EC Number   |
Reference |
|---|
    1.4.1.9 | - |
349661, 349675 |
| 1.4.1.9 | cryo-electron microscopy structures of apo and NAD+-bound LDH at 3.0 and 3.2 A resolution, respectively. A partial conformational change is triggered by the interaction between Ser147 and the nicotinamide moiety of NAD+. NAD+ binding also enhances the strength of oligomerization interfaces formed by the core domains |
763402 |
| 1.4.1.9 | crystallized by addition of ammonium sulfate |
349665 |
| 1.4.1.9 | crystals of the binary complex with 4-methyl-2-oxopentanoate, hanging-drop vapour-diffusion method using PEG 4000 as precipitant |
349692 |
| 1.4.1.9 | hanging drop method of vapour diffusion, using ammonium sulfate as the precipitant |
349693 |
| 1.4.1.9 | homology modeling of structure and semirational engineering to increase the catalytic efficiency |
741659 |
| 1.4.1.9 | homology modeling of structure. Enzyme exhibits several cold-adapted features |
763413 |
| 1.4.1.9 | modeling of structure. Active site residues Lys81, Asp116, and Lys69 are catalytically important. Lys81 linkes the -OH group of the substrate 2-oxobutanoate by a 2.3-A long H-bond, and Asp116 is involved in proton transfer during catalysis |
741659 |
| 1.4.1.9 | structure of apo-protein and in complex with NAD+, to 3.0 and 3.2 A resolution, respectively. NAD+ binds to domain II (residues 137-331), and the NAD+-bound form has a disordered region (residues 142-144) in the loop between domains I and II |
763749 |
