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Information on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone)
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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
- analysis
- diagnostics
- biofuel production
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase
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-
-
-
dehydrogenase, glucose (pyrroloquinoline-quinone)
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-
-
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EC 1.1.99.17
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-
formerly
-
GCD
GDH
GDH-B
GDHm
GlcDH
glucose dehydrogenase
glucose dehydrogenase (PQQ dependent)
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-
-
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glucose dehydrogenase (pyrroloquinoline-quinone)
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-
-
-
m-GDH
membrane-bound 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
PqqC
PQQGDH
PQQGDH-B
pyrroloquinoline quinone dependent glucose dehydrogenase
pyrroloquinoline quinone glucose dehydrogenase
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-
pyrroloquinoline quinone-dependent glucose dehydrogenase
QGDH
quinone-dependent glucose dehydrogenase
quinoprotein aldose sugar dehydrogenase
quinoprotein D-glucose dehydrogenase
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-
-
-
quinoprotein glucose dehydrogenase
quinoprotein glucose DH
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-
-
-
s-GDH
sGDH
Tt_ASD
GDH
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-
-
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PQQGDH
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-
-
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pyrroloquinoline quinone-dependent glucose dehydrogenase
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quinoprotein glucose dehydrogenase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure
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 contains a loop 6BC region which does not directly interact with the substrates
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure from crystal structure, and detailed catalytic mechanism
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure, putative catalytic mechanism and cycle involving Asp466 and Lys493
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
catalytic mechanism, His144, Arg228, and Asn229 are involved
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping pong reaction mechanism
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping-pong mechanism
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D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
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reduction
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-
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oxidation
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-
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
81669-60-5
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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-amino-D-glucose + pyrroloquinoline quinone
2-amino-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol
2-deoxy-D-glucono-1,5-lactone + ?
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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 + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
3-deoxy-D-glucose + pyrroloquinoline quinone
3-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
6-deoxy-D-glucose + pyrroloquinoline quinone
6-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
cellobiose + pyrroloquinoline quinone
?
-
70% of the activity with D-glucose
-
-
?
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-cellobiose + 2,6-dichloroindophenol
D-cellobiono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-cellobiose + phenazine methosulfate
D-cellobiono-1,5-lactone + reduced phenazine methosulfate
D-fructose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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
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-
-
-
?
D-fucose + pyrrolquinoline quinone
6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
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-
-
-
?
D-galactose + 2,6-dichloroindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-galactose + oxidized N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-galactose + phenazine methosulfate
D-galactono-1,5-lactone + reduced phenazine methosulfate
D-glucosamino-1,5-lactone + reduced phenazine methosulfate
D-glucosamine + reduced phenazine methosulfate
-
-
-
?
D-glucose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichloroindophenol
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + 9,10-phenanthrenequinone
D-glucono-1,5-lactone + ?
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9,10-phenanthrenequinone shows low effectivity as redox mediator
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
physiological electron acceptor in not known
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-
?
D-glucose + decylubiquinone
D-glucono-1,5-lactone + decylubiquinol
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-
-
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?
D-glucose + N-ethylphenazonium ethyl sulfate
D-glucono-1,5-lactone + ?
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-
-
-
?
D-glucose + N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + ?
-
D-glucose is the preferred substrate
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-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-glucose + oxidized N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ubiquinol Q1
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ubiquinol Q2
-
-
-
-
?
D-glucose 6-phosphate + phenazine methosulfate
6-phospho-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
D-maltose + 2,6-dichlorophenolindophenol
D-maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-mannose + 2,6-dichloroindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-mannose + 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
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36% activity compared to D-glucose
-
-
?
D-mannose + phenazine methosulfate
D-mannono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-ribose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-ribose + phenazine methosulfate
D-ribono-1,4-lactone + reduced phenazine methosulfate
-
-
-
?
D-ribose + pyrroloquinoline quinone
D-ribono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-xylose + 2,6-dichlorophenolindolphenol
D-xylono-1,5-lactone + ?
-
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
86% activity compared to D-glucose
-
-
?
D-xylose + N-ethylphenazonium ethyl sulfate
D-xylono-1,5-lactone + ?
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-
-
-
?
D-xylose + N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + ?
-
22% activity compared to D-glucose
-
-
?
D-xylose + oxidized N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
-
-
-
?
D-xylose + phenazine methosulfate
D-xylono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
-
-
?
L-arabinose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
97% activity compared to D-glucose
-
-
?
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 + phenazine methosulfate
D-arabinono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
maltose + 2,6-dichloroindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + N-methylphenazonium methyl sulfate
maltono-1,5-lactone + ?
-
17% activity compared to D-glucose
-
-
?
maltose + phenazine methosulfate
D-maltono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
maltotriose + phenazine methosulfate
D-maltotriono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
3% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
3% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
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
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
low activity
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
96% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
96% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
3-methyl-alpha-methyl-D-glucopyranose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
20% activity compared to D-glucose
-
-
?
3-methyl-alpha-methyl-D-glucopyranose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
20% activity compared to D-glucose
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
-
-
-
-
?
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 + 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
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
-
-
-
?
allose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
alpha-D-lactose + phenazine methosulfate
alpha-D-lactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
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-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
85% activity compared to D-glucose
-
-
?
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
85% activity compared to D-glucose
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
D-arabinono-1,5-lactone + ?
-
8.0% activity compared to D-glucose
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
D-arabinono-1,5-lactone + ?
-
8.0% activity compared to D-glucose
-
-
?
D-cellobiose + phenazine methosulfate
D-cellobiono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-cellobiose + phenazine methosulfate
D-cellobiono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
-
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
71% activity compared to D-glucose
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + ?
-
20% activity compared to D-glucose
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + ?
-
20% activity compared to D-glucose
-
-
?
D-galactose + phenazine methosulfate
D-galactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-galactose + phenazine methosulfate
D-galactono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
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 + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
30% of the activity with D-glucose
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
-
6.5% 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-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
low activity, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
86% activity compared to D-glucose
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
-
86% activity compared to D-glucose
-
-
?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
2,3-dichloro-1,4-naphthoquinone shows low effectivity as redox mediator
-
-
?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
-
2,3-dichloro-1,4-naphthoquinone shows low effectivity as redox mediator
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
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 + ?
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
best substrate
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
100% activity
-
-
?
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
r
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
-
-
-
-
r
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
D-glucose is the preferred substrate
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
D-glucose is the preferred substrate
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + oxidized 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + reduced phenazine methosulfate
-
-
-
?
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 + 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 + 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
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
enzyme donates electrons directly to ubiquinone in the respiratory chain
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
linked to the respiratory chain of a wide variety of bacteria
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
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
-
-
-
?
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
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-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
a pivotal PQQ-containing quinoprotein coupled to the respiratory chain in the periplasmic oxidation of alcohols and sugars
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
best substrate, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
with ubiquinone-8 as minor compound, PQQ acts in electron transfer between enzyme and ubiquinone
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
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
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone + ubiquinol Q9
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
91% activity compared to D-glucose
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
91% activity compared to D-glucose
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
-
8.6% of the activity with D-glucose
-
-
?
D-mannose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-melibiose + pyrroloquinoline quinone
?
-
10% of the activity with D-glucose
-
-
?
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
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
20% of the activity with D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
-
13% of the activity with D-glucose
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
40% activity compared to D-glucose
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
-
40% activity compared to 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
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
35% 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
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
-
2.8% of the activity with D-glucose
-
-
?
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
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
-
no activity
-
-
?
lactose + pyrroloquinoline quinone
?
-
65% 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 + pyrroloquinoline quinone
?
-
5% of the activity with D-glucose
-
-
?
maltose + pyrroloquinoline quinone
?
-
3.2% of the activity with D-glucose
-
-
?
maltose + ubiquinone
? + ubiquinol
-
recombinant isozyme PQQGDH-B
-
-
?
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
?
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
?
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
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme
-
-
?
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
?
-
-
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
-
-
?
additional information
?
-
-
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
-
-
?
additional information
?
-
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
?
additional information
?
-
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
?
additional information
?
-
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
?
additional information
?
-
-
the membrane-bound enzyme donates electrons directly to ubiquinone during the oxidation of D-glucose, and these electrons are subsequently transferred to ubiquinol oxidase in the respiratory chain
-
-
?
additional information
?
-
-
the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane
-
-
?
additional information
?
-
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview
-
-
?
additional information
?
-
substrate specificity of recombinant wild-type and mutant enzymes
-
-
?
additional information
?
-
-
substrate specificity of recombinant wild-type and mutant enzymes
-
-
?
additional information
?
-
-
substrate specificity of the enzyme in presence or absence of different recombinant peptide ligands, overview
-
-
?
additional information
?
-
-
less than 8% activity with D-mannitol, D-sorbitol, D-trehalose, D-arabinose, D-glucose 6-phosphate, methal-alpha-D-glucopyranose, D-mannose, sucrose, D-maltose, and D-lactose. No activity with gluconic acid and D-fructose
-
-
?
additional information
?
-
-
less than 8% activity with D-mannitol, D-sorbitol, D-trehalose, D-arabinose, D-glucose 6-phosphate, methal-alpha-D-glucopyranose, D-mannose, sucrose, D-maltose, and D-lactose. No activity with gluconic acid and D-fructose
-
-
?
additional information
?
-
-
the enzyme catalyzes only oxidation of D-aldoses and aldose derivatives
-
-
?
additional information
?
-
-
activity of the enzyme is regulated by both the glucose dehydrogenase apo-enzyme synthesis and the synthesis of the cofactor pyrroloquinoline quinone
-
-
?
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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
beta-D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
physiological electron acceptor in not known
-
-
?
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 + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
enzyme donates electrons directly to ubiquinone in the respiratory chain
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
linked to the respiratory chain of a wide variety of bacteria
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
-
-
-
?
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
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
a pivotal PQQ-containing quinoprotein coupled to the respiratory chain in the periplasmic oxidation of alcohols and sugars
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
-
-
?
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
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
additional information
?
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
-
the membrane-bound enzyme donates electrons directly to ubiquinone during the oxidation of D-glucose, and these electrons are subsequently transferred to ubiquinol oxidase in the respiratory chain
-
-
?
additional information
?
-
-
the enzyme has a ubiquinone reacting site close to the periplasmic side of the membrane and thus its electron transfer to ubiquinone appears to be incapable of forming a proton electrochemical gradient across the inner membrane
-
-
?
additional information
?
-
-
evolutionary analysis of PQQ-containing proteins, overview
-
-
?
additional information
?
-
-
activity of the enzyme is regulated by both the glucose dehydrogenase apo-enzyme synthesis and the synthesis of the cofactor pyrroloquinoline quinone
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ruthenium(III) bispyridine compounds and ruthenium(III) 4-methyl-bispyridine compounds can act as artificial electron transfer mediator system
-
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
during the processing of pyrroloquinoline quinone into the apoenzyme to give active enzyme, its affinity is markedly dependent on the pH, four groups with pK values between pH 7 and pH 8 are involved
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 I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
Sinorhizobium meliloti is unable to synthesize pyrroloquinoline quinone, synthesis of the holoenzyme in alfalfa nodules
pyrroloquinoline quinone
-
the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+
pyrroloquinoline quinone
-
i.e. PQQ, dependent on
pyrroloquinoline quinone
-
i.e. PQQ, dependent on exogenous PQQ, since Escherichia coli does not synthesize PQQ itself
pyrroloquinoline quinone
i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity
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
-
i.e. 2,7,9,-tricarboxyl-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
-
i.e. 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid, prosthetic group, not covalently linked to the polypeptide chain or posttranslationally derived from precursor amino acid residues in the active site of the constituent. enzyme. Biosynthesis of the cofactor in Klebsiella pneumoniae is facilitated by six genes, pqqABCDEF. PqqC is one of two metal free oxidases of known structure and catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid, overview
pyrroloquinoline quinone
PQQ, essential cofactor for enzyme activity, essential role of pqqABCDEF in PQQ biosynthesis, overview
pyrroloquinoline quinone
-
required for catalysis, one molecule per enzyme subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
can replace Ca2+ in reactivation after thermal inactivation
Mg2+
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+
Ca2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Ca2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Ca2+
-
catalytic activity of the membrane-bound enzyme with Ca2+ is very similar to that with Mg2+
Ca2+
-
Ca2+ is needed for the correct folding and for the functionalization of pyrroloquinoline quinone as cofactor
Mg2+
-
Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
Mg2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Mg2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Mg2+
-
the apoenzyme is converted to the holoenzyme with exogenous pyrroloquinoline quinone and Mg2+. The holoenzyme gradually returns to the apoenzyme in absence of pyrroloquinoline quinone and/or Mg2+. Mg2+ allows the cofactor to take a more appropriate position in the active site
Mg2+
required, bound at the active site, cannot be substituted by Ca2+, Sr2+, or Ba2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aptameric enzyme subunit
-
the aptameric enzyme subunit inhibits PQQGDH in the presence of adenosine
-
D-gluconic acid
-
non-competitive inhibitor to D-glucose and competitive inhibitor to N-methylphenazonium methyl sulfate
Mg2+
competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D
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
-
additional information
-
purified enzyme is inactivated upon removal of detergent by acetone treatment. The detergent-depleted enzyme is partially activated by Triton X-100
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mag2
-
the PQQGDH aptameric enzyme subunit Mag2 increases activity of the enzyme by 20%
-
pyrroloquinoline quinone
exogenously added cofector slightly activates the enzyme activity
additional information
-
the aptameric enzyme subunit does not activate PQQGDH in the absence of adenosine
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acrodynia
gdhB, a gene encoding a second quinoprotein glucose dehydrogenase in Pantoea citrea, is required for pink disease of pineapple.
Diabetes Mellitus
Is type 2 diabetes due to a deficiency of FAD-linked glycerophosphate dehydrogenase in pancreatic islets?
Diabetes Mellitus, Type 2
FAD-glycerophosphate dehydrogenase activity in lymphocytes of type-2 diabetic patients and their relatives.
Diabetes Mellitus, Type 2
Is type 2 diabetes due to a deficiency of FAD-linked glycerophosphate dehydrogenase in pancreatic islets?
Diabetes Mellitus, Type 2
Mitochondrial FAD-glycerophosphate dehydrogenase and G-protein-coupled inwardly rectifying K+ channel: No evidence for linkage in maturity-onset diabetes of the young or NIDDM.
Diabetes Mellitus, Type 2
Ontogeny of FAD-linked glycerophosphate dehydrogenase in rat pancreatic islets.
Diabetes, Gestational
Low mitochondrial glycerophosphate dehydrogenase activity in lymphocytes of women with gestational diabetes.
Galactosemias
Erroneous glucose recordings while using mutant variant of quinoprotein glucose dehydrogenase glucometer in a child with galactosemia.
glucose 1-dehydrogenase (pqq, quinone) deficiency
Is type 2 diabetes due to a deficiency of FAD-linked glycerophosphate dehydrogenase in pancreatic islets?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
2-deoxy-D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
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
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
79
3-O-methyl-D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 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-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
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
6.8
D-galactose
-
pH 7.0, wild-type enzyme and mutant enzyme E277K
17.5
D-galactose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
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
0.47
D-glucose
-
pH 6.0, 25°C, reaction with 2,6-dichlorophenolindophenol
2 - 3
D-glucose
-
recombinant cytochrome c-fusion protein, pH 7.0
2.4
D-glucose
-
wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
2.8
D-glucose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
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 Wursterâ Blue as electron acceptor
7.2
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
7.6
D-glucose
-
mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
10.6
D-glucose
-
mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11
D-glucose
-
mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11.3
D-glucose
-
mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
16
D-glucose
recombinant mutant T416V/T417V, pH 7.0, 25°C
20
D-glucose
recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25°C
22.6
D-glucose
-
mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37°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
41.4
D-glucose
-
mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
116
D-mannose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
166
D-ribose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
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
17
D-xylose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
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
31
L-arabinose
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C
18.9
lactose
recombinant wild-type isozyme PQQGDH-B, pH 7.0
20
lactose
-
recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0
36
lactose
recombinant triple mutant enzyme, pH 7.0, 25°C
13
maltose
recombinant triple mutant enzyme, pH 7.0, 25°C
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
0.4
N-methylphenazonium methyl sulfate
-
with D-glucose as cosubstrate, at pH 5.0 and 45°C
0.074
phenazine methosulfate
-
membrane-bound enzyme form
0.00012
pyrroloquinoline quinone
-
C-terminal periplasmic domain of glucose dehydrogenase
0.0001
ubiquinone
-
Km below 0.0002 mM, native enzyme, at pH 7.5 and 28°C
additional information
additional information
-
electrochemical data and kinetics for quinone derivatives as redocx mediators
-
additional information
additional information
-
kinetic study, enzyme follows Michaelis-Menten kinetics using artificial electron transfer mediator system based on ruthenium(III) compounds for activity assays
-
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
metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview
-
additional information
additional information
-
metal binding kinetics, wild-type and mutant enzymes, Km for the different substrates of mutant enzymes with different metal ions bound, overview
-
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
-
detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE