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Literature summary for 1.1.1.346 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
mutant enzymes are expressed in Escherichia coli JM109 cells Corynebacterium sp.

Protein Variants

Protein Variants Comment Organism
K233G the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
K233H the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
K233M the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
K233Q the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
K233R the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
K233S the mutant shows wild type NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
K233T the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235C the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235D the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
R235E the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
R235G the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
R235H the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235M the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235N the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235Q the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235S the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R235T the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
R235Y the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
R238D the mutant shows no activity with NADPH and NADH Corynebacterium sp.
R238E the mutant shows no activity with NADPH and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
R238F the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
R238G the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
R238H the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
R238N the mutant shows reduced NADPH activity and no NADH activity Corynebacterium sp.
R238Q the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
R238Y the mutant shows reduced NADPH activity and increased NADH activity ompared to the wild type enzyme Corynebacterium sp.
S233E the mutant shows no activity with NADPH and NADH Corynebacterium sp.
S233K the mutant shows no activity with NADPH and NADH Corynebacterium sp.
S233M the mutant shows no activity with NADPH and NADH Corynebacterium sp.
S233N the mutant shows no activity with NADPH and NADH Corynebacterium sp.
S233T the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
S233V the mutant shows no activity with NADPH and NADH Corynebacterium sp.
V234D the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234E the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234I the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234M the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234M/R235C the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234N the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234Q the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
V234S the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
1 * 34000, SDS-PAGE Corynebacterium sp.

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE cellulose resin column chromatography, gel filtration 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+
-
?
additional information the wild type enzyme shows no activity with NADH Corynebacterium sp. ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 34000, SDS-PAGE Corynebacterium sp.

Synonyms

Synonyms Comment Organism
2,5-diketo-D-gluconic acid reductase A
-
Corynebacterium sp.
2,5-DKG reductase
-
Corynebacterium sp.
AKR5C
-
Corynebacterium sp.

Cofactor

Cofactor Comment Organism Structure
NADPH dependent on Corynebacterium sp.