EC Number   |
|---|
    2.6.1.7 | - |
| 2.6.1.7 | 5-pyridoxal phosphate and pyridoxamine form and in complex with competing substrate L-phenylalanine |
| 2.6.1.7 | Comparison of the active site residues of the Aedes aegypti enzyme-cysteine structure with those of the human isoform KAT I-phenylalanine structure reveals that Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes aegypti enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does |
| 2.6.1.7 | diffraction to 2.0 A resolution, comparison with crystallization data from Aspergillus fumigatus, Dictyostelium discoideum, Aedes aegypti, Trypanosoma brucei, Rattus norvegicus, and Homo sapiens |
| 2.6.1.7 | full-length pyridoxal phosphate-form, to 1.83 A resolution. The electron density of the active site reveals an aldimine linkage between pyridoxal phosphate and Lys263 |
| 2.6.1.7 | hanging-drop vapor diffusion method, PEG 4000, |
| 2.6.1.7 | in complex with 3-indolepropionic acid or DL-indole-3-lactic acid, hanging drop vapor diffusion method, using 22% (w/v) PEG 4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5 |
| 2.6.1.7 | in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5'-phosphate in the structures. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form. Tyr286 in the Aedes aegypti enzyme is changed to Phe278 in the human enzyme, which may explain why the Aedes enzyme transaminates hydrophilic amino acids more efficiently than the human enzyme does |
| 2.6.1.7 | in complex with L-kynurenine and L-glutamine, hanging drop vapor diffusion method, using 21% (w/v) polyethylene glycol 400, 10% glycerol, 150 mM CaCl2, and 100 mM HEPES, pH 7.5 |
| 2.6.1.7 | in complex with pyridoxal 5'-phosphate and aminooxyacetate, hanging drop vapor diffusion method, using 200 mM sodium acetate, 29% (w/v) PEG4000 in 100 mM Tris, pH 7.3 |
