EC Number   |
Protein Variants |
Reference |
|---|
    1.2.1.59 | C150S |
the mutant is unable to turn over D-glyceraldehyde 3-phosphate in the presence of either NAD+ or NADP+ |
-, 723857 |
| 1.2.1.59 | D35G |
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+ |
-, 743222 |
| 1.2.1.59 | D35G/L36R/P192S |
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency |
-, 743222 |
| 1.2.1.59 | D35G/L36T/T37K |
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme |
-, 743222 |
| 1.2.1.59 | D35G/L36T/T37K/P192S |
site-directed mutagenesis, the mutant shows high catalytic efficiency with NADP+ while the catalytic efficiency with NAD+ also increases. The replacement of Pro192 to Ser benefits the binding affinity of both NAD+ and NADP+ |
743222 |
| 1.2.1.59 | L36T |
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+ |
-, 743222 |
| 1.2.1.59 | more |
the coenzyme specificity of GAPDH, EC 1.2.1.12, of Corynebacterium glutamicum is systematically manipulated by rational protein design and the effect of the manipulation for cellular metabolism and lysine production is evaluated. By a combinatorial modification of four key residues within the coenzyme binding sites, different GAPDH mutants with varied coenzyme specificity are constructed. While increasing the catalytic efficiency of GAPDH towards NADP+ enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (about 60%) is achieved with the mutant showing similar preference towards both NAD+ and NADP+, EC 1.2.1.59 |
-, 743222 |
