EC Number   |
Reference |
|---|
    4.1.2.55 | hanging drop diffusion method, three crystal forms: orthorhombic crystals of space group P2(1)2(1)2(1), which diffract to beyond 2.15 A, monoclinic crystals of space group C2, which diffract to 2.2 A, and cubic crystals of space group P4(2)32, which diffract to 3.4 A |
677304 |
| 4.1.2.55 | hanging-drop method, the enzyme crystallizes in two space groups, P3(1)21 and P6(5)22, for which diffraction data are obtained to a maximum resolution of 1.8 and 2.5 A |
718771 |
| 4.1.2.55 | in complex with 2-dehydro-3-deoxy-6-phospho-D-gluconate, vapor diffusion method |
747152 |
| 4.1.2.55 | trapping of Schiff base complexes with natural substrates pyruvate, 2-dehydro-3-deoxy-D-gluconate, 2-dehydro-3-deoxy-D-galactonate and pyruvate plus D-glyceraldehyde at physiological pH by rapid soaking at low temperature followed by flash freezing prior to X-ray data collection. The complexes explain the substrate promiscuity of the enzyme with a rigid ligand-binding site able to accommodate both 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate |
665573 |
| 4.1.2.55 | X-ray crystallographic analysis of the active site of the aldolase bound to pyruvate, 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at 4°C, reveals that its catalytic mechanism is typical of the N-acetylneuraminic acid lyase superfamily |
715259 |
