Hydroxylase
From Proteopedia
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| - | The enzyme family of aromatic amino acid hydroxylases consists of '''phenylalanine hydroxylase''' (PAH), '''tyrosine hydroxylase''' (TH) and '''tryptophan hydroxylase''' ([[TPH]]). | + | The enzyme family of aromatic amino acid hydroxylases consists of '''[[phenylalanine hydroxylase]]''' (PAH), '''tyrosine hydroxylase''' (TH) and '''tryptophan hydroxylase''' ([[TPH]]). |
These enzymes all contain iron and use BH<sub>4</sub> as a co-substrate in the hydroxylation of their respective aromatic amino acids. Additionally all mammalian AAAH form homotetramers and each monomer consists of three domains. These domains are the N-terminal regulatory domain (100-150 residues), the catalytic domain (approximately 315 residues) and the C-terminal tetramerisation domain (approximately 30-40 residues)<ref>PMID: 10800597</ref>. | These enzymes all contain iron and use BH<sub>4</sub> as a co-substrate in the hydroxylation of their respective aromatic amino acids. Additionally all mammalian AAAH form homotetramers and each monomer consists of three domains. These domains are the N-terminal regulatory domain (100-150 residues), the catalytic domain (approximately 315 residues) and the C-terminal tetramerisation domain (approximately 30-40 residues)<ref>PMID: 10800597</ref>. | ||
Revision as of 09:40, 3 April 2009
The enzyme family of aromatic amino acid hydroxylases consists of phenylalanine hydroxylase (PAH), tyrosine hydroxylase (TH) and tryptophan hydroxylase (TPH).
These enzymes all contain iron and use BH4 as a co-substrate in the hydroxylation of their respective aromatic amino acids. Additionally all mammalian AAAH form homotetramers and each monomer consists of three domains. These domains are the N-terminal regulatory domain (100-150 residues), the catalytic domain (approximately 315 residues) and the C-terminal tetramerisation domain (approximately 30-40 residues)[1].
References
- ↑ Fitzpatrick PF. The aromatic amino acid hydroxylases. Adv Enzymol Relat Areas Mol Biol. 2000;74:235-94. PMID:10800597
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