EC Number   |
Reference  |
|---|
    2.7.7.23 | recombinant enzyme, hanging drop vapor diffusion method |
643073 |
| 2.7.7.23 | - |
643075, 643076 |
| 2.7.7.23 | sitting-drop vapour-diffusion method |
671097 |
| 2.7.7.23 | hanging drop vapour diffusion method |
674815 |
| 2.7.7.23 | hanging drop vapour diffusion method, using 20% PEG 3350, 0.15 M DL-malate pH 7.0 |
690292 |
| 2.7.7.23 | a 1.9 A resolution crystal structure of a synthetic small-molecule inhibitor (4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide) of GlmU is presented. The determined crystal structure indicate that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction |
706622 |
| 2.7.7.23 | homology modeling of structure based on Haemophilus influenzae enzyme, PDB entry 2V0K |
719411 |
| 2.7.7.23 | GlmUMtb in complex with substrates/products bound at the acetyltransferase active site, sitting drop vapor diffusion method, mixing of 400 nl of 15 mg/ml protein, 5 mM acetyl-CoA, 5 mM MgCl2, 5 mM UDP-GlcNAc with 400 nl of 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, 4-8 days, for enzyme complex with CoA and N-acetylglucosamine-1-phosphate, acetyl-Coa-containing crystals are soaked in 5 mM GlcN-1-P, 5 mM MgCl2, 5 mM UDP-GlcNAc, 5 mM acetyl-CoA, 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, or by co-crystallizing the enzyme with 5 mM GlcNAc-1-P, 5 mM MgCl2, 5 mM UDPGlcNAc, and 5 mM CoA under the conditions mentioned for obtaining GlmUMtb(AcCoA) crystals, X-ray diffraction structure determination and analysis at 1.98-2.33 A resolution |
720042 |
| 2.7.7.23 | generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1 |
721526 |
| 2.7.7.23 | structure-based drug design studies. The molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues |
722022 |
