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Information on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone) and Organism(s) Acinetobacter calcoaceticus and UniProt Accession P13650
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1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone)IUBMB Comments
Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed propeller structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses.
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Word Map
- 1.1.5.2
-
quinoproteins
-
electrode
- acinetobacter
- calcoaceticus
-
gluconic
-
bioelectrocatalytic
- gluconobacter
- oxydans
- biotechnology
- pqqh2
-
fad-linked
-
lactobionic
- diagnostics
- analysis
- biofuel production
- medicine
The taxonomic range for the selected organisms is: Acinetobacter calcoaceticus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
pqqgdh, quinoprotein glucose dehydrogenase, m-gdh, pqq-gdh, membrane-bound glucose dehydrogenase, pyrroloquinoline quinone-dependent glucose dehydrogenase, pqq-dependent glucose dehydrogenase, soluble glucose dehydrogenase, gdh-b, pqqgdh-b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase
-
-
-
-
dehydrogenase, glucose (pyrroloquinoline-quinone)
-
-
-
-
GDH
glucose dehydrogenase (PQQ dependent)
-
-
-
-
glucose dehydrogenase (pyrroloquinoline-quinone)
-
-
-
-
PQQGDH
pyrroloquinoline quinone glucose dehydrogenase
-
-
quinoprotein D-glucose dehydrogenase
-
-
-
-
quinoprotein glucose dehydrogenase
quinoprotein glucose DH
-
-
-
-
GDH
-
-
-
-
PQQGDH
-
-
-
-
quinoprotein glucose dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
hexa uni ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure from crystal structure, and detailed catalytic mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
catalytic mechanism, His144, Arg228, and Asn229 are involved
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping pong reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
-
-
-
-
oxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glucose:ubiquinone oxidoreductase
Integral membrane protein containing PQQ as prosthetic group. It also contains bound ubiquinone and Mg2+ or Ca2+. Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate. Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed propeller structure. It occurs in a wide range of bacteria. Catalyses a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm. Oxidizes other monosaccharides including the pyranose forms of pentoses.
CAS REGISTRY NUMBER
COMMENTARY
81669-60-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol
2-deoxy-D-glucono-1,5-lactone + ?
-
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
physiological electron acceptor in not known
-
-
?
D-xylose + 2,6-dichlorophenolindolphenol
D-xylono-1,5-lactone + ?
-
-
-
?
2-deoxy-D-glucose + oxidized N-methylphenazonium methyl sulfate
2-deoxy-D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
low activity, recombinant isozyme PQQGDH-B
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
-
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
allose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
cellobiose + pyrroloquinoline quinone
?
-
70% of the activity with D-glucose
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-fucose + N-ethylphenazonium ethyl sulfate
6-deoxy-D-galactono-1,5-lactone + ?
-
-
-
-
?
D-fucose + oxidized N-methylphenazonium methyl sulfate
6-deoxy-D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
-
?
D-galactose + oxidized N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + N-ethylphenazonium ethyl sulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + oxidized N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-mannose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-melibiose + pyrroloquinoline quinone
?
-
10% of the activity with D-glucose
-
-
?
D-xylose + N-ethylphenazonium ethyl sulfate
D-xylono-1,5-lactone + ?
-
-
-
-
?
D-xylose + oxidized N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
L-arabinose + N-ethylphenazonium ethyl sulfate
L-arabino-1,5-lactone + ?
-
-
-
-
?
L-arabinose + oxidized N-methylphenazonium methyl sulfate
L-arabino-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
-
-
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
-
7.5% of the activity with D-glucose
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
best substrate
-
-
?
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
redox-related structural changes, overview
-
-
?
cellobiose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
30% of the activity with D-glucose
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
highest activity
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
20% of the activity with D-glucose
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
35% of the activity with D-glucose
-
-
?
lactose + pyrroloquinoline quinone
?
-
65% of the activity with D-glucose
-
-
?
lactose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
maltose + pyrroloquinoline quinone
?
-
90% of the activity with D-glucose
-
-
?
maltose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
additional information
?
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the oxidation of dissacharides by the enzyme can be considered as an in vitro artefact caused by the removal of the enzyme from its natural environment
-
-
?
additional information
?
-
-
absolute specificity with respect to the C1 position, only sugars are oxidized which have the same configuration of the H/OH substituents at this site as the beta-anomer of glucose. Absolute specificity with respect to the overall conformation of the sugar molecule, sugars with a 4C1 chair conformation are substrates, those with a 1C4 one are not. The nature and configuration of the substituents at the 3-position are hardly relevant for activity, and an equatorial pyranose group at the 4-position exhibits only a specific hindering of the binding of the aldose moiety of a disaccharide
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme
-
-
?
additional information
?
-
-
substrate specificity of the recombinant enzyme produced in Pichia pastoris
-
-
?
additional information
?
-
-
PQQ-GDH has a broad specificity toward the oxidation of aldose sugars (hexoses, pentoses, mono- and disaccharides) into the corresponding lactones and the reduction of artificial electron acceptors
-
-
?
additional information
?
-
-
no activity with D-glucosamine, L-altrose, L-lyxose, L-talose, L-mannose, D-altrose, D-arabinose, L-xylose, L-glucose, L-galactose, D-talose, and L-allose
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + ?
D-glucono-1,5-lactone + ?
physiological electron acceptor in not known
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
additional information
?
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
each subunit of the dimer contains one molecule of pyrroloquinoline quinone
pyrroloquinoline quinone
-
reconstitution of the apoenzyme to full activity is achieved with a stoichiometric amount of pyrroloquinoline quinone. Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
pyrroloquinoline quinone
-
type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
i.e. PQQ, dependent on
pyrroloquinoline quinone
-
i.e. PQQ, dependent on, functions as a redox mediator by transfer of hydride ions and electrons, redox-related structural changes, overview
pyrroloquinoline quinone
-
i.e. PQQ, or 2,7,9-tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione, residues Gln231, Gln246, Ala350, and Leu376 are involved in binding
pyrroloquinoline quinone
-
contains one pyrroloquinoline quinone per subunit
pyrroloquinoline quinone
-
contains one pyrroloquinoline quinone per subunit, pyrroloquinoline quinone (PQQ) is 2,7,9 tricarboxy-1H-pyrrolo [2,3-f]-quinoline-4,5-dione
pyrroloquinoline quinone
-
apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
pyrroloquinoline quinone
-
required for catalysis, one molecule per enzyme subunit
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
Cd2+
-
can replace Ca2+ in reactivation after thermal inactivation
Mg2+
-
Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
Mn2+
-
can replace Ca2+ in reactivation after thermal inactivation
Ca2+
-
required for dimerization of the subunits as well as for functionalization of the bound pyrroloquinoline quinone. Binding of Ca2+ is much stronger in the holoenzyme than in the apoenzyme
Ca2+
-
pyrroloquinoline quinone is bound at the active site via a Ca2+ bridge, enzyme contains 1.95 mol of Ca2+ per mol of subunit
Ca2+
-
Ca2+ is required for reactivation after thermal inactivation
Ca2+
-
apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aptameric enzyme subunit
-
the aptameric enzyme subunit inhibits PQQGDH in the presence of adenosine
-
pyrroloquinoline quinone
-
substrate inhibition at high concentrations
additional information
-
the protein region responsible for complete EDTA tolerance is located between 32% and 59% from the N-terminus, A27 region
-
additional information
-
poor inhibition of isozyme PQQGDH-B by 5 mM EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mag2
-
the PQQGDH aptameric enzyme subunit Mag2 increases activity of the enzyme by 20%
-
additional information
-
the aptameric enzyme subunit does not activate PQQGDH in the absence of adenosine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27.6
3-O-methyl-D-glucose
recombinant mutant N452T, pH 7.0
28.7
3-O-methyl-D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
41
3-O-methyl-D-glucose
recombinant wild-type enzyme, pH 7.0, 25°C
53
3-O-methyl-D-glucose
recombinant tagged enzyme, pH 7.0, 25°C
56
3-O-methyl-D-glucose
recombinant triple mutant enzyme, pH 7.0, 25°C
198
3-O-methyl-D-glucose
recombinant mutant D167E/N452T, pH 7.0
35.5
allose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
14
cellobiose
recombinant wild-type isozyme PQQGDH-B and mutant N452T, pH 7.0
5
D-galactose
recombinant triple mutant enzyme, pH 7.0, 25°C
5.3
D-galactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
20
D-glucose
recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25°C
25
D-glucose
recombinant triple mutant enzyme, pH 7.0, 25°C
25
D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
27
D-glucose
recombinant wild-type enzyme and tagged enzyme, pH 7.0, 25°C
18.9
lactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
22
2-deoxy-D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
2 - 3
3-O-methyl-D-glucose
-
recombinant Arg-tagged enzyme, pH 7.0
22
3-O-methyl-D-glucose
-
recombinant chimeric mutant enzyme, pH 7.0
5
D-fucose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
12
D-fucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
6.8
D-galactose
-
pH 7.0, wild-type enzyme and mutant enzyme E277K
19
D-galactose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
0.23
D-glucose
-
pH 8.5, reaction with 2,6-dichlorophenolindophenol as electron acceptor
2 - 3
D-glucose
-
recombinant cytochrome c-fusion protein, pH 7.0
4
D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate or N-ethylphenazonium ethal sulfate as electron acceptor
5.9
D-glucose
-
pH 8.5, reaction with Wurster Blue as electron acceptor
7
D-xylose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
12
D-xylose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
18
L-arabinose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
19
L-arabinose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
20
lactose
-
recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0
0.268
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-xylose
0.278
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-glucose
0.291
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-fucose
0.292
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with L-arabinose
0.064
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-galactose
0.156
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-xylose
0.178
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-glucose
0.22
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-fucose
0.362
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with 2-deoxy-D-glucose
0.074
phenazine methosulfate
-
membrane-bound enzyme form
additional information
additional information
predicted binding energy of wild-type and mutant enzymes
-
additional information
additional information
-
predicted binding energy of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, cooperativity in the recombinant chimeric mutant enzyme which possesses only 1 active subunit derived from the wild-type enzyme
-
additional information
additional information
-
detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
215
3-O-methyl-D-glucose
recombinant mutant D167E/N452T, pH 7.0
1253
3-O-methyl-D-glucose
recombinant mutant N452T, pH 7.0
3011
3-O-methyl-D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
2509
allose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1355
cellobiose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
232
D-galactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
3860
D-glucose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1659
lactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1930
maltose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1550
D-glucose
-
pH 7.0, temperature not specified in the publication, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1080
cellobiose
-
pH and temperature not specified in the publication
1470
D-allose
-
pH and temperature not specified in the publication
150
D-galactose
-
pH and temperature not specified in the publication
0.24
D-Lyxose
-
pH and temperature not specified in the publication
50
D-mannose
-
pH and temperature not specified in the publication
11
D-ribose
-
pH and temperature not specified in the publication
46
D-xylose
-
pH and temperature not specified in the publication
1450
L-arabinose
-
pH and temperature not specified in the publication
790
lactose
-
pH and temperature not specified in the publication
800
maltose
-
pH and temperature not specified in the publication
11
melibiose
-
pH and temperature not specified in the publication
1700
D-glucose
-
pH and temperature not specified in the publication
2100
D-glucose
-
pH 7.0, temperature not specified in the publication, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
pH-dependence of native and immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
pH 7.5: about 40% of maximal activity, pH 9.5: about 85% of maximal activity, membrane-bound enzyme, reaction with phenazine methosulfate, 2,6-dichlorophenol indophenol and pyrroloquinoline quinone
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6 - 4.7
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
effects of different carbon sources and glucose concentrations on the cell growth and sPQQGDH production, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
there are two types of PQQGDH, the membrane-bound glucose dehydrogenase and the soluble glucose dehydrogenase
-
-
enzyme exists as a soluble form and a membrane-bound form
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
the purified recombinant PQQGDH shows thermal stability and substrate specificity as the native enzyme
physiological function
GDH activity plays a role in the solubilization of mineral phosphorus
physiological function
in some species the enzyme is involved in an additional route in energy transduction, in others it can be a dominating one
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
65000
-
x * 65000, recombinant cytochrome c-fusion protein, SDS-PAGE
83000
50000
-
2 * 50000, deglycosylated recombinant isozyme PQQGDH-B, SDS-PAGE
83000
-
1 * 83000, membrane-bound enzyme form, mainly monomeric in detergent solution
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
homodimer
monomer
-
1 * 83000, membrane-bound enzyme form, mainly monomeric in detergent solution
additional information
dimer
(alpha)2, functional subunit composition, domain and overall structure analysis
dimer
structure analysis, 6-blade beta-propeller protein with each blade consisting of a 4-stranded anti-parallel beta-sheet
dimer
-
2 * 50000, deglycosylated recombinant isozyme PQQGDH-B, SDS-PAGE
dimer
-
apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
additional information
the monomeric enzyme is not active, 3D models of wild-type and mutant enzymes
additional information
-
the monomeric enzyme is not active, 3D models of wild-type and mutant enzymes
additional information
-
redox-related structural changes, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
secreted recombinant isozyme PQQGDH-B expressed in Pichia pastoris
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of enzyme in ternary complex with beta-D-glucose and PQQ
-
ternary complex of the enzyme with pyrroloquinoline quinone and methylhydrazine
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant
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
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
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
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
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
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
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
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
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
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
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
Y171G/E245D/M341V/T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.20 A resolution
additional information
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
additional information
engineering PQQ glucose dehydrogenase with improved substrate specificity
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
35
-
pH 6, 10 min, in absence of Ca2+, stable below, reversible inactivation above
55
55
recombinant tagged wild-type enzyme and mutant enzyme show about 90% remaining activity after 10 min, the nontagged wild-type enzyme shows about 40% remaining activity after 10 min
55
thermal stability of wild-type and mutant isozymes PQQGDH-B, overview
55
-
t1/2: 10 min for wild-type enzyme and mutant enzyme E277K, 4 min for mutant enzymes E277Q and N279H, 25 min for mutant enzyme I278F, less than 2 min for mutant enzymes E277G, E277A, E277D, E277H, E277N, E277V, D275E and D276E
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
optimization of the purification process involving cation exchange chromatography in presence of Zn2+
recombinant isozyme PQQGDH-B from Pichia pastoris culture medium, optimization of down-stream processing
-
recombinant soluble His-tagged enzyme 11.3fold from Escherichia coli strain BL21 (DE3)by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in the periplasm of Escherichia coli strain PP2418, with and without a C-terminal tag of 3 Arg residues
expression of wild-type isozyme PQQGDH-B and mutant enzymes in Escherichia coli
into a His-tagged vector for expression in Escherichia coli JM109
expression of isozyme PQQGDH-B with and without an polyarginine tail in Escherichia coli strain PP2418, and of mutant H168Q
-
expression of isozyme PQQGDH-B, in Pichia pastoris using the alpha-factor signal sequence of Saccharomyces cerevisiae, recombinant enzyme is secreted to the medium, optimization of enzyme production
-
gene gdhB, expression of the enzyme GDH-B as fusion protein C-terminally fused to cytochrome c domain from Comamonas testosteroni in Escherichia coli DH5alpha
-
recombinant high-level production of soluble His-tagged pyrroloquinoline quinone-dependent glucose dehydrogenase in Escherichia coli strain BL21 (DE3), 6fold improvement improvement of sPQQGDH expression in MMBL medium
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
protein dissociation and redimerization of recombinant wild-type and Arg-tagged enzyme, and the mutant H168Q, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
analysis
biotechnology
diagnostics
medicine
-
insertion of a calmodulin domain into enzyme results in a selective Ca2+ biosensor that could be used to rapidly measure Ca2+ concentrations in human biological fluids
biotechnology
engineering PQQ glucose dehydrogenase with improved substrate specificity
biotechnology
enzyme has a great potential for application as glucose sensor constituent
biotechnology
surface charge engineering of the enzyme for optimization of downstream processing in large scale enzyme production
analysis
-
application of mutant enzyme S231K as a glucose sensor constituent. The mutant has more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme and retains catalytic activity similar to the wild-type enzyme
analysis
-
enzyme is used as coupling enzyme for monitoring carbohydrate-transport reactions, the method is particularly suited for determining transport reactions that are not coupled to any form of metabolic energy such as uniport reactions, or for characterizing mutant proteins with a defective energy-coupling mechanism or system with high-affinity constants for sugars
analysis
-
because of its high turnover number, PQQ-GDH is proposed as an enzyme label for the development of sensitive electrochemical enzyme-amplified bioaffinity assays. It has, for example, been applied to the amperometric detection of DNA hybrids or sandwich DNA aptamers at the surface of a carbon electrode
biotechnology
-
engineering of the soluble enzyme GDH-B to enable the electron transfer to the electrode in absence of artificial electron mediator by mimicking the domain structure of the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni, which is composed of a PQQ-containing catalytic domain and a cytochrome c domain
biotechnology
-
optimization of an expression system using Pichia pastoris for use in industrial level production
biotechnology
-
the enzyme is used for glucose biosensor diagnosis
diagnostics
-
enzyme is industrially used as glucose sensor with high catalytic activity and insensitivity to oxygen
diagnostics
-
purified enzyme is immobilized on carbon electrodes modified with 4-ferrocenylphenol, 4-(4-ferrocenylimino-methyl)phenol, or 4-ferrocenylnitrophenol, for use as glucose biosensors, kinetic behaviour during immobilization
diagnostics
-
the enzyme is attractive for application in glucose detection in clinic diagnosis and industrial bioprocess controls
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duine, J.A.; Frank, J.; van Zeeland, J.K.
Glucose dehydrogenase from Acinetobacter calcoaceticus: a quinoprotein
FEBS Lett.
108
443-446
1979
Acinetobacter calcoaceticus
Geiger, O.; Goerisch, H.
Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus
Biochemistry
25
6043-6048
1986
Acinetobacter calcoaceticus
-
Dokter, P.; Frank, J.; Duine, J.A.
Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41
Biochem. J.
239
163-167
1986
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41, Escherichia coli, Gluconobacter oxydans, Klebsiella aerogenes, Pseudomonas sp.
Dokter, P.; Pronk, J.T.; van Schie, B.J.; van Dijken, J.P.; Duine, J.A.
The in vivo and in vitro substrate specificity of quinoprotein glucose dehydrogenase of Acinetobacter calcoaceticus LMD79.41
FEMS Microbiol. Lett.
43
195-200
1987
Acinetobacter calcoaceticus, Pseudomonas sp., Acinetobacter calcoaceticus LMD 79.41
-
Matsushita, K.; Shinagawa, E.; Adachi, O.; Ameyama, M.
Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species
Biochemistry
28
6276-6280
1989
Acinetobacter calcoaceticus
Geiger, O.; Goerisch, H.
Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus
Biochem. J.
261
415-421
1989
Acinetobacter calcoaceticus
Matsushita, K.; Shinagawa, E.; Adachi, O.; Ameyama, M.
Quinoprotein D-glucose dehydrogenase in Acinetobacetr calcoaceticus LMD 79.41: purification and characterization of the membrane-bound enzyme distinct from the soluble enzyme
Antonie van Leeuwenhoek
56
63-72
1989
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
Matsushita, K.; Shinagawa, E.; Inoue, T.; Adachi, O.; Ameyama, M.
Immunological evidence for two types of PQQ-dependent D-glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli
FEMS Microbiol. Lett.
37
141-144
1986
Acetobacter aceti, Gluconobacter oxydans, Acinetobacter calcoaceticus, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa
-
Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Duine, J.A.; Dijkstra, B.W.
The 1.7 A crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat
J. Mol. Biol.
289
319-333
1999
Acinetobacter calcoaceticus (P13650), Acinetobacter calcoaceticus
Yoshida, H.; Kojima, K.; Witarto, A.B.; Sode, K.
Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity
Protein Eng.
12
63-70
1999
Acinetobacter calcoaceticus, Escherichia coli
Olsthoorn, A.J.; Duine, J.A.
On the mechanism and specificity of soluble, quinoprotein glucose dehydrogenase in the oxidation of aldose sugars
Biochemistry
37
13854-13861
1998
Acinetobacter calcoaceticus
Heuberger, E.H.M.L.; Poolman, B.
A spectroscopic assay for the analysis of carbohydrate transport reactions
Eur. J. Biochem.
267
228-234
2000
Acinetobacter calcoaceticus
Igarashi, S.; Ohtera, T.; Yoshida, H.; Witarto, A.B.; Sode, K.
Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values--site-directed mutagenesis studies on the putative active site
Biochem. Biophys. Res. Commun.
264
820-824
1999
Acinetobacter calcoaceticus
Olsthoorn, A.J.J.; Duine, J.A.
Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus
Arch. Biochem. Biophys.
336
42-48
1996
Acinetobacter calcoaceticus
Sode, K.; Ootera, T.; Shirahane, M.; Witarto, A.B.; Igarashi, S.; Yoshida, H.
Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement
Enzyme Microb. Technol.
26
491-496
2000
Acinetobacter calcoaceticus
Dewanti, A.R.; Duine, J.A.
Reconstitution of membrane.integrated quinoprotein glucose dehydrogenase apoenzyme with PQQ and the holoenzymes mechanism of action
Biochemistry
37
6810-6818
1998
Acinetobacter calcoaceticus
Oubrie, A.; Rozeboom, H.J.; Dijkstra, B.W.
Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex
Proc. Natl. Acad. Sci. USA
96
11787-11791
1999
Acinetobacter calcoaceticus
Okuda, J.; Sode, K.
PQQ glucose dehydrogenase with novel electron transfer ability
Biochem. Biophys. Res. Commun.
314
793-797
2004
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD79.41
Oubrie, A.
Structure and mechanism of soluble glucose dehydrogenase and other PQQ-dependent enzymes
Biochim. Biophys. Acta
1647
143-151
2003
Acinetobacter calcoaceticus
Yamada, M.; Elias, M.D.; Matsushita, K.; Migita, C.T.; Adachi, O.
Escherichia coli PQQ-containing quinoprotein glucose dehydrogenase: its structure comparison with other quinoproteins
Biochim. Biophys. Acta
1647
185-192
2003
Escherichia coli, Acinetobacter calcoaceticus (P13650)
Laurinavicius, V.; Razumiene, J.; Kurtinaitiene, B.; Gureviciene, V.; Marcinkeviciene, L.; Bachmatova, I.
Comparative characterization of soluble and membrane-bound PQQ-glucose dehydrogenases
Biologia (Bratisl. )
2
31-34
2003
Acinetobacter calcoaceticus, Erwinia sp., Erwinia sp. 34-1, Acinetobacter calcoaceticus L.M.D. 79.41
-
Igarashi, S.; Hirokawa, T.; Sode, K.
Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase
Biomol. Eng.
21
81-89
2004
Acinetobacter calcoaceticus (P13650)
Koh, H.; Igarashi, S.; Sode, K.
Surface charge engineering of PQQ glucose dehydrogenase for downstream processing
Biotechnol. Lett.
25
1695-1701
2003
Acinetobacter calcoaceticus (P13650)
Tanaka, S.; Igarashi, S.; Ferri, S.; Sode, K.
Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface
BMC Biochem.
6
1
2005
Acinetobacter calcoaceticus (P13650), Acinetobacter calcoaceticus
Yoshida, H.; Araki, N.; Tomisaka, A.; Sode, K.
Secretion of water soluble pyrroloquinoline quinone glucose dehydrogenase by recombinant Pichia pastoris
Enzyme Microb. Technol.
30
312-318
2002
Acinetobacter calcoaceticus
-
Reddy, S.Y.; Bruice, T.C.
Mechanism of glucose oxidation by quinoprotein soluble glucose dehydrogenase: insights from molecular dynamics studies
J. Am. Chem. Soc.
126
2431-2438
2004
Acinetobacter calcoaceticus
Igarashi, S.; Sode, K.
Construction and characterization of heterodimeric soluble quinoprotein glucose dehydrogenase
J. Biochem. Biophys. Methods
61
331-338
2004
Acinetobacter calcoaceticus
Sanchez-Weatherby, J.; Southall, S.; Oubrie, A.
Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding
Acta Crystallogr. Sect. F
62
518-521
2006
Acinetobacter calcoaceticus, Escherichia coli, Streptomyces coelicolor
Hamamatsu, N.; Suzumura, A.; Nomiya, Y.; Sato, M.; Aita, T.; Nakajima, M.; Husimi, Y.; Shibanaka, Y.
Modified substrate specificity of pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with optimized amino acid substitution
Appl. Microbiol. Biotechnol.
73
607-617
2006
Acinetobacter calcoaceticus (P13650)
Lau, C.; Borgmann, S.; Maciejewska, M.; Ngounou, B.; Gruendler, P.; Schuhmann, W.
Improved specificity of reagentless amperometric PQQ-sGDH glucose biosensors by using indirectly heated electrodes
Biosens. Bioelectron.
22
3014-3020
2007
Acinetobacter calcoaceticus
Ikebukuro, K.; Morita, Y.; Yoshida, W.; Sode, K.
Construction of target molecule sensing system using aptameric enzyme subunit based on PQQGDH activity
Nucleic Acids Symp. Ser.
51
401-402
2007
Acinetobacter calcoaceticus
Ikebukuro, K.; Takase, M.; Sode, K.
Selection of DNA aptamers that inhibit enzymatic activity of PQQGDH and its application
Nucleic Acids Symp. Ser.
51
403-404
2007
Acinetobacter calcoaceticus
Yu, Y.; Wei, P.; Zhu, X.; Huang, L.; Cai, J.; Xu, Z.
High-level production of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase in Escherichia coli
Eng. Life Sci.
12
574-582
2012
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus L.M.D. 79.41
-
Durand, F.; Limoges, B.; Mano, N.; Mavre, F.; Miranda-Castro, R.; Saveant, J.M.
Effect of substrate inhibition and cooperativity on the electrochemical responses of glucose dehydrogenase. Kinetic characterization of wild and mutant types
J. Am. Chem. Soc.
133
12801-12809
2011
Acinetobacter calcoaceticus
Stredansky, M.; Monosik, R.; Mastihuba, V.; Sturdik, E.
Monitoring of PQQ-dependent glucose dehydrogenase substrate specificity for its potential use in biocatalysis and bioanalysis
Appl. Biochem. Biotechnol.
171
1032-1041
2013
Acinetobacter calcoaceticus
Scherbahn, V.; Putze, M.T.; Dietzel, B.; Heinlein, T.; Schneider, J.J.; Lisdat, F.
Biofuel cells based on direct enzyme-electrode contacts using PQQ-dependent glucose dehydrogenase/bilirubin oxidase and modified carbon nanotube materials
Biosens. Bioelectron.
61
631-638
2014
Acinetobacter calcoaceticus
Guo, Z.; Johnston, W.A.; Stein, V.; Kalimuthu, P.; Perez-Alcala, S.; Bernhardt, P.V.; Alexandrov, K.
Engineering PQQ-glucose dehydrogenase into an allosteric electrochemical Ca(2+) sensor
Chem. Commun. (Camb.)
52
485-488
2016
Acinetobacter calcoaceticus
Babanova, S.; Matanovic, I.; Atanassov, P.
Quinone-modified surfaces for enhanced enzyme-electrode interactions in pyrroloquinoline-quinone-dependent glucose dehydrogenase anodes
ChemElectroChem
1
2017-2028
2014
Acinetobacter calcoaceticus
-
Duine, J.A.; Strampraad, M.J.; Hagen, W.R.; de Vries, S.
The cooperativity effect in the reaction of soluble quinoprotein (PQQ-containing) glucose dehydrogenase is not due to subunit interaction but to substrate-assisted catalysis
FEBS J.
283
3604-3612
2016
Acinetobacter calcoaceticus
Guo, Z.; Murphy, L.; Stein, V.; Johnston, W.A.; Alcala-Perez, S.; Alexandrov, K.
Engineered PQQ-glucose dehydrogenase as a universal biosensor platform
J. Am. Chem. Soc.
138
10108-10111
2016
Acinetobacter calcoaceticus
Nakashima, Y.; Mizoshita, N.; Tanaka, H.; Nakaoki, Y.
Amphiphilic polymer mediators promoting electron transfer on bioanodes with PQQ-dependent glucose dehydrogenase
Langmuir
32
12986-12994
2016
Acinetobacter calcoaceticus
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