EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.37 | 3-acetylpyridine adenine dinucleotide |
about 30% of the activity with NADH |
722201 |
| 1.1.1.37 | 3-acetylpyridine-adenine dinucleotide |
- |
700146 |
| 1.1.1.37 | more |
can also use 3-acetylpyridine-adenine and nicotinamide guanine as cofactors but with less specificity than NAD+ |
700562 |
| 1.1.1.37 | more |
cannot use NADP+ and NADPH as cofactor |
655488 |
| 1.1.1.37 | more |
no activity with malate and NADP+ |
686623 |
| 1.1.1.37 | more |
no activity with NADP(H) |
689325 |
| 1.1.1.37 | more |
no activity with NADPH |
722201, 733816 |
| 1.1.1.37 | more |
no detectable activity with NADPH and NADP+ |
654907 |
| 1.1.1.37 | more |
no significant oxaloacetate (OAA) reduction is detected when NADPH was used as coenzyme at 70°C. the presence of an aspartic residue at position 54 of the alignment suggests that Ignicoccus islandicus MalDH would use NADH instead of NADPH, and the lack of NADPH recognition confirmes it. In contrast, those characterized as NADPH-dependent MalDHs have a glycine residue at this position. This is because the smaller size of glycine allows accommodating the additional phosphate of NADPH |
761765 |
| 1.1.1.37 | more |
the recombinant SaMDH may also use NADPH as a cofactor although it is a highly NAD(H)-specific enzyme, no activity with malate and NADP+ as substrates |
723141 |
