EC Number |
Cofactor |
Reference |
---|
1.1.1.202 | more |
NADP+ has no coenzyme activity |
389488 |
1.1.1.202 | NAD+ |
- |
389488, 389490, 655107, 657320, 657406, 670216, 675901, 684171, 684524, 688171, 698602, 721395, 724566, 725951, 740214, 740216, 740927, 760717 |
1.1.1.202 | NADH |
- |
389488, 389490, 655107, 657406, 664422, 667270, 670216, 675901, 684171, 684524, 688171, 695842, 696785, 699149, 699357, 721395, 724566, 725951, 739886, 740214, 740216, 740927, 761555 |
1.1.1.202 | NADPH |
- |
695764, 695844 |
1.1.1.202 | NADH |
overexpression of PDOR leads to enhanced NADH and production ratio of NADH/NAD+ exceeds after the inducement of isopropyl-beta-D-thiogalactoside for the constructed strain |
697666 |
1.1.1.202 | NADH |
the electrostatic energy is the major force discriminating NADH from NADPH. Residue Asp41 is the key residue responsible for the coenzyme specificity |
712531 |
1.1.1.202 | NADPH |
no substrate for wild-type, but substrate for mutant D41G |
712531 |
1.1.1.202 | more |
no cofactor: NADPH |
721395 |
1.1.1.202 | NAD+ |
the enzyme contains a cofactor motif, the conserved sequence G-GG-S-X-X-D. The binding site for cofactor NAD(H) is located in the deep hydrophilic pocket between the PDOR two domains |
739886 |
1.1.1.202 | more |
PDOR requires NAD(H) as a cofactor, but the highly conserved NAD(H) binding fingerprint pattern G-X-G-X-X-G is not present in the amino acid sequence |
740927 |