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Literature summary for 1.1.1.47 extracted from

  • Ding, H.; Gao, F.; Liu, D.; Li, Z.; Xu, X.; Wu, M.; Zhao, Y.
    Significant improvement of thermal stability of glucose 1-dehydrogenase by introducing disulfide bonds at the tetramer interface (2013), Enzyme Microb. Technol., 53, 365-372.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Lysinibacillus sphaericus

Protein Variants

Protein Variants Comment Organism
DS255 the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.072
-
NADP+ wild type enzyme, at pH 8.0 and 25°C Lysinibacillus sphaericus
0.094
-
NAD+ wild type enzyme, at pH 8.0 and 25°C Lysinibacillus sphaericus
0.197
-
NADP+ mutant enzyme DS255, at pH 8.0 and 25°C Lysinibacillus sphaericus
0.293
-
NAD+ mutant enzyme DS255, at pH 8.0 and 25°C Lysinibacillus sphaericus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
4 * 30000, SDS-PAGE Lysinibacillus sphaericus
120000
-
gel filtration Lysinibacillus sphaericus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + NAD+ Lysinibacillus sphaericus
-
D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NAD+ Lysinibacillus sphaericus G10
-
D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NADP+ Lysinibacillus sphaericus
-
D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose + NADP+ Lysinibacillus sphaericus G10
-
D-glucono-1,5-lactone + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus C5IFU0
-
-
Lysinibacillus sphaericus G10 C5IFU0
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NAD+
-
Lysinibacillus sphaericus D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NAD+
-
Lysinibacillus sphaericus G10 D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NADP+
-
Lysinibacillus sphaericus D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose + NADP+
-
Lysinibacillus sphaericus G10 D-glucono-1,5-lactone + NADPH + H+
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 30000, SDS-PAGE Lysinibacillus sphaericus

Synonyms

Synonyms Comment Organism
GDH
-
Lysinibacillus sphaericus
glucose 1-dehydrogenase
-
Lysinibacillus sphaericus
NAD(P)-dependent glucose 1-dehydrogenase
-
Lysinibacillus sphaericus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
the enzyme shows half-lives of 23100, 364.5, and 5.3 min after 10 min at 30°C, 40°C, and 50°C, respectively. The enzyme is inactive after 10 min at 60°C Lysinibacillus sphaericus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
93
-
NADP+ wild type enzyme, at pH 8.0 and 25°C Lysinibacillus sphaericus
115
-
NAD+ wild type enzyme, at pH 8.0 and 25°C Lysinibacillus sphaericus
130
-
NADP+ mutant enzyme DS255, at pH 8.0 and 25°C Lysinibacillus sphaericus
180
-
NAD+ mutant enzyme DS255, at pH 8.0 and 25°C Lysinibacillus sphaericus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
in glycine-NaOH buffer Lysinibacillus sphaericus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Lysinibacillus sphaericus
NADP+
-
Lysinibacillus sphaericus