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Literature summary for 1.1.1.346 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

Organism UniProt Comment Textmining
Corynebacterium sp.
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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+
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Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NADPH dependent on Corynebacterium sp.