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.

Reaction

D-glucose
+
NAD(P)+
=
D-glucono-1,5-lactone
+
NAD(P)H
+
H+

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, D-glucose dehydrogenase (NAD(P)), EC 1.1.5.2, GDH, gdh-2, general stress protein 74, GlcDH, GlcDH-I, GlcDH-II, GlcDH-IWG3, glucose 1-dehydrogenase, glucose 1-dehydrogenase 3, glucose 1-dehydrogenase III, glucose 1-dehydrogenase IV, glucose dehydrogenase, glucose1-dehydrogenase, GSP74, hexose phosphate dehydrogenase, hexose-6-phosphate dehydrogenase, LsGDH, More, NAD(P)-dependent glucose-1-dehydrogenase, NAD-GDH, nicotinamide adenine dinucleotide (NAD)-linked glucose dehydrogenase, SsGDH, SSO3204

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.47 glucose 1-dehydrogenase [NAD(P)+]

Engineering

Engineering on EC 1.1.1.47 - glucose 1-dehydrogenase [NAD(P)+]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E170K
-
decrease in melting temperature by 7.1 degrees
E170K/K252L
-
increase in melting temperature by 5.6 degrees
F155Y
-
increase in melting temperature by 1.9 degrees
K252L
-
increase in melting temperature by 8.9 degrees
K252Q
-
decrease in melting temperature by 2.7 degrees
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
E96K
-
mutation increases thermostability by about 15°C at pH 6.5
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/A258G
-
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
Q252L/E170K
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
-
mutant enzyme has higher stability at 60°C and 56% remaining activity compared to the wild type enzyme
-
Q252L/A258G
-
mutant enzyme has higher stability at 60°C and 61% remaining activity compared to the wild type enzyme
-
Y253C
-
mutant enzyme has higher stability at 60°C and 1% remaining activity compared to the wild type enzyme
-
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
E170K
-
increase in melting temperature by 25.9 degrees
E170R
-
increase in half-life at 65°C
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
K204E
-
no catalytic activity
K234D
-
no catalytic 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
-
increase in melting temperature by 17.3 degrees
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
Q31G
-
no catalytic 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
V227A
-
slight increase in half-life at 25°C
W230F
-
no catalytic acitivity
G28A
-
slight decrease in half-life at 25°C, decrease in specific activity
-
K204E
-
no catalytic activity
-
P105S
-
slight increase in half-life at 25°C, decrease in specific activity
-
Q252L
-
increase in melting temperature by 17.3 degrees
-
Q252L/E170K
-
strong increase in half-life at 65°C, about 50% increase in specific activity
-
E170K
-
increase in melting temperature by 18.5 degrees
F155Y
-
increase in melting temperature by 4.5 degrees
L252Q
-
decrease in melting temperature by 19.3 degrees
T41A
-
reduced activity
T41V
-
reduced activity