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Enzyme Nomenclature
Information on EC 1.1.1.118 - glucose 1-dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.118
Word Map on EC 1.1.1.118
- 1.1.1.118
- gluconate
- quinone
-
electrode
-
pyrroloquinoline
- subtilis
-
electrochemical
- pqq
-
biosensors
- megaterium
-
biocatalyst
-
biofuel
-
quinoproteins
- acinetobacter
- calcoaceticus
-
anode
-
amperometric
-
nanotube
-
entner-doudoroff
-
cathode
- 2-ketogluconate
- gluconobacter
-
bioanode
- acidophilum
-
glassy
- oxydans
-
thermoplasma
-
pqq-dependent
- 4-chloro-3-oxobutanoate
-
quinone-dependent
-
forespore
-
bioreduction
-
glucometer
-
phosphate-solubilizing
-
bioelectrocatalytic
-
electrocatalytic
-
dipicolinic
-
electrocatalysts
-
biocathode
-
bioelectronic
-
icodextrin
- synthesis
- biotechnology
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.118
-
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RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:NAD+ 1-oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-49-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxy-D-glucose + NAD+
? + NADH
-
26% activity compared to D-glucose in combination with NAD+
-
-
?
2-amino-2-deoxy-D-glucose + NADP+
? + NADPH
-
5% activity compared to D-glucose in combination with NAD+
-
-
?
2-deoxy-D-glucose + NADP+
? + NADPH
-
25% activity compared to D-glucose in combination with NAD+
-
-
?
3,6-dideoxy-D-galactose + NAD+
3,6-dideoxy-D-galactono-1,5-lactone + NADH
-
-
-
-
?
6-deoxy-D-glucose + NADP+
? + NADPH
-
9% activity compared to D-glucose in combination with NAD+
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH + H+
-
5% activity compared to D-glucose in combination with NAD+
-
-
?
D-altrose + NADP+
? + NADPH
-
12% activity compared to D-glucose in combination with NAD+
-
-
?
D-galactose + NADH
D-galactono-1,5-lactone + NADH + H+
-
15% activity compared to D-glucose in combination with NAD+
-
-
?
D-gulose + NAD+
? + NADH
-
8% activity compared to D-glucose in combination with NAD+
-
-
?
D-gulose + NADP+
? + NADPH
-
12% activity compared to D-glucose in combination with NAD+
-
-
?
D-idose + NAD+
? + NADH
-
65% activity compared to D-glucose in combination with NAD+
-
-
?
D-idose + NADP+
? + NADPH
-
12% activity compared to D-glucose in combination with NAD+
-
-
?
D-mannose + NADP+
? + NADPH
-
4% activity compared to D-glucose in combination with NAD+
-
-
?
D-ribose + NADP+
? + NADPH
-
4% activity compared to D-glucose in combination with NAD+
-
-
?
D-xylose + NAD+
? + NADH
-
26% activity compared to D-glucose in combination with NAD+
-
-
?
D-xylose + NADP+
? + NADPH
-
28% activity compared to D-glucose in combination with NAD+
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
12% activity compared to D-glucose in combination with NAD+
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
-
12% activity compared to D-glucose in combination with NAD+
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
66% activity compared to D-glucose in combination with NAD+
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
-
66% activity compared to D-glucose in combination with NAD+
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
-
100% activity
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
9% activity compared to D-glucose in combination with NAD+
-
-
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
9% activity compared to D-glucose in combination with NAD+
-
-
?
additional information
?
-
-
no activity with: D-glucuronic acid, D-galacturonic acid, D-galactose 6-phosphate, D-glucose 6-phosphate, D-glucosamine, N-acetyl-D-glucosamine, 6-deoxy-D-allose, 6-iodo-6-deoxy-D-galactose, 2-acetamide-6-deoxy-D-allose, 2-acetamido-6-deoxy-D-altrose
-
-
-
additional information
?
-
-
no activity with: D-glucuronic acid, D-galacturonic acid, D-galactose 6-phosphate, D-glucose 6-phosphate, D-glucosamine, N-acetyl-D-glucosamine, 6-deoxy-D-allose, 6-iodo-6-deoxy-D-galactose, 2-acetamide-6-deoxy-D-allose, 2-acetamido-6-deoxy-D-altrose
-
-
-
additional information
?
-
-
no activity towards D-mannose,D-galactose, and D-ribose in combination with NAD+
-
-
-
additional information
?
-
-
no activity towards D-mannose,D-galactose, and D-ribose in combination with NAD+
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Zn2+ is partially effective, whereas Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
5% residual activity at 50 mM, addition of Mg2+ in excess restored the initial activity
NADPH
-
inhibits the NAD+-dependent carbohydrate oxidations in a competitive manner with respect to NAD+
additional information
-
D-alactose, D-mannose and D-ribose, in concentrations as high as 0.04 mM do not inhibit glucose oxidation by NAD+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
D-galactose
-
in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.03
NADP+
-
in the presence of D-galactose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C; in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C; in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.44
D-glucose
-
in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
8
D-glucose
-
in the presence of NAD+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
2.2
D-xylose
-
in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
68
D-xylose
-
in the presence of NAD+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
1.2
NAD+
-
in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C; in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60200
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
homodimer
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
homodimer
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
-
homotetramer
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
homotetramer
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
the enzyme stability does not vary significantly in the pH range 5-9
639110
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Ethanol
Methanol
SDS
-
a slow time-dependent decrease of activity is observed in the presence of 0.1% SDS
urea
additional information
Acetone
-
stable in the presence of chaotropic agents and water-miscible organic solvents such as acetone
Acetone
-
stable in the presence of chaotropic agents and water-miscible organic solvents such as acetone
-
Ethanol
-
a slow time-dependent decrease of activity is observed in the presence of ethanol
Ethanol
-
a slow time-dependent decrease of activity is observed in the presence of ethanol
-
Methanol
-
stable in the presence of chaotropic agents and water-miscible organic solvents such as methanol
Methanol
-
stable in the presence of chaotropic agents and water-miscible organic solvents such as methanol
-
urea
-
a slow time-dependent decrease of activity is observed in the presence of 4 M urea
urea
-
a slow time-dependent decrease of activity is observed in the presence of 4 M urea
-
additional information
-
2 M urea and 0.05% (w/v) SDS do not cause any loss of enzymic activity
additional information
-
2 M urea and 0.05% (w/v) SDS do not cause any loss of enzymic activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 40 days, 50% loss of activity
-
4°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, several months, remains stable
-
70°C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 45 h, 50% loss of activity
-
stable to freezing for at least 6 months, pH 7.0, 10 mM sodium phosphate buffer
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
SP-Sephadex C-50 gel filtration, phenyl-Sepharose column chromatography, and Affi-Gel Blue matrix gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tag GDH variants, into pET28a and expressed in Escherichia coli BL21(DE3)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E170K
-
has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65°C. Stability dependence on salt concentration
E170K/Q252L
-
has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
P45A/F155Y/V227A
-
has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65°C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
-
has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
E170K
-
has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65°C. Stability dependence on salt concentration
-
E170K/Q252L
-
has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
-
P45A/F155Y/V227A
-
has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65°C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
-
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
-
has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65°C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
immobilization of GDH1 on the surface of a graphite felt electrode, construction and optimization of an electrochemical bioreactor, co-immobilization of 3,4-dihydroxybenzaldehyde as mediator allows the system to operate at 0.2 V and increases both the activity (2.4-times) and the stability of the immobilized enzyme by 2.2-times, the immobilized enzyme is termed IMGDH1
synthesis
synthesis
-
glucose dehydrogenase and L-carnitine dehydrogenase are coimmobilized in a nanofiltration membrane bioreactor for the continuous production of 1-carnitine from 3-dehydrocarnitine with NADH regeneration
synthesis
-
glucose dehydrogenase and L-carnitine dehydrogenase are coimmobilized in a nanofiltration membrane bioreactor for the continuous production of 1-carnitine from 3-dehydrocarnitine with NADH regeneration
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.118)
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