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Literature summary for 1.1.1.274 extracted from

  • Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.
    Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A (2002), Protein Eng., 15, 131-140.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expresssion of several isoenzyme A mutants in Escherichia coli Corynebacterium sp.

Protein Variants

Protein Variants Comment Organism
K232 isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
K232Q isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
K232S isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
R235G isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
R235T isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
R238E isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
R238H isoenzyme A, designed to improve the ability to use NADH as cofactor, 7fold higher activity with NADH than wild-type Corynebacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
NADH isoenzyme A, K232G mutant Corynebacterium sp.
2.1
-
NADH isoenzyme A, R238H mutant Corynebacterium sp.
2.6
-
NADH isoenzyme A, wild-type Corynebacterium sp.
2.8
-
NADH isoenzyme A, K232S mutant Corynebacterium sp.
3.9
-
NADH isoenzyme A, K232M mutant Corynebacterium sp.
3.9
-
NADH isoenzyme A, K232Q mutant Corynebacterium sp.
8.4
-
NADH isoenzyme A, R235G mutant Corynebacterium sp.
8.4
-
NADH isoenzyme A, R238E mutant Corynebacterium sp.
8.8
-
NADH isoenzyme A, R235T mutant Corynebacterium sp.

Organism

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 + NADH
-
Corynebacterium sp. 2-keto-L-gulonate + NAD+
-
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