Crystallization (Comment) | Organism |
---|---|
mutant enzyme F22Y/K232G/R238H/A272G in complex with NADH, hanging drop vapor diffusion method, using 1.5 M lithium sulfate and 0.1 M Na HEPES (pH 7.5), at 22°C | Corynebacterium sp. |
Protein Variants | Comment | Organism |
---|---|---|
F22Y/K232G/R238H/A272G | the mutation enhances binding to NADH, while retaining to a large extent the ability to bind NADPH. The mutant is also more stable and can, therefore, be expected to exhibit greater effective activity at elevated temperatures in comparison to the wild type enzyme | Corynebacterium sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium sp. | P06632 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,5-didehydro-D-gluconate + NADPH + H+ | - |
Corynebacterium sp. | 2-dehydro-L-gulonate + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2,5-diketo-D-gluconic acid reductase A | isoform | Corynebacterium sp. |
2,5-DKGRA | isoform | Corynebacterium sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | the enzyme exhibits a preference for NADPH compared to NADH | Corynebacterium sp. |