Biopterin-dependent aromatic amino acid hydroxylase
| Biopterin_H | |||||||||
|---|---|---|---|---|---|---|---|---|---|
crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (Fe(II)) complexed with tetrahydrobiopterin and norleucine | |||||||||
| Identifiers | |||||||||
| Symbol | Biopterin_H | ||||||||
| Pfam | PF00351 | ||||||||
| InterPro | IPR019774 | ||||||||
| PROSITE | PDOC00316 | ||||||||
| SCOP2 | 1toh / SCOPe / SUPFAM | ||||||||
| CDD | cd00361 | ||||||||
| |||||||||
Biopterin-dependent aromatic amino acid hydroxylases (AAAH) are a family of aromatic amino acid hydroxylase enzymes which includes phenylalanine 4-hydroxylase (EC 1.14.16.1), tyrosine 3-hydroxylase (EC 1.14.16.2), and tryptophan 5-hydroxylase (EC 1.14.16.4). These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively.
The AAAH enzymes are functionally and structurally related proteins which act as rate-limiting catalysts for important metabolic pathways. Each AAAH enzyme contains iron and catalyzes the ring hydroxylation of aromatic amino acids using tetrahydrobiopterin (BH4) as a substrate. The AAAH enzymes are regulated by phosphorylation at serines in their N-termini.