EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.27 | NADH |
NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH did not change with pH |
686679 |
| 1.1.1.27 | NADH |
the coenzyme is in an open conformation and the adenine ribose ring of it is surrounded by Asp 38, Val 39, and Gly 99. Asp 38 and Gly 99 give some specificity to the adenine orientation, Asp 38 is an important residue in stabilizing NADH binding, overview |
684519 |
| 1.1.1.27 | NADH |
the NADH-cofactor binding site of heart LDH is involved in the interaction of the isozyme with liposomes made of acidic phospholipids, overview |
686014 |
| 1.1.1.27 | NADP+ |
- |
684561, 685322 |
| 1.1.1.27 | NADP+ |
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+ |
670748 |
| 1.1.1.27 | NADPH |
- |
684561, 685322 |
| 1.1.1.27 | NADPH |
coenzyme |
286441, 286448, 286468 |
| 1.1.1.27 | NADPH |
NADH is 10fold preferred over NADPH |
762306 |
| 1.1.1.27 | nicotinamide hypoxanthine dinucleotide |
alternative coenzyme |
286471 |
| 1.1.1.27 | thio-NAD+ |
alternative coenzyme |
286471 |
