BRENDA - Enzyme Database show
show all sequences of 1.1.1.119

Crystallization and characterization of NADP-dependent D-glucose dehydrogenase from Gluconobacter suboxydans

Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.; Agric. Biol. Chem. 44, 301-308 (1980)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
-
Gluconobacter oxydans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Gluconobacter oxydans
Hg2+
-
Gluconobacter oxydans
Ni2+
-
Gluconobacter oxydans
p-chloromercuribenzoate
-
Gluconobacter oxydans
sulfhydryl reagents
-
Gluconobacter oxydans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADP+
-
Gluconobacter oxydans
5
-
D-glucose
-
Gluconobacter oxydans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
4 * 40000, SDS-PAGE
Gluconobacter oxydans
153000
-
gel filtration on Sephadex G-200
Gluconobacter oxydans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gluconobacter oxydans
-
IFO 12528
-
Purification (Commentary)
Commentary
Organism
column chromatography on DEAE-Sephadex A-50 and affinty chromatography by blue-dextran Sepharose 4B
Gluconobacter oxydans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
140
-
-
Gluconobacter oxydans
Storage Stability
Storage Stability
Organism
5°C, crystalline preparation in ammonium sulfate, 6 months
Gluconobacter oxydans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
4% of the reverse reaction when assayed with D-glucono-1,5-lactone and NADPH at neutral or weak alkaline pH
285782
Gluconobacter oxydans
D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-mannose + NADP+
-
285782
Gluconobacter oxydans
D-mannono-1,5-lactone + NADPH
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 40000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Gluconobacter oxydans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
in Tris-buffer
Gluconobacter oxydans
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Gluconobacter oxydans
NADPH
-
Gluconobacter oxydans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Gluconobacter oxydans
NADPH
-
Gluconobacter oxydans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Gluconobacter oxydans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Gluconobacter oxydans
Hg2+
-
Gluconobacter oxydans
Ni2+
-
Gluconobacter oxydans
p-chloromercuribenzoate
-
Gluconobacter oxydans
sulfhydryl reagents
-
Gluconobacter oxydans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADP+
-
Gluconobacter oxydans
5
-
D-glucose
-
Gluconobacter oxydans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
4 * 40000, SDS-PAGE
Gluconobacter oxydans
153000
-
gel filtration on Sephadex G-200
Gluconobacter oxydans
Purification (Commentary) (protein specific)
Commentary
Organism
column chromatography on DEAE-Sephadex A-50 and affinty chromatography by blue-dextran Sepharose 4B
Gluconobacter oxydans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
140
-
-
Gluconobacter oxydans
Storage Stability (protein specific)
Storage Stability
Organism
5°C, crystalline preparation in ammonium sulfate, 6 months
Gluconobacter oxydans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + NADP+
4% of the reverse reaction when assayed with D-glucono-1,5-lactone and NADPH at neutral or weak alkaline pH
285782
Gluconobacter oxydans
D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-mannose + NADP+
-
285782
Gluconobacter oxydans
D-mannono-1,5-lactone + NADPH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 40000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
-
Gluconobacter oxydans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
in Tris-buffer
Gluconobacter oxydans
Other publictions for EC 1.1.1.119
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Sugii
Characterization of the low-te ...
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1
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1
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12
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2
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2
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1
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4
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12
1
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1
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1
1
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1
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12
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2
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1
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4
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12
1
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-
-
-
-
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-
12
12
699602
Pire
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Alteration of coenzyme specifi ...
Haloferax mediterranei
J. Mol. Catal. B
59
261-265
2009
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-
1
-
4
-
3
25
-
-
-
-
-
2
-
-
1
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1
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1
6
-
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7
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2
10
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2
3
-
8
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3
10
34
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-
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1
1
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-
1
6
-
-
-
-
7
-
-
-
-
-
-
-
-
16
16
701014
Baker
Active site dynamics in the zi ...
Haloferax mediterranei
Proc. Natl. Acad. Sci. USA
106
779-784
2009
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1
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1
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1
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684637
Schewe
Improvement of P450(BM-3) whol ...
Bacillus megaterium
Appl. Microbiol. Biotechnol.
78
55-65
2008
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2
1
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1
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1
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1
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1
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696604
Sovic
The utilization of bathocuproi ...
Pseudomonas fluorescens
Bioorg. Chem.
36
91-95
2008
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1
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1
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1
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686754
Esclapez
Analysis of acidic surface of ...
Haloferax mediterranei
FEBS Lett.
581
837-842
2007
1
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4
-
1
9
-
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1
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-
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1
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3
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2
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1
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2
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4
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1
-
9
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-
-
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-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
728653
Britton
Analysis of protein solvent in ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Proc. Natl. Acad. Sci. USA
103
4846-4851
2006
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1
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1
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5
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1
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667073
Esclapez
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. F
61
743-746
2005
1
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-
1
1
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2
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6
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1
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1
1
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1
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1
2
1
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2
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2
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1
1
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656318
Satoh
Enzyme-catalyzed poly(3-hydrox ...
Cupriavidus necator
J. Biosci. Bioeng.
95
335-341
2003
-
1
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1
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285785
Johnsen
Different glycolytic pathways ...
Halococcus saccharolyticus
Arch. Microbiol.
175
52-61
2001
-
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3
-
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1
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1
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1
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3
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1
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1
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726569
Ferrer
Crystallization and preliminar ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
Acta Crystallogr. Sect. D
57
1887-1889
2001
-
-
1
1
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5
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1
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1
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1
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1
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285784
Kataoka
Escherichia coli transformant ...
Bacillus megaterium
Biosci. Biotechnol. Biochem.
62
167-169
1998
-
-
1
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1
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639098
Bonete
Glucose dehydrogenase from the ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
FEBS Lett.
383
227-229
1996
-
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1
3
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5
2
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9
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1
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1
1
4
1
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1
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2
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2
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1
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3
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5
2
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1
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1
1
4
1
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1
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285783
Buckmann
-
A different acceptance of aden ...
Bacillus megaterium, Filobasidium uniguttulatum
Biotechnol. Appl. Biochem.
14
104-113
1991
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5
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2
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7
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5
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5
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7
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285782
Adachi
-
Crystallization and characteri ...
Gluconobacter oxydans
Agric. Biol. Chem.
44
301-308
1980
-
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1
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5
2
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2
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1
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1
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1
1
2
1
1
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1
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1
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1
1
2
1
1
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1
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285781
Avigad
Aldohexose dehydrogenase from ...
Gluconobacter cerinus
Methods Enzymol.
41
142-147
1975
-
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2
3
5
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1
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4
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285780
Avigad
Purification and properties of ...
Gluconobacter cerinus
J. Biol. Chem.
243
1936-1941
1968
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7
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1
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