Application | Comment | Organism |
---|---|---|
analysis | usage for quantitative determination of glucose in clinical tests and in the food industry | Priestia megaterium |
diagnostics | usage for quantitative determination of glucose in clinical tests and in the food industry | Priestia megaterium |
synthesis | usage as NADP+ cofactor regenerator for enzymatic synthesis of chiral compounds such as ethyl-(S)-4-chloro-3-hydroxybutanoate and ethyl 4-chloro-3-oxobutanoate | Priestia megaterium |
Cloned (Comment) | Organism |
---|---|
DNA sequence determination and analysis, expression in Escherichia coli strain JM109 | Bacillus subtilis |
DNA sequence determination and analysis, expression in Escherichia coli strain JM109 | Priestia megaterium |
DNA sequence determination and analysis, expression in Escherichia coli strain JM109 | Bacillus licheniformis |
Protein Variants | Comment | Organism |
---|---|---|
Q252L | natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme | Priestia megaterium |
Q252L/E170K | site-directed mutagenesis of the mutant strain IWG3, the mutant is insensitive against NaCl concentration and pH value, slightly increased activity compared to the wild-type enzyme | Priestia megaterium |
General Stability | Organism |
---|---|
NaCl stabilizes the enzyme at alkline pH and elevated temperatures | Priestia megaterium |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
8 | - |
beta-D-glucose | mutant Q252L, pH 8.0, 25°C | Priestia megaterium | |
8.5 | - |
beta-D-glucose | mutant Q252L/E170K, pH 8.0, 25°C | Priestia megaterium | |
14 | - |
beta-D-glucose | wild-type enzyme, pH 8.0, 25°C | Priestia megaterium |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
NaCl | stabilizes the enzyme at alkline pH and elevated temperatures | Priestia megaterium |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28200 | - |
4 * 28200 | Priestia megaterium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
IFO 12200 | - |
Bacillus subtilis | - |
IFO 13719 | - |
Priestia megaterium | - |
mutant strain IWG3, wild-type strain IFO 15308 | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli | Bacillus subtilis |
recombinant enzyme from Escherichia coli | Bacillus licheniformis |
recombinant wild-type and mutant enzymes from Escherichia coli | Priestia megaterium |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-D-glucose + NAD(P)+ | best substrate, wild-type and mutant enzymes | Priestia megaterium | D-glucono-1,5-lactone + NAD(P)H + H+ | - |
? | |
beta-D-glucose + NAD+ | - |
Bacillus subtilis | D-glucono-1,5-lactone + NADH + H+ | - |
? | |
beta-D-glucose + NAD+ | - |
Bacillus licheniformis | D-glucono-1,5-lactone + NADH + H+ | - |
? | |
D-fructose + NAD(P)+ | no activity with mutants Q252L and Q252L/E170K | Priestia megaterium | ? + NAD(P)H | - |
? | |
D-galactose + NAD(P)+ | low activity with wild-type and mutant enzymes | Priestia megaterium | D-galactono-1,5-lactone + NAD(P)H | - |
? | |
D-maltose + NAD(P)+ | no activity with mutants Q252L and Q252L/E170K | Priestia megaterium | ? + NAD(P)H | - |
? | |
D-mannose + NAD(P)+ | wild-type and mutant enzymes | Priestia megaterium | ? + NAD(P)H | - |
? | |
D-xylose + NAD(P)+ | wild-type and mutant enzymes | Priestia megaterium | D-xylono-1,5-lactone + NAD(P)H + H+ | - |
? | |
additional information | no activity of wild-type and mutant enzymes with sucrose | Priestia megaterium | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | reversible dissociation in to inactive monomers at alkaline pH | Priestia megaterium |
tetramer | 4 * 28200 | Priestia megaterium |
Synonyms | Comment | Organism |
---|---|---|
GlcDH | - |
Bacillus subtilis |
GlcDH | - |
Priestia megaterium |
GlcDH | - |
Bacillus licheniformis |
glucose dehydrogenase | - |
Bacillus subtilis |
glucose dehydrogenase | - |
Priestia megaterium |
glucose dehydrogenase | - |
Bacillus licheniformis |
More | enzyme belongs to the family of short-chain dehydrogenases/reductases | Bacillus subtilis |
More | enzyme belongs to the family of short-chain dehydrogenases/reductases | Priestia megaterium |
More | enzyme belongs to the family of short-chain dehydrogenases/reductases | Bacillus licheniformis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus subtilis |
25 | - |
assay at | Priestia megaterium |
25 | - |
assay at | Bacillus licheniformis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermostability is highly increased by addition of NaCl | Priestia megaterium |
66 | - |
half-life: mutant Q252L 1.3 min, mutant Q252L/E170K 540 min | Priestia megaterium |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
317 | - |
beta-D-glucose | mutant Q252L, pH 8.0, 25°C | Priestia megaterium | |
334 | - |
beta-D-glucose | mutant Q252L/E170K, pH 8.0, 25°C | Priestia megaterium | |
395 | - |
beta-D-glucose | wild-type enzyme, pH 8.0, 25°C | Priestia megaterium |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bacillus subtilis |
8 | - |
assay at | Priestia megaterium |
8 | - |
assay at | Bacillus licheniformis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
sharp drop in activity at alkaline pH of wild-type and mutant Q252L activities, not mutant Q252L/E170K | Priestia megaterium |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Bacillus subtilis | |
NAD+ | - |
Priestia megaterium | |
NAD+ | - |
Bacillus licheniformis | |
NADP+ | - |
Priestia megaterium |