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Literature summary for 1.1.1.47 extracted from

  • Pongtharangkul, T.; Chuekitkumchorn, P.; Suwanampa, N.; Payongsri, P.; Honda, K.; Panbangred, W.
    Kinetic properties and stability of glucose dehydrogenase from Bacillus amyloliquefaciens SB5 and its potential for cofactor regeneration (2015), AMB Express, 5, 68.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Bacillus amyloliquefaciens

Inhibitors

Inhibitors Comment Organism Structure
acetone 1% residual activity at 50% (v/v) Bacillus amyloliquefaciens
ethanol 19% residual activity at 50% (v/v) Bacillus amyloliquefaciens
n-butanol 1% residual activity at 50% (v/v) Bacillus amyloliquefaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
NADP+ at pH 8.0 and 37°C Bacillus amyloliquefaciens
0.25
-
NAD+ at pH 8.0 and 37°C Bacillus amyloliquefaciens
5.5
-
D-glucose with NADP+ as cosubstrate,at pH 8.0 and 37°C Bacillus amyloliquefaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
-
Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + NAD+ Bacillus amyloliquefaciens
-
D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NAD+ Bacillus amyloliquefaciens SB5
-
D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NADP+ Bacillus amyloliquefaciens
-
D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose + NADP+ Bacillus amyloliquefaciens SB5
-
D-glucono-1,5-lactone + NADPH + H+
-
?

Organic Solvent Stability

Organic Solvent Comment Organism
1-hexanol the enzyme exhibits an extreme tolerance towards 1-hexanol with 6%loss of activity at 10% (v/v) Bacillus amyloliquefaciens
2-hexanol the enzyme exhibits an extreme tolerance towards 2-hexanol with 7%loss of activity at 50% (v/v) Bacillus amyloliquefaciens
DMSO the enzyme exhibits an extreme tolerance towards DMSO with 1% loss of activity at 50% (v/v) Bacillus amyloliquefaciens
n-hexane the enzyme exhibits an extreme tolerance towards n-hexane with no loss of activity at 50% (v/v) Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-
Bacillus amyloliquefaciens SB5
-
-
-

Purification (Commentary)

Purification (Comment) Organism
PrepEase histidine-tagged protein purification kits Bacillus amyloliquefaciens

Storage Stability

Storage Stability Organism
-80°C, in CPB buffer (pH 6.0), at least 4 months, no loss of activity Bacillus amyloliquefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + NAD+
-
Bacillus amyloliquefaciens D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NAD+
-
Bacillus amyloliquefaciens SB5 D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose + NADP+
-
Bacillus amyloliquefaciens D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose + NADP+
-
Bacillus amyloliquefaciens SB5 D-glucono-1,5-lactone + NADPH + H+
-
?

Subunits

Subunits Comment Organism
? x * 28000, His6-tagged enzyme, SDS-PAGE Bacillus amyloliquefaciens

Synonyms

Synonyms Comment Organism
glucose dehydrogenase
-
Bacillus amyloliquefaciens
GluDH
-
Bacillus amyloliquefaciens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Bacillus amyloliquefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
the enzyme is stable up to 42°C Bacillus amyloliquefaciens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
70
-
D-glucose at pH 8.0 and 37°C Bacillus amyloliquefaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
Bacillus amyloliquefaciens

pH Range

pH Minimum pH Maximum Comment Organism
5 8 when incubated for 6 h at 37°C, the enzyme is highly stable in acidic conditions (pH 5.0-6.0) but is completely inactivated at pH values above 8.0 Bacillus amyloliquefaciens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus amyloliquefaciens
NADP+
-
Bacillus amyloliquefaciens