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Literature summary for 1.1.1.47 extracted from

  • Yokota, A.; Sasajima, K.; Yoneda, M.
    Reactivation of inactivated D-glucose dehydrogenase of a Bacillus species by pyridine and adenine nucleotides (1979), Agric. Biol. Chem., 43, 271-278.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
ADP NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
AMP NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
ATP NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
dipicolinic acid NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
NAD+ NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
NADH NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
NADP+ NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
NADPH NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)

General Stability

General Stability Organism
crude enzyme loses 90% activity after 3 days at 5°C Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.061
-
NADP+
-
Bacillus sp. (in: Bacteria)
0.082
-
NAD+
-
Bacillus sp. (in: Bacteria)
4.2
-
beta-D-glucose
-
Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
(NH4)2SO4 NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
KCl NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
Na2SO4 NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)
NaCl NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
inactive enzyme form, gel filtration Bacillus sp. (in: Bacteria)
80000
-
active enzyme form, gel filtration Bacillus sp. (in: Bacteria)

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
D-ribose producing mutant
-
Bacillus sp. (in: Bacteria) BG 1722
-
D-ribose producing mutant
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-cellulose, partially purified enzyme, 10 mM NAD(P)+ protects from inactivation on column Bacillus sp. (in: Bacteria)

Storage Stability

Storage Stability Organism
4°C, 89% loss of activity after 4 days without stabilzing agent, complete stabilization by 10 mM NAD+ or 10 mM NADP+, and to a lesser extent by 800 mM NaCl. Partial stabilization by 800 MM (NH4)2SO4, 800 mM Na2SO4 or 800 mM dipicolinic acid Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-glucose + NAD+ 113% of the activity with D-glucose Bacillus sp. (in: Bacteria) 2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
?
2-deoxy-D-glucose + NAD+ 113% of the activity with D-glucose Bacillus sp. (in: Bacteria) BG 1722 2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
?
2-deoxy-D-glucose + NADP+ 103% of the activity with D-glucose and NAD+ Bacillus sp. (in: Bacteria) 2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
?
2-deoxy-D-glucose + NADP+ 103% of the activity with D-glucose and NAD+ Bacillus sp. (in: Bacteria) BG 1722 2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
?
beta-D-glucose + NADP+ 93% of the activity with NAD+ Bacillus sp. (in: Bacteria) D-glucono-1,5-lactone + NADPH + H+
-
?
beta-D-glucose + NADP+ 93% of the activity with NAD+ Bacillus sp. (in: Bacteria) BG 1722 D-glucono-1,5-lactone + NADPH + H+
-
?
maltose + NAD+ 6% of the activity with D-glucose Bacillus sp. (in: Bacteria) ? + NADH
-
?
maltose + NAD+ 6% of the activity with D-glucose Bacillus sp. (in: Bacteria) BG 1722 ? + NADH
-
?
maltose + NADP+ 5% of the activity D-glucose and NAD+ Bacillus sp. (in: Bacteria) ? + NADPH
-
?
maltose + NADP+ 5% of the activity D-glucose and NAD+ Bacillus sp. (in: Bacteria) BG 1722 ? + NADPH
-
?

Subunits

Subunits Comment Organism
More
-
Bacillus sp. (in: Bacteria)
tetramer 2 * 45000, gel filtration of inactive monomeric enzyme Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Bacillus sp. (in: Bacteria)

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bacillus sp. (in: Bacteria)
NADP+
-
Bacillus sp. (in: Bacteria)