Hydroxylase
From Proteopedia
(Difference between revisions)
(→This is a placeholder) |
|||
| Line 3: | Line 3: | ||
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>. | ||
| - | This is a placeholder text to help you get started in | ||
| - | placing a Jmol applet on your page. At any time, click | ||
| - | "Show Preview" at the bottom of this page to see how it goes. | ||
| - | |||
| - | Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | ||
| - | and display another structure. | ||
{{STRUCTURE_2pah | PDB=2pah | SCENE= }} | {{STRUCTURE_2pah | PDB=2pah | SCENE= }} | ||
Revision as of 09:17, 3 April 2009
The enzyme family of aromatic amino acid hydroxylases consist 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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Michael Skovbo Windahl, David Canner, Joel L. Sussman, Jaime Prilusky
