BRENDA - Enzyme Database show
show all sequences of 1.1.1.119

Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterization and N-terminal sequence

Bonete, M.J.; Pire, C.; Llorca, F.I.; Camacho, M.L.; FEBS Lett. 383, 227-229 (1996)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
2 mM
Haloferax mediterranei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
NADP+
pH 8.8, 40C
Haloferax mediterranei
1.2
-
NAD+
pH 8.8, 40C
Haloferax mediterranei
3.9
-
beta-D-glucose
pH 8.8, 40C
Haloferax mediterranei
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
KCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Haloferax mediterranei
Mg2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mg2+ is more effective than Mg2+ or Ni2+
Haloferax mediterranei
Mn2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+
Haloferax mediterranei
NaCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Haloferax mediterranei
Ni2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Ni2+ is more effective than Mg2+ or Mn2+
Haloferax mediterranei
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
2 * 53000, SDS-PAGE
Haloferax mediterranei
89000
-
gel filtration
Haloferax mediterranei
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Haloferax mediterranei
Q977U7
-
-
Haloferax mediterranei DSM 1411
Q977U7
-
-
Purification (Commentary)
Commentary
Organism
-
Haloferax mediterranei
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
550
-
pH 8.8, 40C
Haloferax mediterranei
Storage Stability
Storage Stability
Organism
4C, stable for several months
Haloferax mediterranei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-D-glucose + NAD+
activity with NAD+ is 26% of the activity with NADP+
639098
Haloferax mediterranei
?
-
-
-
?
beta-D-glucose + NAD+
activity with NAD+ is 26% of the activity with NADP+
639098
Haloferax mediterranei DSM 1411
?
-
-
-
?
beta-D-glucose + NADP+
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
639098
Haloferax mediterranei
?
-
-
-
?
beta-D-glucose + NADP+
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
639098
Haloferax mediterranei DSM 1411
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 53000, SDS-PAGE
Haloferax mediterranei
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
65
-
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
Haloferax mediterranei
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
Haloferax mediterranei
NADP+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
Haloferax mediterranei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
Haloferax mediterranei
NADP+
Km-value for NAD+ is 50fold higher than Km-value for NADP+
Haloferax mediterranei
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
2 mM
Haloferax mediterranei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.024
-
NADP+
pH 8.8, 40C
Haloferax mediterranei
1.2
-
NAD+
pH 8.8, 40C
Haloferax mediterranei
3.9
-
beta-D-glucose
pH 8.8, 40C
Haloferax mediterranei
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
KCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Haloferax mediterranei
Mg2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mg2+ is more effective than Mg2+ or Ni2+
Haloferax mediterranei
Mn2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+
Haloferax mediterranei
NaCl
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
Haloferax mediterranei
Ni2+
besides KCl/NaCl, the activity also depends on presence of bivalent cations. Ni2+ is more effective than Mg2+ or Mn2+
Haloferax mediterranei
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53000
-
2 * 53000, SDS-PAGE
Haloferax mediterranei
89000
-
gel filtration
Haloferax mediterranei
Purification (Commentary) (protein specific)
Commentary
Organism
-
Haloferax mediterranei
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
550
-
pH 8.8, 40C
Haloferax mediterranei
Storage Stability (protein specific)
Storage Stability
Organism
4C, stable for several months
Haloferax mediterranei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
beta-D-glucose + NAD+
activity with NAD+ is 26% of the activity with NADP+
639098
Haloferax mediterranei
?
-
-
-
?
beta-D-glucose + NAD+
activity with NAD+ is 26% of the activity with NADP+
639098
Haloferax mediterranei DSM 1411
?
-
-
-
?
beta-D-glucose + NADP+
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
639098
Haloferax mediterranei
?
-
-
-
?
beta-D-glucose + NADP+
activity with NAD+ is 26% of the activity with NADP+. The enzyme shows also activity with D-fucose and NADP+ (at 18% compared to the activity with beta-D-glucose and NADP+), with D-galactose and NADP+ (at 13% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NAD+ (at 79% compared to the activity with beta-D-glucose and NADP+), with D-xylose and NADP+ (at 88% compared to the activity with beta-D-glucose and NADP+)
639098
Haloferax mediterranei DSM 1411
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 53000, SDS-PAGE
Haloferax mediterranei
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
65
-
half-life: 56.8 h, in the presence of 3 M NaCl, stability decreases significantly with lower salt concentrations
Haloferax mediterranei
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)
728011
Sugii
Characterization of the low-te ...
Sulfolobus tokodaii, Sulfolobus tokodaii DSM 16993
J. Biosci. Bioeng.
118
367-371
2014
-
-
1
-
1
-
-
12
-
-
-
2
-
2
-
-
1
-
-
-
-
-
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
-
-
-
-
-
-
-
12
12
699602
Pire
-
Alteration of coenzyme specifi ...
Haloferax mediterranei
J. Mol. Catal. B
59
261-265
2009
-
-
1
-
4
-
3
25
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-
-
-
-
2
-
-
1
-
1
-
-
1
6
-
-
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7
-
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-
2
10
-
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-
2
3
-
8
-
-
3
10
34
-
-
-
-
-
-
-
1
1
-
-
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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1
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684637
Schewe
Improvement of P450(BM-3) whol ...
Bacillus megaterium
Appl. Microbiol. Biotechnol.
78
55-65
2008
-
2
1
-
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
-
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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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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-
-
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
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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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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
-
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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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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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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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2
-
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2
1
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5
-
2
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2
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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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1
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1
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4
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1
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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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2
4
7
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1
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1
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1
2
4
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
2
-
4
-
7
-
-
-
-
-
-
-
1
-
-
1
2
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-