EC Number |
Reaction |
Reference |
---|
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
fully random mechanism |
1550 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
fully random terter mechanism |
1536 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
phosphate-binding region of adenylosuccinate synthetase is involved in a conformational change induced by GTP and IMP binding. GTP and IMP binding depend on the presence of the other substrate at the active site of the enzyme |
1556 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
random sequential binding mechanism |
1535 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
rapid equilibrium random AB steady-state ordered C kinetic mechanism |
-, 726945 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
sequential mechanism with a fully random order of substrate addition |
1544 |
6.3.4.4 | GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP |
sequential rapid equilibrium fully random mechanism |
1548 |