EC Number   |
Cofactor |
Reference |
|---|
   1.1.1.67 | more |
no activity with NADPH/NADP+ |
763052 |
| 1.1.1.67 | more |
only trace activity for utilization of NADP+ |
722234 |
| 1.1.1.67 | more |
Thermotoga maritima MtDH is active with both NADH and NADPH cofactors. But the enzyme catalytic efficiency for D-fructose reduction with NADH is 2.5times higher than that with NADPH, possibly because of the Glu193, Lys194, Asp195, and Glu196 sequence motif |
763052 |
| 1.1.1.67 | NAD(P)+ |
its catalytic efficiency is 33times higher with NAD+ than with NADP+ |
695814 |
| 1.1.1.67 | NAD(P)H |
MtDH has a higher Vmax with NADPH than with NADH, whereas its catalytic efficiency is 2.2times higher with NADH than with NADPH. Cofactor specificity is due to the high density of negatively charged residues (Glu193, Asp195, and Glu196) downstream of the NAD(P) interaction site, the glycine motif |
695814 |
| 1.1.1.67 | NAD+ |
- |
285866, 287237, 287238, 287239, 287240, 287241, 287242, 287243, 287244, 287246, 287247, 287248, 287249, 287250, 287251, 287252, 287253, 287255, 287256, 287257, 287258, 654295, 654390, 655617, 667367, 668058, 686764, 712470, 722234, 740876, 740930, 741375, 763052, 763682, 94717, 94720 |
| 1.1.1.67 | NAD+ |
although MtDH has a higher Vmax with NADPH than with NADH, its catalytic efficiency is 33 times higher with NAD+ than with NADP+ |
695814 |
| 1.1.1.67 | NAD+ |
best initial reaction rates with 0.5 mM |
667367 |
| 1.1.1.67 | NAD+ |
binding structure, the carboxylate group of Asp69 forms a bifurcated hydrogen bond with the 2' and 3' hydroxyl groups of the adenosine of NAD+ and contributes to the 400fold preference of the enzyme for NAD+ as compared to NADP+, overview |
686764 |
| 1.1.1.67 | NAD+ |
dependent on, M2DH is a much poorer enzyme when it employes NADP+ and NADPH as compared to NAD+ and NADH |
697276 |
