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1.1.3.4: glucose oxidase

This is an abbreviated version!
For detailed information about glucose oxidase, go to the full flat file.

Word Map on EC 1.1.3.4

Reaction

beta-D-glucose
+
O2
=
D-glucono-1,5-lactone
+
H2O2

Synonyms

AldO, beta-D-glucose oxidase, beta-D-glucose oxygen-1-oxidoreductase, beta-D-glucose/oxygen 1-oxidoreductase, beta-D-glucose: oxygen 1-oxidoreductase, beta-D-glucose:O2 1-oxidoreductase, beta-D-glucose:O2-1-oxidoreductase, beta-D-glucose:oxygen 1-oxido-reductase, beta-D-glucose:oxygen 1-oxidoreductase, beta-D-glucose:oxygen oxidoreductase, beta-D-glucose:oxygen-1-oxidoreductase, beta-D-glucose:quinone oxidoreductase, CngoxA, corylophyline, D-glucose oxidase, D-glucose-1-oxidase, deoxin-1, glucose aerodehydrogenase, glucose oxyhydrase, glucose-1-oxidase, GO-2, GOD, GOX, GOxP5, microcid, More, notatin, oxidase, glucose, pen-GOx, penatin, yGOXpenag

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.4 glucose oxidase

Engineering

Engineering on EC 1.1.3.4 - glucose oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A173T/A332S
increased electron transfer (1.2fold)
A173T/F414L
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
A173V/A332S/F414I/V560T
increased electron transfer (6.4fold), decrease in O2 sensitivity
A332S/V560T
increased electron transfer (1.2fold), 70% decrease in O2 sensitivity
A449C
-
site-directed mutagenesis, the mutation results in almost completely diminished activity compared to the wild-type enzyme
E84C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
F414Y
increased electron transfer
H172K
site-directed mutagenesis, mutant H172K shows increased thermosensitivity compared to the wild-type enzyme
H172K/H220D
site-directed mutagenesis, mutant H172K/H220D does not show significant differences in thermal stability but about 70% increased initial activity compared to the wild-type enzyme
H220D
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
H447C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
H447K
I94V/T30S
increased O2 sensitivity, increased electron transfer (1.9fold)
L500D
site-directed mutagenesis, inactive mutant
L569E
N2Y/K13E/T30V/I94V/K152R
site-directed mutagenesis of mutant M12, pH optimum and sugar specificity of M12 mutant of GOx is similar to the wild-type enzyme, while thermostability is slightly decreased. Mutant M12 GOx expressed in Pichia pastoris shows three times higher activity compared to wild-type GOx towards redox mediators like N,N-dimethyl-nitroso-aniline used for glucose strips manufacturing. Mutant M12 GOx remains very specific for glucose but has higher activity for galactose compared to wild-type GOx
Q124R/L569E
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
Q345K
Q469K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q469K/L500D
Q90R
site-directed mutagenesis, the mutant shows increased sensitivity to thermal denaturation, with R1 and R2 values 60% and 80% lower than wild-type enzyme respectively
Q90R/Y509E
Q90R/Y509E/T554M
the triple mutant is a glucose oxidase with high stability
S307C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
T110A
the mutant enzyme displays 12.3fold reduced O2 consumption
T110S
increased electron transfer
T110S/T34V
increased electron transfer
T110S/V20Y
increased O2 sensitivity
T30S/I94V
T30V/I94V/A162T
2.9fold increase in kcat/Km, decrease in t1/2(60°C) by 1.5°C
T30V/I94V/A162T/R537K/M556V
4.0fol2.6fold increase in kcat/Km, increase in t1/2(60°C) by 5.25°C
T554M
random mutagenesis, the mutation generates a sulfur-pi interaction, the mutant shows 60% reduced activity and 40% increased thermal stability compared to the wild-type enzyme
T56V/T132S
T56V/T132S/C521S
-
site-directed mutagenesis, the mutant shows improved catalytic efficiency, mutation C521S does not alter enzyme activity, but the attachment of AuNPs to the native free thiol is prevented
V20Y
increased electron transfer
Y435C
-
site-directed mutagenesis, the mutation does not affect enzyme activity. Attachment of gold nanoparticles to the purified proteins leads to an immediate and dramatic decrease in activity
Y509E
site-directed mutagenesis, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
H220D
-
site-directed mutagenesis, mutant H220D shows increased thermosensitivity and reduced activity compared to the wild-type enzyme
-
Q124R/L569E
-
site-directed mutagenesis, the mutation has no significant effect on stability but causes a twofold increase of the enzyme's specific activity
-
Q90R/Y509E
-
site-directed mutagenesis, the mutation does not cause a significant change in the thermal stability of the enzyme, but causes increased enzyme activity compared to the wild-type enzyme
-
T554M
-
random mutagenesis, the mutation generates a sulfur-pi interaction, the mutant shows 60% reduced activity and 40% increased thermal stability compared to the wild-type enzyme
-
Y169C/A211C
F418A
12.6fold increase in apparent Km value
G423D
H520A
the enzyme variant is almost completely inactive
H520V
the enzyme variant is almost completely inactive
H563A
the enzyme variant is completely inactive
H563V
the enzyme variant is completely inactive
K19E
-
site-directed mutagenesis
K23E
-
site-directed mutagenesis
K260E.
-
site-directed mutagenesis
K424E
K424I
-
site-directed mutagenesis, the mutation does not significantly affect the enzyme activity
K48/50E
-
site-directed mutagenesis
Q184E
-
site-directed mutagenesis
Q75E
-
site-directed mutagenesis
R516K
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
R516Q
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
S114A/F355L
increased electron transfer, 88% decrease in O2 sensitivity
V464A/K424E
2.4fold increase in electron transfer, 95% decrease in O2 sensitivity
V564S
1.1fold increase in electron transfer, 88% decrease in O2 sensitivity
F418A
-
12.6fold increase in apparent Km value
-
H520A
-
the enzyme variant is almost completely inactive
-
R516K
-
the mutant enzyme whose side chain forms only one hydrogen bond with the 3-OH group of beta-D-glucose, exhibits an 80fold higher apparent Km (513 mM) but a Vmax only 70% lower than the wild type
-
R516Q
-
the complete elimination of a hydrogen-bond interaction between residue 516 and the 3-OH group of beta-D-glucose through the substitution R516Q effects a 120fold increase in the apparent Km for glucose (to 733 mM) and a decrease in the Vmax to 1/30
-
additional information