_EC 1.14.16.4 Tryptophan 5-monooxygenase. 6 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,609 PDB entries]
EC 1.14.-.- Acting on paired donors, with incorporation or reduction of molecu [1,433 PDB entries]
EC 1.14.16.- With reduced pteridine as one donor, and incorporation of one ato [41 PDB entries]
EC 1.14.16.4 Tryptophan 5-monooxygenase. [6 PDB entries]    
1in9

Pathway: Biopterin Biosynthesis
Reaction: L-tryptophan + tetrahydrobiopterin + O(2) = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
 


L-tryptophan
+
tetrahydrobiopterin
+
O(2)
=
5-hydroxy-L-tryptophan
+
4a-hydroxytetrahydrobiopterin
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Indoleacetic acid-5-hydroxylase. L-tryptophan hydroxylase. Tryptophan 5-hydroxylase. Tryptophan hydroxylase.
Cofactor(s): Iron.
Comments: Activated by phosphorylation, catalyzed by a Ca(2+)-activated protein kinase. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7- dihydrobiopterin, both spontaneously and by the action of Ec 4.2.1.96. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by Ec 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 6 PDB entries in enzyme class E.C.1.14.16.4

  PDB code Protein
1in9
Homology-based theoretical molecular model of human tryptophan hydroxylase regulatory, catalytic and tetramerization domains
Source: Homo sapiens. Human
Chain: A (443 residues)
1mlw
Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-l-biopterin cofactor and fe(iii)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: tph. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (290 residues) CATH domain: 1.10.800.10
Bound ligand:   Het Group HBI corresponds to enzyme reactant Tetrahydrobiopterin
3e2t
The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan
Source: Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Strain: white leghorn. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (307 residues) CATH domain: 1.10.800.10
Bound ligand:   Het Group TRP corresponds to enzyme reactant L-tryptophan
3hf6
Crystal structure of human tryptophan hydroxylase type 1 with bound lp-521834 and fe
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (280 residues) CATH domain: 1.10.800.10
3hf8
Crystal structure of human tryoptophan hydroxylase type 1 wi lp-533401 and fe
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (274 residues) CATH domain: 1.10.800.10
3hfb
Crystal structure of human tryoptophan hydroxylase type 1 wi 534193
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (274 residues) CATH domain: 1.10.800.10