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1.14.16.4: tryptophan 5-monooxygenase

This is an abbreviated version!
For detailed information about tryptophan 5-monooxygenase, go to the full flat file.

Word Map on EC 1.14.16.4

Reaction

L-tryptophan
+
a 5,6,7,8-tetrahydropteridine
+
O2
=
5-hydroxy-L-tryptophan
+
a 4a-hydroxy-5,6,7,8-tetrahydropteridine

Synonyms

hTPH2, indoleacetic acid-5-hydroxylase, L-tryptophan 5-hydroxylase, L-tryptophan hydroxylase, oxygenase, tryptophan 5-mono-, peripheral tryptophan hydroxylase, PTMO, putative tryptophan monooxygenase, TH2, TPH, TPH-1, TPH-2, TPH1, TPH2, TRpOH, tryptophan 5-hydroxylase, tryptophan 5-monooxygenase, tryptophan hydroxylase, tryptophan hydroxylase 1, tryptophan hydroxylase 2, tryptophan hydroxylase I, tryptophan hydroxylase isoform 1, tryptophan hydroxylase isoform 2, tryptophan hydroxylase isoform2, tryptophan hydroxylase type I, tryptophan hydroxylase-1, tryptophan hydroxylase-2, tryptophan-5-hydroxylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.16.4 tryptophan 5-monooxygenase

Crystallization

Crystallization on EC 1.14.16.4 - tryptophan 5-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
purified enzyme without 7,8-dihydro-L-biopterin, sitting drop vapour diffusion method, 0.002 ml of 4.2 mg/ml protein in 20 mM Tris/NaOH, 100 mM (NH4)2SO4 pH 8.5, is mixed with 0.002 ml of reservoir solution containing 0.2 M imidazole malate, pH 8.5, 22.5% PEG 10000, and tetrahydrobiopterin in excess, X-ray diffraction structure determination and analysis at 3.0 A reslution
compound 4-(4-amino-6-[[(1R)-1-naphthalen-2-ylethyl]amino]-1,3,5-triazin-2-yl)-L-phenylalanine co-crystallized with TPH1
modeled structure based on the known crystal structures of phenylalanine hydroxylase and tyrosine hydroxylase
-
sitting drop vapor diffusion method, X-ray crystal structure of a truncated functional form of enzyme (DELTANH102-DELTACOOH402) with the bound cofactor analogue 7,8-dihydro-L-biopterin
residue Phe241 forms a displaced sandwich-type pi-complex with tetrahydrobiopterin, this complex has a counterpoise-corrected second order Moller Plesset Theory interaction energy of about 24.68 kcal/mol
-