EC Number   |
Cofactor |
Reference |
|---|
    1.2.1.24 | 3-acetylpyridine adenine dinucleotide |
- |
288158 |
| 1.2.1.24 | 3-acetylpyridine adenine dinucleotide |
reduced at nearly the same rate as NAD+ |
288170 |
| 1.2.1.24 | deamino-NAD+ |
reduced at nearly the same rate as NAD+ |
288170 |
| 1.2.1.24 | more |
human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding |
743762 |
| 1.2.1.24 | more |
no activity with NADP+ |
700082, 742640 |
| 1.2.1.24 | NAD+ |
- |
246674, 288042, 288149, 288150, 288151, 288152, 288153, 288154, 288155, 288156, 288157, 288158, 288159, 288160, 288161, 288163, 288164, 288165, 288166, 288167, 288168, 288169, 288170, 288171, 288172, 288173, 288174, 654852, 655493, 656587, 656808, 657160, 690435, 692615, 692620, 692836, 696968, 697282, 698174, 699375, 700082, 700887, 710394, 710898, 741570, 743762, 763330, 763340, 763472 |
| 1.2.1.24 | NAD+ |
absolutely specific for |
742640 |
| 1.2.1.24 | NAD+ |
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive |
700082 |
| 1.2.1.24 | NAD+ |
no activity in presence of NADP+ |
722211 |
| 1.2.1.24 | NAD+ |
required |
689379 |
