Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A71P/N454S
mutant, relative activity vs wild type, substrate glucose 0.95, substrate maltose 0.75
A98G/K126R/L445I/N454S
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
D167A
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167C
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167E
site-directed mutagenesis, substrate binding residue mutation, slightly reduced activity compared to the wild-type enzyme
D167E/N452T
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D167G
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167H
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167K
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167N
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Q
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167R
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167S
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167V
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167W
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Y
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D276E
-
drastic decrease in EDTA tolerance
E277A
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277D
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277G
-
drastic decrease in EDTA tolerance
E277H
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277K
-
decreased Km value for glucose and altered substrate specificity, significantly increased catalytic efficiency compared with the wild-type enzyme
E277N
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277Q
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277V
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
G100R
mutant, relative activity vs wild type, substrate glucose 0.35, substrate maltose 0.26
G100W/G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.55, substrate maltose 0.20
G320E
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.70
G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.25
G320F/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.48, substrate maltose 0.17
G320Y/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.49, substrate maltose 0.16
H168C
site-directed mutagenesis, catalytic residue mutation, highly reduced activity compared to the wild-type enzyme
K166E
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166G
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166I
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K3E/E278G/G392C
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.53
L194F/A376T
mutant, relative activity vs wild type, substrate glucose 0.39, substrate maltose 0.075
L194F/G320E/M367P
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.14
L194F/G320E/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.36, substrate maltose 0.051
L194F/G320F
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.060
L194Q
mutant, relative activity vs wild type, substrate glucose 0.22, substrate maltose 0.15
M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.65, substrate maltose 0.24
N275E
-
drastic decrease in EDTA tolerance
N340F/Y418F
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
N340F/Y418I
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
N428C
-
site-directed mutagenesis, at relatively high concentrations of mediator and substrate, catalysis by the mutant type may be more efficient than with the wild-type
N452T
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
N454S
mutant, relative activity vs wild type, substrate glucose 0.87, substrate maltose 0.69
Q169E
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q169K
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q193H
mutant, relative activity vs wild type, substrate glucose 0.41, substrate maltose 0.23
Q193S/G320E
mutant, relative activity vs wild type, substrate glucose 0.56, substrate maltose 0.19
Q209R/N240R/T389R
site-directed mutagenesis, increased thermal stability compared to the wild-type enzyme
S231C
-
increase in thermal stability
S231D
-
increase in thermal stability
S231H
-
increase in thermal stability
S231K
-
more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme, retains catalytic activity similar to the wild-type enzyme
S231L
-
increase in thermal stability
S231M
-
increase in thermal stability
S231N
-
increase in thermal stability
T348G
-
mutant crystallized by microseeding, data set is collected at 2.36 A resolution
T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.15 A resolution
T416V/T417V
site-directed mutagenesis, mutation of resides of the hydrophobic region, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme
V157I/M367V/T463S
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
V91A/W372R
mutant, relative activity vs wild type, substrate glucose 0.44, substrate maltose 0.22
Y171G/E245D/M341V/T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.20 A resolution
Y248F/N342D/A376T/A418V
mutant, relative activity vs wild type, substrate glucose 0.74, substrate maltose 0.43
Y302H
mutant, relative activity vs wild type, substrate glucose 0.47, substrate maltose 0.35
D354N/N355D
site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D448N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D456N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D457N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D730A
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730N
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730R
-
reduced affnity for pyrroloquinoline quinone
E217Q
-
the mutant retains its function similar to that of wild type GDH
E742G/P757L
-
slightly higher Km value for Mg2+
G689D
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
G776A
-
the mutant retains its function similar to that of wild type GDH
H262A
-
reduced affinity both for glucose, 11fold, and pyrroloquinoline quinone, 8fold, without significant effect on glucose oxidase activity
H262Y
-
greatly diminished catalytic efficiency for all substrates, rate of electron transfer to oxygen is unaffected, 230fold increased Km value for glucose
H775A
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone
H775R
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone, 230fold higher Km than wild-type enzyme
N355D
site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
N452D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452I
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452T
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B
N462D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462Y
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
S145C
-
site-directed mutagenesis, introduction of a Cys residue in each monomer of the enzyme leads to formation of an intersubunit disulfide bridge at the dimer interface resulting in 30fold increased thermal stability at 55°C compared to the wild-type enzyme
S357L
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
W404A
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low glucose oxidase activity and phenazine methosulfate reductase activity compared with wild-type enzyme
W404F
-
pronounced reduction of affinity for pyrroloquinoline quinone, very weak activity of phenazine methosulfate reductase but still retains glucose oxidase activity equivalent to that of the wild-type
D354N
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
-
D466E
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
D466N
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
K493A
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
K493R
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
-
Q126E
-
the mutant shows 25.6% relative activity on maltose
Q126R
-
the mutant shows 11.4% relative activity on maltose
Q126S
-
the mutant shows 12.4% relative activity on maltose
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
Q219K/F220C
-
the mutant shows 20% relative activity on maltose
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
Q219N/F220K
-
the mutant shows 11.7% relative activity on maltose
Q126E
-
the mutant shows 25.6% relative activity on maltose
-
Q126R
-
the mutant shows 11.4% relative activity on maltose
-
Q126S
-
the mutant shows 12.4% relative activity on maltose
-
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
-
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
-
Y156A
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
Y156K
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
Y156A
-
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
-
Y156K
-
impaired activities and affinities for all substrates and completely loses the activity for alcohols. The catalytic efficiency of the Y156A mutant is lower than that of the Y156K mutant for most substrates
-
G320D/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.51, substrate maltose 0.16
G320D/M367P/A376T
mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.24
H168Q
site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant
H168Q
-
site-directed mutagenesis, inactive mutant, a heterodimeric chimeric enzyme consisiting of 1 wild-type subunit and 1 mutant subunit shows decreased activity and a substrate specificity similar to the wild-type enzyme
D354N
site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D354N
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
D466E
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme
D466E
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
D466N
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone
D466N
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
K493A
-
very low glucose oxidase activity, without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493A
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
K493R
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493R
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
engineering PQQ glucose dehydrogenase with improved substrate specificity
additional information
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
additional information
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
-
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
-
construction of a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region and production of a linked-dimeric enzyme, the linked-dimeric enzyme shows higher thermal stability than native dimeric enzyme
additional information
-
co-expression of peptide ligands in a random phage diplay modifies the substrate specificity of the enzyme towards mono- and disaccharides, overview
additional information
-
studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH
additional information
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
additional information
-
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
additional information
-
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
-
additional information
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
additional information
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
-