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2.6.1.57: aromatic-amino-acid transaminase

This is an abbreviated version!
For detailed information about aromatic-amino-acid transaminase, go to the full flat file.

Word Map on EC 2.6.1.57

Reaction

an aromatic amino acid
+
2-oxoglutarate
=
an aromatic oxo acid
 +
L-glutamate

Synonyms

AAT, AAT I-III, AAT1, aminotransferase, aromatic amino acid, ArAT, ArAT-I, ArAT-ITL, ArATPf, ArATPh, Aro8, ARO9, AroAT, AroAT II, AroATEs, AroH, arom. amino acid transferase, arom.-amino-acid transaminase, aromatic amino acid aminotransferase, aromatic amino acid transaminase, aromatic amino transferase I, aromatic aminotransferase, aromatic aminotransferase AT-1, aromatic aminotransferase AT-2, aromatic aminotransferase II, aromatic L-amino acid transaminase, aromatic-amino-acid aminotransferase, aromatic-amino-acid:2-oxoglutarate transaminase, AT-1, AT-2, AT-IA, At1g80360, bifunctional 2-aminoadipate transaminase/aromatic-amino-acid:2-oxoglutarate transaminase, CaAro8p, CaAro9p, CaYer152Cp, eAroATEs, F5I6.11, hisC1, indole severe sensitive 1, ISS1, More, pdArAT, pdAroAT, PH1371, phhC, PjAT, SmAroAT, TyrB, TyrB-2, VAT1, Yer152, Yer152C

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.57 aromatic-amino-acid transaminase

Crystallization

Crystallization on EC 2.6.1.57 - aromatic-amino-acid transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of unliganded pdAroAT, pdAroAT in a complex with maleate and 3-phenylpropionate at 2.33 A, 2.5 A and 2.3 A resolution
tertiary structures of pdAroAT complexed with nine kind of inhibitors: 3-indolebutyric acid, 4-phenylbutyric acid, 5-phenylvaleric acid, 4-(2-thienyl)butyric acid, cyclohexanepropionic acid, 4-amminohydrocinnamic acid, 3-(p-tolyl)-propionic acid and 3-(3,4-dimethoxyphenyl)propionic acid, crystals of the maleate complex of pdAroAT are made by the micro-seeding method using 24% poly(ethylene)glycol 4000, 200 mM sodium maleate, pH 5.7 and 5 mM MgCl2 as precipitating buffer, cocrystallized inhibitor maleate is replaced by soaking the crystals in 24% poly(ethylene)glycol 4000, 100 mM sodium citrate, pH 5.7 containing 100 mM inhibitor for 10 h
hanging drop vapor diffusion, an equi-volume of 3 M 1,6-hexanediol solution at pH 7.5, 100 mM HEPES buffer, containing 10 mM MgCl2 is added to a protein solution containing 1.6% AeATPh and 0.02 mM pyridoxal 5'-phosphate, a droplet of the solution is equilibrated with 1 ml of 3 M 1,6-hexane-di-ol solution, crystals are grown at room temperature for 1 week, crystal structure of the native enzyme 2.1 a resolution, heavy atom derivatives diffract to 3.0 A resolution
-
hanging-drop vapor diffusion method at 20°C using 3 M 1,6-hexanediol, 100 mM HEPES (pH 7.5), and 10 mM MgCl2 as the precipitant solution. The crystal structure of the ligand-free enzyme is analyzed at a resolution of 1.8 A
ARO9 by hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 18.0 mg/ml protein in 25 mM Tris-HCl, pH 7.0, with 0.001 ml of reservoir solution containing 0.2 M potassium chloride, pH 7.0, and 20% w/v PEG 3550, and equilibration against 0.02 ml reservoir, X-ray diffraction structrue determination and analysis at 2.2 A resolution, molecular replacement method using the crystal structure of AroAT from Pyrococcus horikoshii strain OT3 (PDB ID 1dju) as initial search model, modeling
-