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2.6.1.1: aspartate transaminase

This is an abbreviated version!
For detailed information about aspartate transaminase, go to the full flat file.

Word Map on EC 2.6.1.1

Reaction

L-aspartate
+
2-oxoglutarate
=
oxaloacetate
 +
L-glutamate

Synonyms

2-oxoglutarate-glutamate aminotransferase, AAT, AAT-2, AAT-3, AAT3, aatA, AATase, aatB3, all2340, alr1039, alr2765, alr4853, aminotransferase, aspartate, aoa/coa, AsAT, Asp AT, aspartate alpha-ketoglutarate transaminase, aspartate aminotransferase, aspartate aminotransferase 1, aspartate aminotransferase A, aspartate AT, aspartate transaminase, aspartate, 2-oxoglutarate aminotransferase, aspartate-2-oxoglutarate transaminase, aspartate/(R)-cysteate:2-oxoglutarate aminotransferase, aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase, aspartate:2-oxoglutarate amino-transferase, aspartate:2-oxoglutarate aminotransferase, aspartic acid aminotransferase, aspartic aminotransferase, aspartyl aminotransferase, AspAT, AspATSs, aspB, aspC, AspT, AST, AST-Bb, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, C-S lyase, CAA1, cAST, Cgl0240, class Ibeta AAT, EcAspAT, GL50803_91056, glutamate oxaloacetate transaminase, glutamate oxaloacetate transaminase 1, glutamate-oxalacetate aminotransferase, glutamate-oxalate transaminase, glutamate-oxaloacetate transaminase 1, glutamic oxalic transaminase, glutamic oxaloacetic transaminase, glutamic-aspartic aminotransferase, glutamic-aspartic transaminase, glutamic-oxalacetic transaminase, glutamic-oxaloacetic transaminase, GOT, GOT (enzyme), GOT1, GOT1L1, GOT2, KAT IV, L-aspartate aminotransferase, L-aspartate transaminase, L-aspartate-2-ketoglutarate aminotransferase, L-aspartate-2-oxoglutarate aminotransferase, L-aspartate-2-oxoglutarate-transaminase, L-aspartate-alpha-ketoglutarate transaminase, L-aspartate:2-oxoglutarate aminotransferase, L-aspartateartate aminotransferase, L-aspartic aminotransferase, L-AspAT, mitAAT, More, oxaloacetate transferase, oxaloacetate-aspartate aminotransferase, Pat, PfAspAT, plastid aspartate aminotransferase, prephenate aminotransferase, protein TT0402, PT-AAT, Rv3722c, Sar2028, SsAspAT, Tb11.02.2740, transaminase A

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.1 aspartate transaminase

Crystallization

Crystallization on EC 2.6.1.1 - aspartate transaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtPAT wild-type enzyme and K306A, T84V, and T84V/K169V mutant enzymes in complex with either 2-oxoglutarate or pyridoxamine 5'-phosphate and glutamate, X-ray diffraction structure determination and analysis at 1.4-3.0 A resolution, molecular replacement
vapour diffusion method, 10 mM NaOH-glycine, pH 9.1, polyethylene glycol 4000 18% w/v, 1 week, X-ray analysis
-
in complex with pyridoxal phosphate and a citrate molecule, to 2.0 A resolution
crystallization of V39F AspAT is performed by the hanging drop vapor diffusion method
crystals are grown at 19°C by the hanging-drop technique, unliganded and hydrocinnamate complex of V39L/K41Y/T47I/N69L/T109S/A293D/N297S, hydrocinnamate complex and maleate complexes of A12T/P13T/N34D/T109S/G261A/S285G/N297S and the hydrocinnamate complex of A12T/P13T/N34D/T109S/G261A/S285G/A293D/N297S
hanging drop vapour diffusion, crystals of mutants P195A and P138A/P195A in complex with maleate, protein solution: 20 mg/ml, 10 mM potassium phosphate, 0.01 mM pyridoxal 5'-phosphate, 2 mM EDTA, 0.5 mM DTT, reservoir solution: 1.9-2.1 M ammonium sulfate, 0.2 M 2-methylmorpholine, 2% polyethylene glycol 400, mutant P138A/P195A is also crystallized in complex with maleate, 20 mM, X-ray diffraction structure analysis
purified mutant K258A, batch method, protein solution: 5.2 mg/ml, 50 mM potassium phosphate, pH 7.5, 53% ammonium sulfate, room temperature, 1 week, preparation of crystals with heavy atom derivatives by soaking crystals for 24 or 48 h, structure analysis
-
purified mutant V39L, hanging drop method, room temperature, protein solution: 12.5 mg/ml, 20 mM sodium phosphate, pH 7.5, 30 mM maleate, 0.4 M sodium chloride, 12.5% w/v polyethylene glycol 4000, reservoir solution: 23-25% w/v polyethylene glycol 4000, 0.8 M sodium chloride, 20 mM sodium phosphate, pH 7.5, X-ray diffraction structure determination
-
sitting drop method, protein solution: 30 mg/ml, 10 mM potassium phosphate, pH 7.0, 0.01 mM pyridoxal 5'-phosphate, 1 mM EDTA, 2 mM succinate, 0.3 mM azide, reservoir solution: same composition as protein solution, contains no protein but polyethylene glycol 4000, 11-17% w/v, 20°C, stepwise addition of protein solution, X-ray diffraction analysis
-
the crystal triple mutant I33Q/Y214Q/R280Y is determined to relate the observed changes in reaction kinetics to the changes in active-site structure
the crystals of AspATs reconstituted with phosphopyridoxyl-L-Glu, phosphopyridoxyl-D-Glu, and phosphopyridoxal-2-methyl-L-glutamate are obtained by the hanging drop vapor diffusion method using ammonium sulfate as the precipitant. Crystals of suitable size for diffraction experiments are obtained within a week. The crystal structures of the complexes of aspartate aminotransferase with phosphopyridoxyl derivatives of L-glutamate, D-glutamate, and 2-methyl-L-glutamate are solved as the models for the external aldimine and ketimine complexes of L-glutamate. All the structures are in the closed form, and the two carboxylate groups and the arginine residues binding them are superimposable on the external aldimine complex with 2-methyl-L-aspartate
two nearly identical crystal structures of the complexes between (S)-4-amino-4,5-dihydro-2-furancarboxylic acid and L-AspAT obtained at pH 7.5 and 8 are shown. The inhibitor forms only one adduct with the enzyme, with active site lysine 246, thus irreversibly inactivating the L-AspAT transamination reaction
vapour diffusion technique, protein solution: 10 mg/ml, 10 mM potassium phosphate,pH 7.0, 2.5 mM pyridoxal 5'-phosphate, 2.5% polyethylene glycol w/v, 4°C, 7-10 days
-
purified cytosolic enzyme, variation of crystallization conditions resulting in different crystal types, influence of various divalent metal ions, dioxane and non-ionic detergent beta-octylglucoside, structure analysis
-
vapour diffusion method with hanging drops, protein solution: 10 mg/ml, 50 mM sodium phosphate, pH 7.5, 8-24% polyethylene glycol 2000-20000, reservoir solution: 8-24% polyethylene glycol 2000-20000, equal amounts, room temperature, X-ray structure analysis
-
in open an closed conformation. Pyridoxal phosphate is covalently bound to the active site lysine via a Schiff base
sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol 3350 5% (w/v) Cymal, and 0.1 M sodium acetate trihydrate (pH 4.5)
to 2.99 A resolution, space group P1, with unit-cell parameters a = 56.7, b = 76.1, c = 94.2 A, alpha =78.0, beta =85.6, gamma = 78.4°
in open an closed conformation. Pyridoxal phosphate is covalently bound to the active site lysine via a Schiff base
to 2.5 A resolution, space group P212121, with unit-cell parameters a = 93.27, b = 98.19, c = 198.70 A
concentrated isoenzyme AAT-1 solution, 10 mM Tris-HCl, pH 8.0, 1 mM 2-oxoglutarate, 2 mM KOH, 0.01 pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, polyethylene glycol 6000 8% w/v, 4°C, 6 days
-
concentrated isoenzyme AAT-2 solution, 10 mM potassium phosphate, pH 7.0, 1 mM 2-oxoglutarate, 2 mM KOH, 0.001 mM pyridoxal 5'-phosphate, 0.01% 2-mercaptoethanol, dialysis against distilled water at 4°C for 3 days
-
crystalized to a maximum resolution of 2.8 A
-
the X-ray structure of the PfAspAT homodimer at a resolution of 2.8 A is reported. While the overall fold is similar to the currently available structures of other AspATs, the structure presented shows a significant divergence in the conformation of the N-terminal residues
concentrated protein solution, potassium phosphate 0,01 M, pH 7.2, 0.01 mM pyridoxal 5'-phosphate, ammonium sulfate
-
hanging drop vapor diffusion method, using 20% (w/v) polyethyleneglycol 8000 and 0.1 M sodium HEPES (pH 8.5)
hanging drop vapour diffusion and sitting drop vapour diffusion using 23.6% (w/v) PEG 4000, 0.1 M HEPES pH 8.0
-
crystals of cytosolic enzyme, or enzyme in complex with substrates, N-methylpyridoxal, and inhibitors, depression-plate and sandwich-box techniques, protein solution: 35-40 mg/ml, pH 5.4, 40 mM sodium acetate, 4% polyethylene glycol 4000-6000, with or without substrate, cofactor or inhibitor compounds, reservoir solution: 40 mM sodium acetate, pH 5.4, 8% polyethylene glycol 4000-6000, crystals appear within 1 week, spectroscopic analysis
-
crystals of enzyme-inhibitor complex, sitting drop vapour diffusion method, 4°C, protein solution: 7 mg/ml, polyethylene glycol 4000 11% w/v, 50 mM potassium phosphate, pH 7.5, reservoir solution: polyethylene glycol 4000 22% w/v, 50 mM potassium phosphate, pH 7.5, X-ray structure analysis
-
forced dialysis lead to crystal formation or pure protein, 8.5 mg/ml, in solution for microdiffusion, 53% (NH4)2SO4 and pH 6.0-7.0, 4°C, 2 months
-
hanging drop vapor diffusion method, using 8% (w/v) polyethylene glycol 6000
vapour diffusion method with hanging drops, crystals from solution: 10 mg/ml protein, polyethylene glycol 4000 16-17% w/v, 10 mM sodium phosphate, pH 7.5, injection of seed crystal into the hanging drop of chicken mitochondrial aspartate aminotransferase
-
vapour diffusion method with hanging drops, crystals from solution: polyethylene glycol 4000 17% w/v, 10 mM glycine/NaOH, pH 9.1, microspectrophotometric equilibrium and kinetic analysis
-
native and selenomethionine-substituted TT0402 proteins are crystallized in hanging drops at 4°C
-
equilibrium diffusion in a sitting drop, ammonium sulfate solution
-
in open an closed conformation. Pyridoxal phosphate is covalently bound to Lys237 via a Schiff base. In mutant K237A, pyridoxal phosphate is clearly bound to the active site