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Literature summary extracted from

  • Baik, S.H.; Ide, T.; Yoshida, H.; Kagami, O.; Harayama, S.
    Significantly enhanced stability of glucose dehydrogenase by directed evolution (2003), Appl. Microbiol. Biotechnol., 61, 329-335.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.1.47 analysis usage for quantitative determination of glucose in clinical tests and in the food industry Priestia megaterium
1.1.1.47 diagnostics usage for quantitative determination of glucose in clinical tests and in the food industry Priestia megaterium
1.1.1.47 synthesis usage as NADP+ cofactor regenerator for enzymatic synthesis of chiral compounds such as ethyl-(S)-4-chloro-3-hydroxybutanoate and ethyl 4-chloro-3-oxobutanoate Priestia megaterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.47 DNA sequence determination and analysis, expression in Escherichia coli strain JM109 Bacillus subtilis
1.1.1.47 DNA sequence determination and analysis, expression in Escherichia coli strain JM109 Priestia megaterium
1.1.1.47 DNA sequence determination and analysis, expression in Escherichia coli strain JM109 Bacillus licheniformis

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.47 Q252L natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme Priestia megaterium
1.1.1.47 Q252L/E170K site-directed mutagenesis of the mutant strain IWG3, the mutant is insensitive against NaCl concentration and pH value, slightly increased activity compared to the wild-type enzyme Priestia megaterium

General Stability

EC Number General Stability Organism
1.1.1.47 NaCl stabilizes the enzyme at alkline pH and elevated temperatures Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.47 8
-
 beta-D-glucose mutant Q252L, pH 8.0, 25°C Priestia megaterium
1.1.1.47 8.5
-
 beta-D-glucose mutant Q252L/E170K, pH 8.0, 25°C Priestia megaterium
1.1.1.47 14
-
 beta-D-glucose wild-type enzyme, pH 8.0, 25°C Priestia megaterium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.47 NaCl stabilizes the enzyme at alkline pH and elevated temperatures Priestia megaterium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.47 28200
-
 4 * 28200 Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.47 Bacillus licheniformis
-
 IFO 12200
-
1.1.1.47 Bacillus subtilis
-
 IFO 13719
-
1.1.1.47 Priestia megaterium
-
 mutant strain IWG3, wild-type strain IFO 15308
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.47 recombinant enzyme from Escherichia coli Bacillus subtilis
1.1.1.47 recombinant enzyme from Escherichia coli Bacillus licheniformis
1.1.1.47 recombinant wild-type and mutant enzymes from Escherichia coli Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.47 beta-D-glucose + NAD(P)+ best substrate, wild-type and mutant enzymes Priestia megaterium D-glucono-1,5-lactone + NAD(P)H + H+
-
 ?
1.1.1.47 beta-D-glucose + NAD+
-
 Bacillus subtilis D-glucono-1,5-lactone + NADH + H+
-
 ?
1.1.1.47 beta-D-glucose + NAD+
-
 Bacillus licheniformis D-glucono-1,5-lactone + NADH + H+
-
 ?
1.1.1.47 D-fructose + NAD(P)+ no activity with mutants Q252L and Q252L/E170K Priestia megaterium ? + NAD(P)H
-
 ?
1.1.1.47 D-galactose + NAD(P)+ low activity with wild-type and mutant enzymes Priestia megaterium D-galactono-1,5-lactone + NAD(P)H
-
 ?
1.1.1.47 D-maltose + NAD(P)+ no activity with mutants Q252L and Q252L/E170K Priestia megaterium ? + NAD(P)H
-
 ?
1.1.1.47 D-mannose + NAD(P)+ wild-type and mutant enzymes Priestia megaterium ? + NAD(P)H
-
 ?
1.1.1.47 D-xylose + NAD(P)+ wild-type and mutant enzymes Priestia megaterium D-xylono-1,5-lactone + NAD(P)H + H+
-
 ?
1.1.1.47 additional information no activity of wild-type and mutant enzymes with sucrose Priestia megaterium ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.47 More reversible dissociation in to inactive monomers at alkaline pH Priestia megaterium
1.1.1.47 tetramer 4 * 28200 Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
1.1.1.47 GlcDH
-
 Bacillus subtilis
1.1.1.47 GlcDH
-
 Priestia megaterium
1.1.1.47 GlcDH
-
 Bacillus licheniformis
1.1.1.47 glucose dehydrogenase
-
 Bacillus subtilis
1.1.1.47 glucose dehydrogenase
-
 Priestia megaterium
1.1.1.47 glucose dehydrogenase
-
 Bacillus licheniformis
1.1.1.47 More enzyme belongs to the family of short-chain dehydrogenases/reductases Bacillus subtilis
1.1.1.47 More enzyme belongs to the family of short-chain dehydrogenases/reductases Priestia megaterium
1.1.1.47 More enzyme belongs to the family of short-chain dehydrogenases/reductases Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.47 25
-
 assay at Bacillus subtilis
1.1.1.47 25
-
 assay at Priestia megaterium
1.1.1.47 25
-
 assay at Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.47 additional information
-
 thermostability is highly increased by addition of NaCl Priestia megaterium
1.1.1.47 66
-
 half-life: mutant Q252L 1.3 min, mutant Q252L/E170K 540 min Priestia megaterium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.47 317
-
 beta-D-glucose mutant Q252L, pH 8.0, 25°C Priestia megaterium
1.1.1.47 334
-
 beta-D-glucose mutant Q252L/E170K, pH 8.0, 25°C Priestia megaterium
1.1.1.47 395
-
 beta-D-glucose wild-type enzyme, pH 8.0, 25°C Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.47 8
-
 assay at Bacillus subtilis
1.1.1.47 8
-
 assay at Priestia megaterium
1.1.1.47 8
-
 assay at Bacillus licheniformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.47 additional information
-
 sharp drop in activity at alkaline pH of wild-type and mutant Q252L activities, not mutant Q252L/E170K Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.47 NAD+
-
 Bacillus subtilis
1.1.1.47 NAD+
-
 Priestia megaterium
1.1.1.47 NAD+
-
 Bacillus licheniformis
1.1.1.47 NADP+
-
 Priestia megaterium