1.1.1.47: glucose 1-dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glucose 1-dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.47
Reaction
Synonyms
alkali-resistant glucose 1-dehydrogenase, beta-D-glucose:NAD(P)+ 1-oxido-reductase, beta-D-glucose:NAD(P)+ 1-oxidoreductase, BmGlcDH-III, BmGlcDH-IV, bzgdh, D-glucose dehydrogenase (NAD(P)), EC 1.1.5.2, GDH, gdh-2, GDHB, general stress protein 74, GlcDH, GlcDH-I, GlcDH-II, GlcDH-IWG3, glucose 1-dehydrogenase, glucose 1-dehydrogenase 3, glucose 1-dehydrogenase B, glucose 1-dehydrogenase III, glucose 1-dehydrogenase IV, glucose dehydrogenase, glucose1-dehydrogenase, GluDH, GSP74, hexose phosphate dehydrogenase, hexose-6-phosphate dehydrogenase, LsGDH, More, NAD(P)-dependent glucose 1-dehydrogenase, NAD(P)-dependent glucose dehydrogenase, NAD(P)-dependent glucose-1-dehydrogenase, NAD-GDH, nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase, SsGDH, SSO3204
ECTree
1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]Advanced search results
results (
results (Engineering
Engineering on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A11L
-
slight decrease in half-life at 25°C, decrease in specific activity
A246V
-
slight decrease in half-life at 25°C, decrease in specific activity
F155Y
-
slight increase in half-life at 25°C, almost 100% increase in specific activity
G114E
-
slight increase in half-life at 25°C, decrease in specific activity
G28A
-
slight decrease in half-life at 25°C, decrease in specific activity
I12V
-
slight decrease in half-life at 25°C, 4fold decrease in specific activity
I186V
-
slight increase in half-life at 25°C, decrease in specific activity
I75M
-
slight decrease in half-life at 25°C, decrease in specific activity
I90V
-
half-life at 25°C similar to wild-type, decrease in specific activity
K107E
-
slight decrease in half-life at 25°C, decrease in specific activity
M23I
-
slight increase in half-life at 25°C, decrease in specific activity
M89L
-
slight decrease in half-life at 25°C, slight increase in specific activity
N46A
-
slight increase in half-life at 25°C, decrease in specific activity
P105S
-
slight increase in half-life at 25°C, decrease in specific activity
P45A
-
slight increase in half-life at 25°C, 40% increase in specific activity
P45A/F155Y/E170K/V227A/Q252L
-
strong increase in half-life at 65°C, about 50% increase in specific activity
P45A/F155Y/E170R/V227A/W230F/Q252L
-
strong increase in half-life at 65°C, about 40% increase in specific activity
P45A/F155Y/V227A
-
strong increase in half-life at 25°C, 50% increase in specific activity
P45A/N46E/F155Y/E170K/V227A/W230F/Q252L
-
strong increase in half-life at 65°C, about 50% increase in specific activity
P45A/N46E/F155Y/V227A
-
strong increase in half-life at 25°C, decrease in specific activity
P45A/N46E/F155Y/V227A/W230F
-
increase in half-life at 65°C
P45A/V227A
-
strong increase in half-life at 25°C, decrease in specific activity
Q252L/E170K
-
strong increase in half-life at 65°C, about 50% increase in specific activity
Q252L/E170R
-
strong increase in half-life at 65°C, about 50% increase in specific activity
Q43E
-
half-life at 25°C similar to wild-type, slight increase in specific activity
V140I
-
slight decrease in half-life at 25°C, decrease in specific activity
G28A
-
slight decrease in half-life at 25°C, decrease in specific activity
-
P105S
-
slight increase in half-life at 25°C, decrease in specific activity
-
Q252L/E170K
-
strong increase in half-life at 65°C, about 50% increase in specific activity
-
DS255
A258F
Km (D-glucose) increased at pH 6 compared to wild-type, decreased at pH 8 compared to wild-type. Mutant shows higher substrate specificity with D-xylose, D-mannose, D-galactose and D-glucosamine compared to wild-type. Mutant shows a markedly deteriorated thermostability
DELTAG261
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type.Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Mutant shows a markedly deteriorated thermostability
E170K
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
E96A
E96G
E96K/D108N/P194Q/E210K
mutant enzyme has higher stability at 60°C and 97% remaining activity compared to the wild type enzyme
E96K/V112A/E133K/Y217H
mutant enzyme has higher stability at 60°C and 85% remaining activity compared to the wild type enzyme
E96K/V183I
mutant enzyme has higher stability at 60°C and 72% remaining activity compared to the wild type enzyme
G259A
Km (D-glucose) increased at pH 6 and pH 8 compared to wild-type. Specific activity of the G259A mutant is slightly lower, but is still comparable with wild-type BmGlcDH-IV. Thermostability comparable to wild-type
G259V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261A
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
G261V
Km (D-glucose) highly increased at pH 6 and pH 8 compared to wild-type. Specific activity of mutant for D-glucose is severely decreased at both pH 6.0 and pH 8.0. Thermostability comparable to wild-type
Q252L
Q252L/A258G
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K
Q252L/E170K/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/K137R
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I
kinetic parameters of the mutant enzyme are determined
Q252L/E170K/S100P/K166R/V72I/K137R
the mutant enzyme exhibits a 9.2fold increase in tolerance against 10% (v/v) 1-phenylethanol and is more stable than mutant enzyme Q252L/E170K (BmGDHM0) when exposed to hydrophobic and enzyme-inactivating compounds such as acetophenone, ethyl 2-oxo-4-phenylbutyrate, and ethyl (R)-2-hydroxy-4-phenylbutyrate
Y253C
E170K
Priestia megaterium IGW3
-
mutant is unstable at an alkaline pH (26% residual activity at pH 10-10.5), dissociates into dimers at an alkaline pH
-
Q252L
Priestia megaterium IGW3
-
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
-
Q252L/E170K
Priestia megaterium IGW3
-
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
-
E96A
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
-
E96G
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
-
Q252L
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
-
Q252L/A258G
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
-
Q252L/E170K/K166R
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Q252L/E170K/S100P/K166R/V72I
Priestia megaterium IWG3
-
kinetic parameters of the mutant enzyme are determined
-
Y253C
Priestia megaterium IWG3
-
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
-
I192T
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
I192T/V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 3fold lower than the kcat/Km-value of the wild-type enzyme
I192T/V306I
mutant enzyme shows 10fold higher activity with 1-phenethyl-1,4-dihydropyridine-3-carboxamide compared with the wild-type enzyme. Using this engineered variant in combination with an enoate reductase from Thermus scotoductus results in an enzyme-coupled regeneration process for biomimetic cofactor without ribonucleotide or ribonucleotide analogue and full conversion of 10 mM 2-methylbut-2-enal with 1-phenethyl-1,4-dihydropyridine-3-carboxamide as cofactor
V306G
kcat/Km-values of the mutant enzyme for the biomimetic cofactors are slightly higher than the kcat/Km-values of wild-type enzyme. The kcat/Km-value for NAD+ is about 2fold lower than the kcat/Km-value of the wild-type enzyme
V306I
kcat/Km-values of the mutant enzyme for NAD+ and the biomimetic cofactors are lower than the kcat/Km-values of wild-type enzyme
DS255
the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme
DS255
-
the mutant displays significantly enhanced thermal stability with considerable soluble expression and high specific activity. It is extremely stable at pH ranging from 4.5 to 10.5, as it retains nearly 100% activity after incubating at different buffers for 1 h. The mutant also exhibits high thermostability, having a half-life of 9900 min at 50°C, which is 1868fold as that of the wild type enzyme
-
E96A
mutant enzyme has higher stability at 60°C and 90% remaining activity compared to the wild type enzyme
E96G
mutant enzyme has higher stability at 60°C and 47% remaining activity compared to the wild type enzyme
Q252L
-
natural mutant strain IWG3, Leu252 increases enzyme stability, slightly increased activity compared to the wild-type enzyme
Q252L
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
Q252L
mutant is inactivated at pH values above 9, dissociates into dimers at an alkaline pH
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
Q252L/E170K
mutant exhibits increased pH stability (95% residual activity at pH 8-10.5) in the absence of NaCl
Q252L/E170K
kinetic parameters of the mutant enzyme are determined
Y253C
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
