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Literature summary for 1.1.1.346 extracted from

  • Sonoyama, T.; Kobayashi, K.
    Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp (1987), J. Ferment. Technol., 65, 311-317.
No PubMed abstract available
Search for more literature for 1.1.1.346

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
 NADPH isoform 2,5-diketo-D-gluconate reductase I, at pH 7.0 and 30°C Corynebacterium sp.
0.013
-
 NADPH isoform 2,5-diketo-D-gluconate reductase II, at pH 7.0 and 30°C Corynebacterium sp.
1.8
-
 2,5-didehydro-D-gluconate isoform 2,5-diketo-D-gluconate reductase I, at pH 7.0 and 30°C Corynebacterium sp.
13.5
-
 2,5-didehydro-D-gluconate isoform 2,5-diketo-D-gluconate reductase II, at pH 7.0 and 30°C Corynebacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 1 * 29000, isoform 2,5-diketo-D-gluconate reductase I, SDS-PAGE Corynebacterium sp.
34000
-
 1 * 34000, isoform 2,5-diketo-D-gluconate reductase II, SDS-PAGE Corynebacterium sp.

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-
Corynebacterium sp. SHS 0007
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Amicon Matrix Gel Red A gel filtration Corynebacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,5-didehydro-D-gluconate + NADPH + H+ 100% activity Corynebacterium sp. 2-dehydro-L-gulonate + NADP+
-
 ?
2,5-didehydro-D-gluconate + NADPH + H+ 100% activity Corynebacterium sp. SHS 0007 2-dehydro-L-gulonate + NADP+
-
 ?
5-dehydro-D-fructose + NADPH + H+ isoforms 2,5-diketo-D-gluconate reductase I and II show 150% and 13% activity, respectively, compared to 2,5-didehydro-D-gluconate Corynebacterium sp. L-sorbose + NADP+
-
 ?
additional information no activity with 2-dehydro-L-gulonate, 2-dehydro-D-gluconate, 5-dehydro-D-gluconate, D-fructose, and L-sorbose Corynebacterium sp. ?
-
 ?
additional information no activity with 2-dehydro-L-gulonate, 2-dehydro-D-gluconate, 5-dehydro-D-gluconate, D-fructose, and L-sorbose Corynebacterium sp. SHS 0007 ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 29000, isoform 2,5-diketo-D-gluconate reductase I, SDS-PAGE Corynebacterium sp.
monomer 1 * 34000, isoform 2,5-diketo-D-gluconate reductase II, SDS-PAGE Corynebacterium sp.

Synonyms

Synonyms Comment Organism
2,5-diketo-D-gluconate reductase I isoform Corynebacterium sp.
2,5-diketo-D-gluconate reductase II isoform Corynebacterium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 isoform 2,5-diketo-D-gluconate reductase I Corynebacterium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
 38 temperature stability of isoform 2,5-diketo-D-gluconate reductase I is measured by storing the enzyme in 0.1 M Tris-HC1 buffer (pH 7.0) for 1 h. The activity of the enzyme decreases gradually with temperature from 0°C to 27°C, falls rapidly above 27°C, and is lost completely at about 38°C. The remaining activity at 27°C is about 77% of that at 0°C Corynebacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7 isoform 2,5-diketo-D-gluconate reductase I Corynebacterium sp.
6 7.5 isoform 2,5-diketo-D-gluconate reductase II Corynebacterium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 7 when isoform I is incubated at different pH values for 3 h at 30°C, the remaining activity is about 29% of the original level at pH 5.0, about 65% at pH 6.0 and about 51% at pH 7.0 Corynebacterium sp.

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Corynebacterium sp.

pI Value

Organism Comment pI Value Maximum pI Value
Corynebacterium sp. isoform 2,5-diketo-D-gluconate reductase II, isoelectric focusing
-
 4.1
Corynebacterium sp. isoform 2,5-diketo-D-gluconate reductase I, isoelectric focusing
-
 4.3