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1.14.16.1: phenylalanine 4-monooxygenase

This is an abbreviated version!
For detailed information about phenylalanine 4-monooxygenase, go to the full flat file.

Word Map on EC 1.14.16.1

Reaction

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

Synonyms

cePAH, DicPAH, EC 1.14.3.1, EC 1.99.1.2, HPAH, L-phenylalanine 4-hydroxylase, oxygenase, phenylalanine 4-mono-, P4H, PAH, PheH, phenylalaninase, phenylalanine 4-hydroxylase, phenylalanine hydroxylase, phenylalanine monooxygenase, PheOH, phhA

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
                1.14.16.1 phenylalanine 4-monooxygenase

Crystallization

Crystallization on EC 1.14.16.1 - phenylalanine 4-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
hanging drop vapor diffusion method, using 0.1 M Na-HEPES, pH 7.0, 0.01 M magnesium chloride hexahydrate, 0.005 M nickel(II) chloride hexahydrate, and 15% (w/v) PEG 3350, or sitting drop vapor diffusion method, using 0.1 M Na-HEPES pH 7.0, 0.01 M magnesium chloride hexahydrate, and 15% (w/v) PEG
vapor-diffusion hanging drop method at 4°C, reservoir solution contains 1 ml of 1.65-1.9 M ammonium sulfate, 40-100 mM NaCl and 20 mM HEPES pH 7.5, hanging drops are made using equal volumes of enzyme, 20 mg/ml, and reservoir solution, crystals grow in about one week, crystal structures of Fe-free apoenzyme, Fe3+-bound enzyme and Fe3+ plus 7,8-dihydro-L-biopterin-bound enzyme at 1.7 A, 2.0 A and 1.4 A resolution respectively
vapour diffusion, 1 mg enzyme dissolved in 0.1 ml 35% ammonium sulfate, 50 mM acetate, pH 6.0, 1 mM dithiothreitol, reservoir contains 60% ammonium sulfate, crystals appear after 3-4 d at 4°C
-
native enzyme by hanging drop method, 0.001 ml of protein solution containing 10 mg/ml protein in 20 mM Na-HEPES, 200 mM NaCl, pH 7.0, are mixed with 0.001 ml of reservoir solution containing 1.6-1.8 M ammonium sulfate, 100 mM NaCl, and 20 mM NaHepes, pH 7.5, equilibration at 4 °C, 3 weeks, cryoprotection with 25% glycerol, X-ray diffraction structure determination and analysis
-
apo DicPAH and DicPAH complexed with dihydrobiopterin (BH2) and FeIII are crystallized by the hanging-drop vapour-diffusion method. Crystals of apo DicPAH and the DicPAH-BH2-FeIII complex diffract to 2.6 and 2.07 A resolution, respectively, and belong to space group P21, with unit-cell parameters a = 70.02, b = 85.43, c = 74.86 A, beta= 110.12° and a = 70.97, b = 85.33, c = 74.89 A, beta = 110.23°, respectively
-
crystal structure of ternary complex of catalytic domain, Fe2+ form, with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine
crystal structure of the catalytic domain in its catalytic active Fe2+ form and as binary complex with tetrahydrobiopterin, 1.7 and 1.5 A resolution
-
in complex with 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin and substrate analogues 3-(2-thienyl)-L-alanine or L-norleucine
native and selenomethyl-labelled enzyme
-
sitting drop vapor diffusion method, using 0.1 M Bis-Tris-HCl pH 5.5, 25% (w/v) polyethylene glycol 3350, and 0.2 M magnesium chloride
vapor diffusion method, using 140 mM Na-acetate, 70 mM Na-citrate, 100 mM Na-cacodylate (pH 6.5), and 31.5% (w/v) PEG 1000