912)
Hydroxylation of the aromatic amino acids phenylalanine, tyrosine and tryptophan is carried out by a family of non-heme iron and tetrahydrobiopterin (BH4) dependent enzymes: the aromatic amino acid hydroxylase [PMID: 3475690]. Theseenzymes are structurally and functionally similar. The eukaryotic forms include a regulatory N-terminal domain, a catalytic domain and a C-terminal oligomerization motif. The eukaryotic enzymes are all homotetramers [PMID: 14640675, PMID: 15537351].
Three-dimensional structures have been determined for the three types of enzymes. The iron atom is bound to three amino acid residues, two close histidine and a more distant acidic residue. This arrangement of ligands has been observed in a number of metalloproteins with divergent function [PMID: 11718561].
Enzymes that belong to the aromatic amino acid hydroxylase family are listed below:
- Phenylalanine-4-hydroxylase (EC:18.104.22.168) (PAH). Catalyzes the conversion of phenylalanine to tyrosine. In humans, deficiencies [PMID: 8594560] of PAH are the cause of phenylketonuria, the most common inborn error of amino acid metabolism. In the bacteria Chromobacterium violaceum [PMID: 1655752], PAH is copper-dependent; it is iron-dependent in Pseudomonas aeruginosa [PMID: 8108417].
- Tyrosine 3-hydroxylase (EC:22.214.171.124) (TYH). Catalyzes the rate limiting step in catecholamine biosynthesis: the conversion of tyrosine to 3,4- dihydroxy-L-phenylalanine.
- Tryptophan 5-hydroxylase (EC:126.96.36.199) (TRH). Catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of tryptophan to 3-hydroxy- anthranilate.
This entry represents a domain containing the catalytic domain and the coiled-coil C-terminal oligomerization motif.
- SSF56534 (SSF56534)