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Literature summary for extracted from

  • Khurana, S.; Sanli, G.; Powers, D.B.; Anderson, S.; Blaber, M.
    Molecular modeling of substrate binding in wild-type and mutant Corynebacteria 2,5-diketo-D-gluconate reductases (2000), Proteins, 39, 68-75.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F22Y the mutation causes a 2.5fold decrease in Km for 2,5-didehydro-D-gluconate whereas the value of kcat remains essentially unchanged Corynebacterium sp.
Q192R the mutation primarily affects the kcat parameter toward the 2,5-didehydro-D-gluconate substrate, increasing its value approximately 2.5fold, whereas Km is relatively unaffected, or increases slightly Corynebacterium sp.


Organism UniProt Comment Textmining
Corynebacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,5-didehydro-D-gluconate + NADPH + H+ isoform DKGR B exhibits 66fold higher specific activity toward 2,5-didehydro-D-gluconate than isoform DKGR A Corynebacterium sp. 2-dehydro-L-gulonate + NADP+


Synonyms Comment Organism
2,5-diketo-D-gluconate reductase
Corynebacterium sp.
2,5-DKGR A isoform Corynebacterium sp.
2,5-DKGR B isoform Corynebacterium sp.


Cofactor Comment Organism Structure
NADPH dependent on Corynebacterium sp.