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Literature summary for extracted from

  • Sanli, G.; Banta, S.; Anderson, S.; Blaber, M.
    Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase (2004), Protein Sci., 13, 504-512.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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 22Ā°C Corynebacterium sp.

Protein Variants

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 and Products (Substrate)

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.