BRENDA - Enzyme Database show
show all sequences of 1.1.1.113

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
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
Storage Stability
Storage Stability
Organism
4°C, stable for several months
Haloferax mediterranei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-xylose + NADP+
88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+)
639098
Haloferax mediterranei
?
-
-
-
?
D-xylose + NADP+
88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor 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
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
2 mM
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
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 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
D-xylose + NADP+
88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor NADP+)
639098
Haloferax mediterranei
?
-
-
-
?
D-xylose + NADP+
88% of the activity with D-glucose and NADP+. The enzyme shows also activity with D-xylose and NAD+ as cofactor, D-glucose (NADP+ or NAD+ as cofactor), D-fucose (cofactor NADP+) and D-galactose (cofactor 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 1.1.1.113
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)
738984
Zhang
Rapid ethanol production at el ...
Neurospora crassa
Metab. Eng.
31
140-152
2015
-
-
1
-
-
-
-
-
-
-
-
1
-
6
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
725843
Xiong
-
Comparative study on the mutat ...
Saccharomyces cerevisiae
J. Taiwan Inst. Chem. Eng.
44
605-610
2013
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
639098
Bonete
Glucose dehydrogenase from the ...
Haloferax mediterranei, Haloferax mediterranei DSM 1411
FEBS Lett.
383
227-229
1996
-
-
-
-
-
-
1
-
-
-
2
-
-
5
-
-
1
-
-
-
-
1
2
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
1
-
-
-
1
2
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
285763
Uehara
L-Xylose dehydrogenase in bake ...
Saccharomyces cerevisiae
J. Biochem.
52
461-463
1962
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-