EC Number   |
Cofactor |
Reference |
|---|
    1.2.1.10 | acetyl-CoA |
- |
763253, 763497 |
| 1.2.1.10 | CoA |
- |
286052, 286197, 390162, 390163, 390164, 390166, 390167, 390168, 390170, 390171, 390173, 390174, 390175, 390176, 390177, 390178, 390179, 763253, 763497 |
| 1.2.1.10 | CoA |
shares a binding site with NAD+. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis |
690971 |
| 1.2.1.10 | more |
enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine |
390176 |
| 1.2.1.10 | more |
the purified ADHES77 preferred to use NAD+ as an electron acceptor as compared to NADP+. In the specific activities of acetaldehyde dehydrogenase, the catalytic efficiencies for NAD+ i about 15.7 greater than for NADP+. Similarly, in the catalytic reductions of acetyl-CoA, the ADHES77 preferentially utilizes NADH as an electron donor, exhibiting approximately 5.6fold higher activity than for NADPH. The results suggest that the ADHES77 prefers to use NAD(H) as redox partners as compared to NADP(H) |
742936 |
| 1.2.1.10 | NAD+ |
- |
286052, 390162, 390163, 390164, 390168, 390170, 390171, 390173, 390174, 390175, 390176, 657161, 695594, 724341, 724721, 735506, 763253, 763497 |
| 1.2.1.10 | NAD+ |
57fold preferred over NADP+ |
738721 |
| 1.2.1.10 | NAD+ |
NAD+-specific |
390177 |
| 1.2.1.10 | NAD+ |
NADH-dependent |
286197 |
| 1.2.1.10 | NAD+ |
no reaction with NADP+ |
390166, 390167, 390177 |
