EC Number |
Cofactor |
Reference |
---|
1.1.1.375 | NAD(P)H |
the cofactor is bound at the active site |
728123 |
1.1.1.375 | NAD+ |
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases |
728123 |
1.1.1.375 | NAD+ |
the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate |
389520 |
1.1.1.375 | NADH |
NADPH is the preferred coenzyme |
728317 |
1.1.1.375 | NADH |
preference of NADP(H) over NAD(H).. The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases |
728123 |
1.1.1.375 | NADH |
preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site |
728123 |
1.1.1.375 | NADH |
the enzyme prefers NADPH over NADH in reduction of oxaloacetate |
389520 |
1.1.1.375 | NADP+ |
preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases |
728123 |
1.1.1.375 | NADP+ |
the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate |
389520 |
1.1.1.375 | NADPH |
NADPH is the preferred coenzyme |
728317 |