EC Number   |
|---|
    6.3.4.4 | - |
| 6.3.4.4 | analysis of high-resolution vibrational spectral fingerprints of each substrate and intermediate. The bound IMP is distorted toward its N1-deprotonated form even in the absence of any other ligands. Specific interactions between GTP and active-site amino acid residues result in large Raman shifts and contribute substantially to intrinsic binding energy. When both IMP and GTP are simultaneously bound, IMP is converted into an intermediate 6-phosphoryl inosine 5'-monophosphate. The intermediate complex is stable upon binding of the third ligand, L-aspartae analogue hadaicin. In the absence of hadaicin, 6-phosphoryl inosine 5'-monophosphate is quickly released from ADSS, is unstable in solution, and converts back into IMP. Hadaicin allosterically stabilizes ADSS through local conformational rearrangements |
| 6.3.4.4 | crystal structure of guanine nucleotide complexes of adenylosuccinate synthetase |
| 6.3.4.4 | crystal structure of the enzyme complexed with GDP, IMP hadacidin, NO3-, and Mg2+ |
| 6.3.4.4 | crystal structure of unligated enzyme |
| 6.3.4.4 | crystals grown by the method of hanging drops |
| 6.3.4.4 | crystals grown by the method of hanging drops, space group P4(#)2(1)2, a = b = 69.93, c = 198.49 |
| 6.3.4.4 | crystals grown by the method of hanging drops, space group P4(3)2(1)2, unit cell parameters a = b = 70.24 A, c = 199.14 A |
| 6.3.4.4 | entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli |
| 6.3.4.4 | enzyme-hydantocidin complex at 2.6 A resolution |
