EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.35 | more |
the enzyme prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H) |
739840 |
| 1.1.1.35 | NAD+ |
- |
2207, 2220, 286052, 286269, 286588, 286589, 286590, 286591, 286592, 286593, 286594, 286596, 286598, 286601, 286602, 286603, 286604, 286606, 286607, 286608, 286609, 286610, 286611, 286612, 2962, 33713, 657276, 673340, 684609, 685573, 687573, 722124, 726748, 739806, 739812, 739815, 739840, 740235, 740804, 741307 |
| 1.1.1.35 | NAD+ |
dependent on |
673530 |
| 1.1.1.35 | NAD+ |
mode of cofactor binding, overview. The NAD+-binding site is located at the G-x-G-x-x-G nucleotide-binding motif, comprising residues Gly8-Ala9-Gly10-Thr11-Met12-Gly13. The hydroxyl groups of a phosphate moiety are hydrogen-bonded with the main chain nitrogen atoms of Thr11 and Met12. The nicotinamide and the two ribose rings of NAD+ are stabilized through hydrogen bond interactions mediated by the conserved Asp31, Glu90, Lys95, Asn115, Ser117, and Asn141 residues. The adenine moiety of NAD+ is positioned at the hydrophobic pocket formed by hydrophobic residues such as Leu7, Ile32, Ala88, Ile89, Ile94, and Ile98. One exception is Arg30, which assists the binding of the adenine moiety of NAD+ through a hydrogen bond |
740854 |
| 1.1.1.35 | NAD+ |
no activity with NADP+ |
727751 |
| 1.1.1.35 | NAD+ |
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor |
712966 |
| 1.1.1.35 | NAD+ |
specific for |
716755 |
| 1.1.1.35 | NAD+ |
the NAD+ cofactor is bound to the N-terminal Rossmann fold, the NAD+-binding pocket is made up of 5 loops, enzyme binding structure analysis, overview |
739989 |
| 1.1.1.35 | NADH |
- |
657276, 739806, 739812, 739815, 739840, 739989, 740804, 740854, 741307, 760296, 761222, 761558 |
| 1.1.1.35 | NADH |
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA |
712966 |
