We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

TPH

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: ==Tryptophan hydroxylase== Tryptophan hydroxylase (TPH) (tryptophan 5-monooxygenase, EC 1.14.16.4) catalyses the reaction between tryptophan, 5,6,7,8-tetrahydrobiopterin (BH4) and O2 to gi...)
Line 1: Line 1:
==Tryptophan hydroxylase==
==Tryptophan hydroxylase==
Tryptophan hydroxylase (TPH) (tryptophan 5-monooxygenase, EC 1.14.16.4) catalyses the reaction between tryptophan, 5,6,7,8-tetrahydrobiopterin (BH4) and O2 to give 5-hydroxytryptophan and 4a-hydroxy-tetrahydrobiopterin (4a-hydroxy-BH4. This reaction is the first and rate limiting step in the biosynthesis of serotonin (See scheme).
Tryptophan hydroxylase (TPH) (tryptophan 5-monooxygenase, EC 1.14.16.4) catalyses the reaction between tryptophan, 5,6,7,8-tetrahydrobiopterin (BH4) and O2 to give 5-hydroxytryptophan and 4a-hydroxy-tetrahydrobiopterin (4a-hydroxy-BH4. This reaction is the first and rate limiting step in the biosynthesis of serotonin (See scheme).
 +
 +
Together with phenylalanine hydroxylase (EC 1.14.16.1) and tyrosine hydroxylase (EC 1.14.16.2), TPH form the small enzyme family of aromatic amino acid hydroxylases (AAAH) []. 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) [ , , , ].
 +
This is a placeholder text to help you get started in
This is a placeholder text to help you get started in

Revision as of 08:19, 3 April 2009

Tryptophan hydroxylase

Tryptophan hydroxylase (TPH) (tryptophan 5-monooxygenase, EC 1.14.16.4) catalyses the reaction between tryptophan, 5,6,7,8-tetrahydrobiopterin (BH4) and O2 to give 5-hydroxytryptophan and 4a-hydroxy-tetrahydrobiopterin (4a-hydroxy-BH4. This reaction is the first and rate limiting step in the biosynthesis of serotonin (See scheme).

Together with phenylalanine hydroxylase (EC 1.14.16.1) and tyrosine hydroxylase (EC 1.14.16.2), TPH form the small enzyme family of aromatic amino acid hydroxylases (AAAH) []. 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) [ , , , ].


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.


PDB ID 3cin

Drag the structure with the mouse to rotate
3cin, resolution 1.70Å ()
Ligands: , ,
Gene: TM1419, TM_1419 (Thermotoga maritima MSB8)
Activity: Inositol-3-phosphate synthase, with EC number 5.5.1.4
Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN
Coordinates: save as pdb, mmCIF, xml


Proteopedia Page Contributors and Editors (what is this?)

Michael Skovbo Windahl, OCA

Retrieved from "http://52.214.119.220/wiki/index.php/TPH"
Personal tools