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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.274 expresssion of several isoenzyme A mutants in Escherichia coli Corynebacterium sp.
1.1.1.346 mutant enzymes are expressed in Escherichia coli JM109 cells Corynebacterium sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.274 K232 isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 K232Q isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 K232S isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 R235G isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 R235T isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 R238E isoenzyme A, designed to improve the ability to use NADH as cofactor Corynebacterium sp.
1.1.1.274 R238H isoenzyme A, designed to improve the ability to use NADH as cofactor, 7fold higher activity with NADH than wild-type Corynebacterium sp.
1.1.1.346 K233G the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
1.1.1.346 K233H the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 K233M the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
1.1.1.346 K233Q the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
1.1.1.346 K233R the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 K233S the mutant shows wild type NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
1.1.1.346 K233T the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235C the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235D the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 R235E the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 R235G the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
1.1.1.346 R235H the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235M the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235N the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235Q the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235S the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R235T the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
1.1.1.346 R235Y the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 R238D the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 R238E the mutant shows no activity with NADPH and increased NADH activity compared to the wild type enzyme Corynebacterium sp.
1.1.1.346 R238F the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R238G the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 R238H the mutant shows wild type NADPH activity and increased NADH activity Corynebacterium sp.
1.1.1.346 R238N the mutant shows reduced NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 R238Q the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.
1.1.1.346 R238Y the mutant shows reduced NADPH activity and increased NADH activity ompared to the wild type enzyme Corynebacterium sp.
1.1.1.346 S233E the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 S233K the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 S233M the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 S233N the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 S233T the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 S233V the mutant shows no activity with NADPH and NADH Corynebacterium sp.
1.1.1.346 V234D the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234E the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234I the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234M the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234M/R235C the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234N the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234Q the mutant shows wild type NADPH activity and no NADH activity Corynebacterium sp.
1.1.1.346 V234S the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity Corynebacterium sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.274 2
-
 NADH isoenzyme A, K232G mutant Corynebacterium sp.
1.1.1.274 2.1
-
 NADH isoenzyme A, R238H mutant Corynebacterium sp.
1.1.1.274 2.6
-
 NADH isoenzyme A, wild-type Corynebacterium sp.
1.1.1.274 2.8
-
 NADH isoenzyme A, K232S mutant Corynebacterium sp.
1.1.1.274 3.9
-
 NADH isoenzyme A, K232M mutant Corynebacterium sp.
1.1.1.274 3.9
-
 NADH isoenzyme A, K232Q mutant Corynebacterium sp.
1.1.1.274 8.4
-
 NADH isoenzyme A, R235G mutant Corynebacterium sp.
1.1.1.274 8.4
-
 NADH isoenzyme A, R238E mutant Corynebacterium sp.
1.1.1.274 8.8
-
 NADH isoenzyme A, R235T mutant Corynebacterium sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.346 34000
-
 1 * 34000, SDS-PAGE Corynebacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.274 Corynebacterium sp. P06632
-
-
1.1.1.346 Corynebacterium sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.346 DEAE cellulose resin column chromatography, gel filtration Corynebacterium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.274 2,5-didehydro-D-gluconate + NADH
-
 Corynebacterium sp. 2-keto-L-gulonate + NAD+
-
 ?
1.1.1.346 2,5-didehydro-D-gluconate + NADPH + H+
-
 Corynebacterium sp. 2-dehydro-L-gulonate + NADP+
-
 ?
1.1.1.346 additional information the wild type enzyme shows no activity with NADH Corynebacterium sp. ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.346 2,5-diketo-D-gluconic acid reductase A
-
 Corynebacterium sp.
1.1.1.346 2,5-DKG reductase
-
 Corynebacterium sp.
1.1.1.346 AKR5C
-
 Corynebacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.346 NADPH dependent on Corynebacterium sp.