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Literature summary for 1.1.1.346 extracted from

  • Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.
    Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis (2002), Biochemistry, 41, 6226-6236.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F22Y/A272G substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme Corynebacterium sp.
F22Y/K232G/R235G/R238H/A272G mutant with wild type kcat value for NADPH Corynebacterium sp.
F22Y/K232G/R235T/R238H/A272G 420 mutant with decreased kcat value for NADPH compared to the wild type enzyme Corynebacterium sp.
F22Y/K232G/R238H/A272G mutant with decreased kcat value for NADPH compared to the wild type enzyme Corynebacterium sp.
F22Y/K232G/R238H/A272G the mutant exhibits activity with NADH that is more than 2 orders of magnitude higher than that of the wild type enzyme and retains a high level of activity with NADPH Corynebacterium sp.
K232G/R238H mutant with decreased kcat value for NADPH compared to the wild type enzyme Corynebacterium sp.

Organism

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+
-
Corynebacterium sp. 2-dehydro-L-gulonate + NADP+
-
?

Synonyms

Synonyms Comment Organism
2,5-diketo-D-gluconic acid reductase
-
Corynebacterium sp.
2,5-DKG reductase
-
Corynebacterium sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2
-
NADPH mutant enzyme F22Y/S233T/R235S/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.
3.3
-
NADPH mutant enzyme F22Y/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.
7
-
NADPH mutant enzyme F22Y/K232G/R235G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.
7.3
-
NADPH mutant enzyme K232G/R238H, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.
18.3
-
NADPH mutant enzyme F22Y/K232G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.
18.3
-
NADPH wild type enzyme, in 100 mM Bis-Tris, pH 7.0, at 25°C Corynebacterium sp.

Cofactor

Cofactor Comment Organism Structure
NADPH the enzyme has a preference for NADPH over NADH Corynebacterium sp.