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Literature summary for 1.1.1.47 extracted from

  • Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
    Crystallization and characterization of NADP-dependent D-glucose dehydrogenase from Gluconobacter suboxydans (1980), Agric. Biol. Chem., 44, 301-308.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
precipitate collected by centrifugation and dissolved in a minimal volume of 0.1 M potassium phosphate buffer, pH 7.5, 1 mM 2-mercaptoethanol Gluconobacter oxydans

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
Gluconobacter oxydans
Hg2+
-
Gluconobacter oxydans
Ni2+
-
Gluconobacter oxydans
PCMB
-
Gluconobacter oxydans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
NADP+ pH 8.0, 25°C Gluconobacter oxydans
5
-
D-glucose pH 8.0, 25°C Gluconobacter oxydans

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Gluconobacter oxydans 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
4 * 40000, SDS-PAGE Gluconobacter oxydans
153000
-
gel filtration Gluconobacter oxydans

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sephadex, Blue-Dextran Sepharose, DEAE-Sephadex, crystallization Gluconobacter oxydans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
140
-
-
Gluconobacter oxydans

Storage Stability

Storage Stability Organism
5°C, crystalline preparation as suspension in ammonium sulfate, stable for 6 months Gluconobacter oxydans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + NADP+ in the reverse reaction only 4% of the reaction occurs at neutral pH Gluconobacter oxydans D-glucono-1,5-lactone + NADPH + H+
-
r
beta-D-glucose + NADP+ the enzyme is specific for NADP+ and completely inactive with NAD+ Gluconobacter oxydans D-glucono-1,5-lactone + NADPH + H+
-
r
D-glucose + NADP+
-
Gluconobacter oxydans D-glucono-1,5-lactone + NADPH + H+
-
r
D-mannose + NADP+ 88% of the activity with D-glucose Gluconobacter oxydans D-mannono-1,5-lactone + NADPH
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 40000, SDS-PAGE Gluconobacter oxydans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Gluconobacter oxydans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9
-
Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme is specific for NADP+ and completely inactive with NAD+ Gluconobacter oxydans
NADP+ the enzyme is specific for NADP+ and completely inactive with NAD+ Gluconobacter oxydans