EC Number   |
|---|
    2.1.1.20 | - |
| 2.1.1.20 | crystallized by the sitting drop method in complex with (6S)-5-methyltetrahydrofolat monoglutamate |
| 2.1.1.20 | crystals are grown at 22°C by hanging drop vapor diffusion method, crystallized in two crystal forms, a monoclinic form and a tetragonal form, P2(1) and P4(1)2(1)2 |
| 2.1.1.20 | crystals are grown at 4°C by hanging drop vapor diffusion method |
| 2.1.1.20 | GNMT complexed with 5-methyltetrahydrofolate, by the sitting drop method at room temperature, two folate binding sites in the intersubunit areas of the tetramer, each folate binding site is formed primarily by two 1-7 N-terminal regions of one pair of subunits and two 205-218 regions of the other pair of subunits. Both the pteridine and p-aminobenzoyl rings are located in the hydrophobic cavities formed by Tyr5, Leu207, and Met215 residues of all subunits |
| 2.1.1.20 | hanging drop method of vapor diffusion, crystal structure of the enzyme complexed with S-adenosyl-L-methionine and acetate (a potent competitive inhibitor of Gly) and the R175K mutated enzyme complexed with S-adenosyl-L-methionine are determined at 2.8 A and 3.0 A resolution, respectively |
| 2.1.1.20 | including R175K mutant |
| 2.1.1.20 | native and recombinant protein, to 2.55 A resolution. The native rat liver GNMT contains an acetylated N-terminal valine and is inhibited much more efficiently compared to the recombinant protein. In the folate-GNMT complexes with the native enzyme, two folate molecules establish three and four hydrogen bonds with the protein. In the folate-recombinant GNMT complex only one hydrogen bond is established. This difference results in more effective inhibition by folate of the native liver GNMT activity compared to the recombinant enzyme |
| 2.1.1.20 | sitting-drop vapor diffusion method in complex with 5-methyltetrahydrofolate pentaglutamate, two molecules of inhibitor bound to a tetramer |
| 2.1.1.20 | wild type and H176N mutant enzyme as cocrystals with a citrate molecule bound in the active site |
