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Literature summary for 1.1.1.47 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

Application Comment Organism
analysis usage for quantitative determination of glucose in clinical tests and in the food industry Priestia megaterium
diagnostics usage for quantitative determination of glucose in clinical tests and in the food industry Priestia megaterium
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)

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

Protein Variants

Protein Variants Comment Organism
Q252L natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme Priestia megaterium
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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

pH Range

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

Cofactor

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