Hydroxylase
From Proteopedia
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{{STRUCTURE_2pah | PDB=2pah | SCENE= }} | {{STRUCTURE_2pah | PDB=2pah | SCENE= }} | ||
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| + | ==3D structures of Aromatic amino acid hydroxylases== | ||
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| + | [[Phenylalanine hydroxylase]] | ||
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| + | [[Tyrosine hydroxylase]] | ||
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| + | [[Tryptophan hydroxylase]] | ||
===Additional Resources=== | ===Additional Resources=== | ||
Revision as of 10:19, 9 May 2011
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].
3D structures of Aromatic amino acid hydroxylases
Additional Resources
For additional information, see: Amino Acid Synthesis & Metabolism
References
- ↑ Fitzpatrick PF. The aromatic amino acid hydroxylases. Adv Enzymol Relat Areas Mol Biol. 2000;74:235-94. PMID:10800597
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