Information on EC 1.1.1.118 - glucose 1-dehydrogenase (NAD+)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.118
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RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose + NAD+ = D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Entner Doudoroff pathway
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SYSTEMATIC NAME
IUBMB Comments
D-glucose:NAD+ 1-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-49-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
No. 93-1
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Manually annotated by BRENDA team
No. 93-1
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Manually annotated by BRENDA team
i.e. Acetobacter xylinum
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Manually annotated by BRENDA team
IAM 12014
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Manually annotated by BRENDA team
IAM 12014
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Manually annotated by BRENDA team
MSU-1
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Manually annotated by BRENDA team
strain MT-4, previously named Caldariella acidofila
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Manually annotated by BRENDA team
strain MT-4, previously named Caldariella acidofila
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxy-D-glucose + NAD+
? + NADH
show the reaction diagram
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26% activity compared to D-glucose in combination with NAD+
-
-
?
2-amino-2-deoxy-D-glucose + NADP+
? + NADPH
show the reaction diagram
-
5% activity compared to D-glucose in combination with NAD+
-
-
?
2-deoxy-D-galactose + NAD+
2-deoxy-D-galactono-1,5-lactone + NADH
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + NAD+
2-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
2-deoxy-D-glucose + NADP+
? + NADPH
show the reaction diagram
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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
show the reaction diagram
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-
-
-
?
6-deoxy-D-galactose + NAD+
6-deoxy-D-galactono-1,5-lactone + NADH
show the reaction diagram
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-
-
-
?
6-deoxy-D-glucose + NAD+
6-deoxy-D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
6-deoxy-D-glucose + NADP+
? + NADPH
show the reaction diagram
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9% activity compared to D-glucose in combination with NAD+
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-
?
D-allose + NAD+
D-allono-1,5-lactone + NADH
show the reaction diagram
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-
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH
show the reaction diagram
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-
-
-
?
D-altrose + NAD+
D-altrono-1,5-lactone + NADH + H+
show the reaction diagram
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5% activity compared to D-glucose in combination with NAD+
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-
?
D-altrose + NADP+
? + NADPH
show the reaction diagram
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12% activity compared to D-glucose in combination with NAD+
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?
D-galactose + NAD+
D-galactono-1,5-lactone + NADH
show the reaction diagram
D-galactose + NADH
D-galactono-1,5-lactone + NADH + H+
show the reaction diagram
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15% activity compared to D-glucose in combination with NAD+
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-
?
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
show the reaction diagram
D-gulose + NAD+
? + NADH
show the reaction diagram
-
8% activity compared to D-glucose in combination with NAD+
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?
D-gulose + NADP+
? + NADPH
show the reaction diagram
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12% activity compared to D-glucose in combination with NAD+
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?
D-idose + NAD+
? + NADH
show the reaction diagram
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65% activity compared to D-glucose in combination with NAD+
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?
D-idose + NADP+
? + NADPH
show the reaction diagram
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12% activity compared to D-glucose in combination with NAD+
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?
D-mannose + NAD+
D-manno-1,5-lactone + NADH
show the reaction diagram
D-mannose + NADP+
? + NADPH
show the reaction diagram
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4% activity compared to D-glucose in combination with NAD+
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?
D-ribose + NADP+
? + NADPH
show the reaction diagram
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4% activity compared to D-glucose in combination with NAD+
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?
D-xylose + NAD+
? + NADH
show the reaction diagram
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26% activity compared to D-glucose in combination with NAD+
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?
D-xylose + NADP+
? + NADPH
show the reaction diagram
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28% activity compared to D-glucose in combination with NAD+
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose + NAD+
D-glucono-1,5-lactone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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maximally active at 20 mM
Mg2+
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maximally active at 20 mM
Mn2+
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maximally active at 20 mM
additional information
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Zn2+ is partially effective, whereas Ni2+, Cd2+ and univalent cations are ineffective in promoting enzyme reactivation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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rapid inactivation at 1 mM
5,5'-dithiobis-(2-nitrobenzoic acid)
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EDTA
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5% residual activity at 50 mM, addition of Mg2+ in excess restored the initial activity
Guanidinium chloride
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rapid inactivation at 4 M
N-ethylmaleimide
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NADPH
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inhibits the NAD+-dependent carbohydrate oxidations in a competitive manner with respect to NAD+
tetrahydrofuran
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additional information
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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 hide
LITERATURE
IMAGE
5.8
D-fucose
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22
D-galactose
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in the presence of NADP+, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70C
0.44 - 8
D-glucose
2.2 - 68
D-xylose
1.2 - 80
NAD+
0.03
NADP+
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in the presence of D-galactose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70C; in the presence of D-glucose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70C; in the presence of D-xylose, in 100 mM triethanolamine/HCl buffer, 20 mM MgCl2, at 70C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
NADPH
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using D-glucose as a substrate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
5,5'-dithiobis-(2-nitrobenzoic acid)
Sulfolobus solfataricus
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at 25C and pH 9
1
N-ethylmaleimide
Sulfolobus solfataricus
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at 25C and pH 9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
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unpurified enzyme, at 70C
437
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after 623fold purification, at 70C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
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Tris-HCl buffer
9 - 10
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glycine-NaOH buffer
10 - 10.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30100
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4 * 30100, gel filtration, in the presence of 5% (w/v) SDS
60200
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2 * 60200, gel filtration, in the presence of 6 M guanidinium chloride
124000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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the enzyme stability does not vary significantly in the pH range 5-9
639110
6 - 8
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30C, 30 min, stable
285777
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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pH 7.0, 10 min, stable up to
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
Ethanol
Methanol
SDS
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a slow time-dependent decrease of activity is observed in the presence of 0.1% SDS
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 40 days, 50% loss of activity
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4C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, several months, remains stable
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70C, in the presence of 20 mM MgCl2 and 20% (v/v) ethylene glycol, 45 h, 50% loss of activity
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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
His-tag GDH variants
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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 hide
LITERATURE
E170K
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has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65C. Stability dependence on salt concentration
E170K/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
P45A/F155Y/V227A
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has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
E170K
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has enhanced stability when compared to the wild-type with half-life of ca. 9 min at 65C. Stability dependence on salt concentration
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E170K/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65C. The mutant demonstrates high stability regardless of salt-type at both water activities of 0.99 and 0.95
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P45A/F155Y/V227A
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has enhanced stability when compared to the wild-type with half-life of ca. 0.05 min at 65C. Most labile variant has significantly lower stability in ethanol, acetone, and 1,4-dioxane than other variants
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P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
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has enhanced stability when compared to the wild-type with half-life of ca. 5000 min at 65C. 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 hide
LITERATURE
biotechnology
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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