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1.1.5.2: glucose 1-dehydrogenase (PQQ, quinone)

This is an abbreviated version!
For detailed information about glucose 1-dehydrogenase (PQQ, quinone), go to the full flat file.

Word Map on EC 1.1.5.2

Reaction

D-glucose
+
ubiquinone
=
D-glucono-1,5-lactone
 +
ubiquinol

Synonyms

(PQQ)GDH, aldose sugar dehydrogenase, Asd, beta-D-glucose:(acceptor) 1-oxidoreductase, D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase, dehydrogenase, glucose (pyrroloquinoline-quinone), EC 1.1.99.17, GCD, GDH, GDH-B, GDH1, GdhA, GDHm, GlcDH, glucose dehydrogenase, glucose dehydrogenase (PQQ dependent), glucose dehydrogenase (pyrroloquinoline-quinone), glucose dehydrogenase Amano 5, m-GDH, membrane glucose dehydrogenase, membrane-bound glucose dehydrogenase, membrane-bound PQQ-dependent glucose dehydrogenase, mGDH, PQQ GDH, PQQ glucose dehydrogenase, PQQ-dependent GDH, PQQ-dependent glucose dehydrogenase, PQQ-dependent mGDH, PQQ-dependent soluble glucose dehydrogenase, PQQ-GDH, PQQ-glucose dehydrogenase, PQQ-linked GCD, PQQ-sGDH, PqqC, PQQGDH, PQQGDH-B, pyrroloquinoline quinone dependent glucose dehydrogenase, pyrroloquinoline quinone glucose dehydrogenase, pyrroloquinoline quinone-dependent glucose dehydrogenase, QGDH, quinone-dependent glucose dehydrogenase, quinoprotein aldose sugar dehydrogenase, quinoprotein D-glucose dehydrogenase, quinoprotein glucose dehydrogenase, quinoprotein glucose DH, s-GDH, sGDH, sGDH-PQQ, soluble glucose dehydrogenase, soluble PQQ-dependent glucose dehydrogenase, soluble quinoprotein (PQQ-containing) glucose dehydrogenase, Tt_ASD, water-soluble PQQ glucose dehydrogenase, water-soluble pyrroquinoline quinone glucose dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.5 With a quinone or similar compound as acceptor
                1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone)

Engineering

Engineering on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
G320D/M367P/A376T
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
H168Q
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
D204A
-
no GDH activity
D354N
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
D466E
D466N
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
E217A
-
no GDH activity
E217L
-
no GDH activity
E217Q
-
the mutant retains its function similar to that of wild type GDH
E591K
-
no GDH activity
E591L
-
no GDH activity
E591Q
-
no GDH activity
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
G776D
-
no GDH activity
G776K
-
no GDH activity
G776L
-
no GDH activity
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
K493A
K493R
L712R
-
no GDH activity
L712W
-
no GDH activity
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
R201A
-
no GDH activity
R266E
-
no GDH activity
R266Q
-
no GDH activity
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
-
additional information