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Information on EC 1.1.1.118 - glucose 1-dehydrogenase (NAD+)
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EC Tree
1.1.1.118 glucose 1-dehydrogenase (NAD+)Specify your search results
Word Map
- 1.1.1.118
- gluconate
-
electrode
- quinone
-
pyrroloquinoline
-
electrochemical
-
biosensors
- pqq
-
biocatalyst
-
megaterium
-
biofuel
-
enantiomeric
-
anode
-
biocatalytic
-
quinoproteins
-
nanotube
-
cathode
-
amperometric
- calcoaceticus
-
pqq-dependent
-
entner-doudoroff
- 2-ketogluconate
- gluconobacter
-
fad-dependent
-
bioanode
-
bioelectrocatalytic
- acidophilum
-
bioreduction
-
thermoplasma
- oxydans
-
space-time
- sibiricum
-
biocathode
-
electrocatalysts
-
bioelectrochemical
-
glucometer
- forespore
-
dipicolinic
-
quinone-dependent
-
bioelectronic
-
self-powered
-
icodextrin
-
phosphate-solubilizing
- synthesis
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
glucose dehydrogenase, d-aldohexose dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GDH
glucose dehydrogenase
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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
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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+
Saccharolobus solfataricus MT-4 / DSM 5833
-
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+
Saccharolobus solfataricus MT-4 / DSM 5833
-
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+
Saccharolobus solfataricus MT-4 / DSM 5833
-
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+
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
?
-
Saccharolobus solfataricus MT-4 / DSM 5833
-
no activity towards D-mannose,D-galactose, and D-ribose in combination with NAD+
-
?
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NATURAL SUBSTRATE
NATURAL 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
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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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INHIBITOR
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
0.44
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
1.2
NAD+
-
in the presence of D-xylose, 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
0.03
NADP+
-
in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70°C
0.03
NADP+
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9HK51_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
255
0
27873
TrEMBL
-
Q97CM7_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
261
0
28195
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30100
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
60200
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
homodimer
-
2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
homodimer
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
Saccharolobus solfataricus MT-4 / DSM 5833
-
4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
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PROTEIN VARIANTS
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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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
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
Saccharolobus solfataricus MT-4 / DSM 5833
-
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
Saccharolobus solfataricus MT-4 / DSM 5833
-
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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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, A.S.L.; Cline, A.L.
The regulation of some sugar dehydrogenases in a Pseudomonad
Biochim. Biophys. Acta
93
237-245
1964
Pseudomonas sp.
brenda
Kobayashi, Y.; Horikoshi, K.
Identification and growth characteristics of alkalophilic Corynebacterium sp. which produces NAD(P)-dependent maltose dehydrogenase and glucose dehydrogenase
Agric. Biol. Chem.
44
41-47
1980
Corynebacterium sp., Corynebacterium sp. No. 93-1
-
brenda
Anderson, R.L.; Dahms, A.S.
D-Aldohexose dehydrogenase
Methods Enzymol.
41
147-150
1975
Pseudomonas sp., Pseudomonas sp. MSU-1
brenda
Lin, S.S.; Miyawaki, O.; Nakamura, K.
Continuous production of L-carnitine with NADH regeneration by a nanofiltration membrane reactor with coimmobilized L-carnitine dehydrogenase and glucose dehydrogenase
J. Biosci. Bioeng.
87
361-364
1999
Pseudomonas putida, Pseudomonas putida IAM 12014
brenda
Giardina, P.; DeBasia, M.G.; DeRosa, M.; Gambacort, A.; Buonocore, V.
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
Biochem. J.
239
517-522
1986
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
brenda
Manjon, A.; Obon, J.M.; Casanova, P.; Fernandez, V.M.; Ilborra1, J.L.
Increased activity of glucose dehydrogenase co-immobilized with a redox mediator in a bioreactor with electrochemical NAD+ regeneration
Biotechnol. Lett.
24
1227-1232
2002
Komagataeibacter xylinus
-
brenda
Vazquez-Figueroa, E.; Yeh, V.; Broering, J.; Chaparro-Riggers, J.; Bommarius, A.
Thermostable variants constructed via the structure-guided consensus method also show increased stability in salts solutions and homogeneous aqueous-organic media
Protein Eng. Des. Sel.
21
673-680
2008
Bacillus subtilis, Bacillus subtilis 168
brenda
Zhang, X.; Rao, Z.; Zhang, L.; Xu, M.; Yang, T.
Efficient 9alpha-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9alpha-hydroxylase and B. subtilis glucose 1-dehydrogenase with NADH regeneration
SpringerPlus
5
1207
2016
Bacillus subtilis, Bacillus subtilis 168
brenda
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