Biopterin-dependent aromatic amino acid hydroxylase GudangMovies21 Rebahinxxi LK21

    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.


    Role in metabolism


    In humans, phenylalanine hydroxylase deficiency can cause phenylketonuria, the most common inborn error of amino acid metabolism. Phenylalanine hydroxylase catalyzes the conversion of L-phenylalanine to L-tyrosine. Tyrosine hydroxylase catalyzes the rate-limiting step in catecholamine biosynthesis: the conversion of L-tyrosine to L-DOPA. Similarly, tryptophan hydroxylase catalyzes the rate-limiting step in serotonin biosynthesis: the conversion of L-tryptophan to 5-hydroxy-L-tryptophan.


    Structure


    It has been suggested that the AAAH enzymes each contain a conserved C-terminal catalytic (C) domain and an unrelated N-terminal regulatory (R) domain. It is possible that the R protein domains arose from genes that were recruited from different sources to combine with the common gene for the catalytic core. Thus, by combining with the same C domain, the proteins acquired the unique regulatory properties of the separate R domains.


    References

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biopterin dependent aromatic amino acid hydroxylases
Biopterin dependent aromatic amino acid hydroxylase - Alchetron, the ...

Biopterin dependent aromatic amino acid hydroxylase - Alchetron, the ...

Biopterin

Biopterin

Phylogeny and reconciliation for aromatic amino acid hydroxylases ...

Phylogeny and reconciliation for aromatic amino acid hydroxylases ...

Alignment of aromatic amino acid hydroxylases. Aromatic amino acid ...

Alignment of aromatic amino acid hydroxylases. Aromatic amino acid ...

Biopterin Biosynthesis

Biopterin Biosynthesis

Biopterin

Biopterin

Biopterin1 - MTHFR Gene health™

Biopterin1 - MTHFR Gene health™

Figure 1 from Structure and function of the aromatic amino acid ...

Figure 1 from Structure and function of the aromatic amino acid ...

Figure 3 from Structure and function of the aromatic amino acid ...

Figure 3 from Structure and function of the aromatic amino acid ...

APExBIO - L-Biopterin | cofactor in the production of many ...

APExBIO - L-Biopterin | cofactor in the production of many ...

The Role of Tetrahydrobiopterin in Aromatic Amino Acid Hydroxylases ...

The Role of Tetrahydrobiopterin in Aromatic Amino Acid Hydroxylases ...

The Biopterin Cycle - Lifecode Gx Support

The Biopterin Cycle - Lifecode Gx Support