Literature summary for 1.14.16.4 extracted from

Windahl, M.S.; Petersen, C.R.; Christensen, H.E.; Harris, P.
Crystal structure of tryptophan hydroxylase with bound amino acid substrate (2008), Biochemistry, 47, 12087-12094.

Search for more literature for 1.14.16.4

Cloned(Commentary)

Cloned (Comment)	Organism
catalytic domain (DETLA1-100/DELTA415-445) of TPH1, expression in Escherichia coli	Gallus gallus

Crystallization (Commentary)

Crystallization (Comment)	Organism
catalytic domain (DETLA1-100/DELTA415-445) of TPH1 in complex with the tryptophan substrate and an iron-bound imidazole, by vapor diffusion method with sitting drops, at 1.9 A resolution, crystallization time of 3-6 months. Loops of residues Leu124-Asp139 and Ile367-Thr369 close around the active site. The tryptophan substrate is bound close to the iron in a binding pocket distinct from the BH4 binding pocket. The hydrophobic part of the tryptophan binding pocket is lined by residues Tyr236, Thr266, Pro269, His273, Phe314, Phe319, and Ile367, while the polar interactions of the tryptophan are with Thr266, Ile367, and Ser337 and a salt bridge to Arg258. The overall structure is more compact with two loops closing around the active site, when compared to the structure of human catalytic domain of TPH1	Gallus gallus

Crystallization (Comment)

Organism

catalytic domain (DETLA1-100/DELTA415-445) of TPH1 in complex with the tryptophan substrate and an iron-bound imidazole, by vapor diffusion method with sitting drops, at 1.9 A resolution, crystallization time of 3-6 months. Loops of residues Leu124-Asp139 and Ile367-Thr369 close around the active site. The tryptophan substrate is bound close to the iron in a binding pocket distinct from the BH4 binding pocket. The hydrophobic part of the tryptophan binding pocket is lined by residues Tyr236, Thr266, Pro269, His273, Phe314, Phe319, and Ile367, while the polar interactions of the tryptophan are with Thr266, Ile367, and Ser337 and a salt bridge to Arg258. The overall structure is more compact with two loops closing around the active site, when compared to the structure of human catalytic domain of TPH1

Gallus gallus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	the iron coordination is a distorted trigonal bipyramidal coordination with His273, His278, and Glu318 (partially bidentate) and one imidazole as ligands. The tryptophan stacks against Pro269 with a distance of 3.9 A between the iron and the tryptophan Czeta3 atom that is hydroxylated	Gallus gallus

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	P70080	-	-

Purification (Commentary)

Purification (Comment)	Organism
catalytic domain (DETLA1-100/DELTA415-445) of TPH1	Gallus gallus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-tryptophan + tetrahydrobiopterin + O2	-	Gallus gallus	5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin	-	?

Synonyms

Synonyms	Comment	Organism
TPH1	-	Gallus gallus
tryptophan hydroxylase	-	Gallus gallus

Cofactor

Cofactor	Comment	Organism	Structure
tetrahydrobiopterin	-	Gallus gallus