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Literature summary extracted from

  • Mitamura, T.; Urabe, I.; Okada, H.
    Enzymatic properties of isozymes and variants of glucose dehydrogenase from Bacillus megaterium (1989), Eur. J. Biochem., 186, 389-393.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.47 expressed in Escherichia coli KP3998 cells Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.47 120000
-
GlcDH-I, gel filtration Priestia megaterium
1.1.1.47 150000
-
GlcDH-II, gel filtration Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Priestia megaterium
-
-
-
1.1.1.47 Priestia megaterium P39482
-
-
1.1.1.47 Priestia megaterium P40288
-
-
1.1.1.47 Priestia megaterium IAM 1030
-
-
-
1.1.1.47 Priestia megaterium IAM 1030 P39482
-
-
1.1.1.47 Priestia megaterium IWG3 P40288
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.47 DEAE-Sepharose CL-6B column chromatography Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.47 2-deoxy-D-glucose + NAD+
-
Priestia megaterium ?
-
?
1.1.1.47 2-deoxy-D-glucose + NAD+
-
Priestia megaterium IAM 1030 ?
-
?
1.1.1.47 2-deoxy-D-glucose + NAD+
-
Priestia megaterium IWG3 ?
-
?
1.1.1.47 D-fructose + NAD+ weak substrate Priestia megaterium ?
-
?
1.1.1.47 D-fructose + NAD+ weak substrate Priestia megaterium IAM 1030 ?
-
?
1.1.1.47 D-fructose + NAD+ weak substrate Priestia megaterium IWG3 ?
-
?
1.1.1.47 D-galactose + NAD+ weak substrate Priestia megaterium ?
-
?
1.1.1.47 D-galactose + NAD+ weak substrate Priestia megaterium IAM 1030 ?
-
?
1.1.1.47 D-galactose + NAD+ weak substrate Priestia megaterium IWG3 ?
-
?
1.1.1.47 D-glucosamine + NAD+
-
Priestia megaterium ?
-
?
1.1.1.47 D-glucose + NAD+ 100% activity Priestia megaterium D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 D-glucose + NAD+ 100% activity Priestia megaterium IAM 1030 D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 D-glucose + NAD+ 100% activity Priestia megaterium IWG3 D-glucono-1,5-lactone + NADH + H+
-
?
1.1.1.47 D-mannose + NAD+ weak substrate Priestia megaterium ?
-
?
1.1.1.47 D-xylose + NAD+ weak substrate Priestia megaterium ?
-
?
1.1.1.47 additional information no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol Priestia megaterium ?
-
?
1.1.1.47 additional information no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol Priestia megaterium IAM 1030 ?
-
?
1.1.1.47 additional information no activity with N-acetyl-D-glucosamine, D-glucose-6-phosphate, D-arabinose, D-ribose, and myo-inositol Priestia megaterium IWG3 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.47 GlcDH-I isozyme is unstable throughout pH range 4-10 Priestia megaterium
1.1.1.47 GlcDH-II isozyme is stable in the alkaline pH region Priestia megaterium
1.1.1.47 GlcDH-IWG3 isozyme is stable in the acidic pH region Priestia megaterium
1.1.1.47 glucose dehydrogenase
-
Priestia megaterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.47 50
-
GlcDH-I1 is the most resistant isozyme against heat inactivation at 50°C (pH 6.5) Priestia megaterium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.47 190
-
D-glucose isozyme GlcDH-I Priestia megaterium
1.1.1.47 190
-
D-glucose isozyme GlcDH-II Priestia megaterium
1.1.1.47 390
-
D-glucose isozyme GlcDH-IWG3 Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.47 8
-
-
Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.47 NAD+
-
Priestia megaterium