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Enzyme Nomenclature
Information on EC 1.1.5.2 - glucose 1-dehydrogenase (PQQ, quinone)
for references in articles please use BRENDA:EC1.1.5.2
Word Map on EC 1.1.5.2
- 1.1.5.2
-
quinoproteins
- acinetobacter
-
electrode
- calcoaceticus
- gluconobacter
-
bioelectrocatalytic
-
fad-linked
- oxydans
- pqqh2
- biotechnology
- diagnostics
- analysis
- medicine
- biofuel production
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.5.2
-
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RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase (PQQ, quinone)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
hexa uni ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
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
-
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
active site structure
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure, putative catalytic mechanism and cycle involving Asp466 and Lys493
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
active site structure
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
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
ping-pong mechanism
-
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene gcd, encoded in the operon pqqABCDEF together with cofactor pyrroloquinoline quinone, PQQ
UniProt
gene gcd, encoded in the operon pqqABCDEF together with cofactor pyrroloquinoline quinone, PQQ
UniProt
-
639190, 639197, 639198, 639200, 639205, 639209, 639214, 639217, 639218, 639219, 639220, 654449, 671165, 685698, 689259, 689260, 724852, 725196, 739873, 740191, 740304, 740321, 740441, 740577, 740933
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
alfalfa plants inoculated with RmH580, a Sinorhizobium meliloti gcd mutant strain show a delay in nodule emergence and a reduced ability for nodulation at various inoculum dosages. Mutant RmH580 strain is also deficient in its competitive ability. In coinoculation experiments a mutant/wild-type inoculum ratio higher than 100:1 is necessary to obtain an equal ratio of nodule occupancy. PQQ-linked GCD is required by Sinorhizobium meliloti for optimal nodulation efficiency and competitiveness on alfalfa roots
physiological function
additional information
physiological function
-
enzymatic analysis of purified mGDH from cells defective in synthesis of ubiquinone and/or menaquinone reveal that quinone-free mGDH has very low levels of activity of glucose dehydrogenase and UQ2 reductase compared with those of ubiquinone-bearing mGDH, both activities are increased by reconstitution with ubuquinone1. mGDH utilizes both menaquinone and ubiquinone as a bound quinine. Bound menaquinone occurs in a fashion similar to that of bound ubiquinone in the mGDH molecule and functions as an electron acceptor from pyrrolo quinoline quinone
physiological function
-
pulse radiolysis analysis reveal that the bound ubiquinone exists very close to pyrroloquinoline quinone at a distance of 11-13 A. Studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH
physiological function
-
multiple genetic loci involved in quinoprotein glucose dehydrogenase activity are required for glucose inhibition of prodigiosin production, including pyrroloquinoline quinone and ubiquinone biosynthetic genes. The enzymatic products of GDH activity are involved in the inhibitory effect. D-Glucono-1,5-lactone and D-gluconic acid, but not D-gluconate, are able to inhibit prodigiosin production. Oxidation of D-glucose by quinoprotein GDH initiates a reduction in pH that inhibits prodigiosin production through transcriptional control of the prodigiosin biosynthetic operon
physiological function
essential role of pqqABCDEF in pyrroloquinoline quinone biosynthesis
physiological function
-
enzymatic analysis of purified mGDH from cells defective in synthesis of ubiquinone and/or menaquinone reveal that quinone-free mGDH has very low levels of activity of glucose dehydrogenase and UQ2 reductase compared with those of ubiquinone-bearing mGDH, both activities are increased by reconstitution with ubuquinone1. mGDH utilizes both menaquinone and ubiquinone as a bound quinine. Bound menaquinone occurs in a fashion similar to that of bound ubiquinone in the mGDH molecule and functions as an electron acceptor from pyrrolo quinoline quinone
-
physiological function
-
essential role of pqqABCDEF in pyrroloquinoline quinone biosynthesis
-
physiological function
-
multiple genetic loci involved in quinoprotein glucose dehydrogenase activity are required for glucose inhibition of prodigiosin production, including pyrroloquinoline quinone and ubiquinone biosynthetic genes. The enzymatic products of GDH activity are involved in the inhibitory effect. D-Glucono-1,5-lactone and D-gluconic acid, but not D-gluconate, are able to inhibit prodigiosin production. Oxidation of D-glucose by quinoprotein GDH initiates a reduction in pH that inhibits prodigiosin production through transcriptional control of the prodigiosin biosynthetic operon
-
additional information
-
the purified recombinant PQQGDH shows thermal stability and substrate specificity as the native enzyme
additional information
-
the purified recombinant PQQGDH shows thermal stability and substrate specificity as the native enzyme
-
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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 + 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
-
-
-
-
?
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-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
-
-
-
-
?
D-fucose + pyrrolquinoline quinone
6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
-
-
-
-
?
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-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 + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + 9,10-phenanthrenequinone
D-glucono-1,5-lactone + ?
-
9,10-phenanthrenequinone shows low effectivity as redox mediator
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
-
physiological electron acceptor in not known
-
-
?
D-glucose + decylubiquinone
D-glucono-1,5-lactone + decylubiquinol
-
-
-
-
?
D-glucose + N-ethylphenazonium ethyl sulfate
D-glucono-1,5-lactone + ?
-
-
-
-
?
D-glucose + N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + ?
-
D-glucose is the preferred substrate
-
-
?
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-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
-
36% activity compared to D-glucose
-
-
?
D-ribose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
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 + ?
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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 + 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
-
-
?
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-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 + 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 + ?
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 + 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 + ?
-
-
-
-
?
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
-
-
654449, 655097, 655127, 655791, 655929, 671165, 725196, 739873, 740191, 740304, 740321, 740441, 740577, 740933, 654864
-
-
?
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-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 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q8ZUN8
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
P13650
-
-
-
?
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
P15877
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
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-
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D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
D4P700
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-
-
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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
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-
-
-
?
additional information
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-
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evolutionary analysis of PQQ-containing proteins, overview
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-
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additional information
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-
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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
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-
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additional information
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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
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-
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additional information
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evolutionary analysis of PQQ-containing proteins, overview
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additional information
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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
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ruthenium(III) bispyridine compounds and ruthenium(III) 4-methyl-bispyridine compounds can act as artificial electron transfer mediator system
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pyrroloquinoline quinone
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each subunit of the dimer contains one molecule of pyrroloquinoline quinone; prosthetic group
pyrroloquinoline quinone
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prosthetic group; type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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prosthetic group; type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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prosthetic group; type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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prosthetic group; type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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prosthetic group; type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
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prosthetic group; Sinorhizobium meliloti is unable to synthesize pyrroloquinoline quinone, synthesis of the holoenzyme in alfalfa nodules
pyrroloquinoline quinone
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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; prosthetic group
pyrroloquinoline quinone
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prosthetic group; 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
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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
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prosthetic group
pyrroloquinoline quinone
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i.e. PQQ, dependent on, functions as a redox mediator by transfer of hydride ions and electrons, redox-related structural changes, overview
pyrroloquinoline quinone
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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
-
prosthetic group
pyrroloquinoline quinone
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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
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i.e. PQQ, dependent on
pyrroloquinoline quinone
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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
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contains one pyrroloquinoline quinone per subunit
pyrroloquinoline quinone
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i.e. 2,7,9,-tricarboxyl-1H-pyrrolo[2,3-f]quinoline-4,5-dione
pyrroloquinoline quinone
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required for catalysis, one molecule per enzyme subunit
pyrroloquinoline quinone
PQQ, essential cofactor for enzyme activity, essential role of pqqABCDEF in PQQ biosynthesis, overview
pyrroloquinoline quinone
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apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
pyrroloquinoline quinone
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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
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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+
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Ca2+ is required for reactivation after thermal inactivation; pyrroloquinoline quinone is bound at the active site via a Ca2+ bridge, enzyme contains 1.95 mol of Ca2+ per mol of subunit
Ca2+
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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+
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apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
Ca2+
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in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Ca2+
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in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Ca2+
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catalytic activity of the membrane-bound enzyme with Ca2+ is very similar to that with Mg2+
Ca2+
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Ca2+ is needed for the correct folding and for the functionalization of pyrroloquinoline quinone as cofactor
Mg2+
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Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
Mg2+
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in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Mg2+
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in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Mg2+
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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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aptameric enzyme subunit
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the aptameric enzyme subunit inhibits PQQGDH in the presence of adenosine
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D-gluconic acid
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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
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substrate inhibition at high concentrations
additional information
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the protein region responsible for complete EDTA tolerance is located between 32% and 59% from the N-terminus, A27 region
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additional information
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poor inhibition of isozyme PQQGDH-B by 5 mM EDTA
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additional information
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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%
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pyrroloquinoline quinone
exogenously added cofector slightly activates the enzyme activity
additional information
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the aptameric enzyme subunit does not activate PQQGDH in the absence of adenosine
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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
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pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
2 - 3
3-O-methyl-D-glucose
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recombinant Arg-tagged enzyme, pH 7.0
22
3-O-methyl-D-glucose
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recombinant chimeric mutant enzyme, pH 7.0
28.7
3-O-methyl-D-glucose
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recombinant wild-type isozyme PQQGDH-B, pH 7.0
41
3-O-methyl-D-glucose
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recombinant wild-type enzyme, pH 7.0, 25°C
53
3-O-methyl-D-glucose
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recombinant tagged enzyme, pH 7.0, 25°C
56
3-O-methyl-D-glucose
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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
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recombinant mutant D167E/N452T, pH 7.0
14
cellobiose
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recombinant wild-type isozyme PQQGDH-B and mutant N452T, pH 7.0
5
D-fucose
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pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
12
D-fucose
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pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
6.8
D-galactose
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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
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pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
0.23
D-glucose
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pH 8.5, reaction with 2,6-dichlorophenolindophenol as electron acceptor
0.47
D-glucose
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pH 6.0, 25°C, reaction with 2,6-dichlorophenolindophenol
2 - 3
D-glucose
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recombinant cytochrome c-fusion protein, pH 7.0
2.4
D-glucose
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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
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pH 8.5, reaction with N-methylphenazonium methyl sulfate or N-ethylphenazonium ethal sulfate as electron acceptor
5.9
D-glucose
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pH 8.5, reaction with Wurster‘ Blue as electron acceptor
7.2
D-glucose
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mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
7.6
D-glucose
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mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
10.6
D-glucose
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mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11
D-glucose
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mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
11.3
D-glucose
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mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
20
D-glucose
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recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25°C
22.6
D-glucose
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mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37°C
27
D-glucose
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recombinant wild-type enzyme and tagged enzyme, pH 7.0, 25°C
41.4
D-glucose
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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
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pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
12
D-xylose
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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
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pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
19
L-arabinose
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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
20
lactose
-
recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0
0.268
N-ethylphenazonium ethyl sulfate
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pH 8.5, reaction with D-xylose
0.278
N-ethylphenazonium ethyl sulfate
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pH 8.5, reaction with D-glucose
0.291
N-ethylphenazonium ethyl sulfate
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pH 8.5, reaction with D-fucose
0.292
N-ethylphenazonium ethyl sulfate
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pH 8.5, reaction with L-arabinose
0.064
N-methylphenazonium methyl sulfate
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pH 8.5, reaction with D-galactose
0.156
N-methylphenazonium methyl sulfate
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pH 8.5, reaction with D-xylose
0.178
N-methylphenazonium methyl sulfate
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pH 8.5, reaction with D-glucose
0.22
N-methylphenazonium methyl sulfate
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pH 8.5, reaction with D-fucose
0.362
N-methylphenazonium methyl sulfate
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pH 8.5, reaction with 2-deoxy-D-glucose
0.4
N-methylphenazonium methyl sulfate
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with D-glucose as cosubstrate, at pH 5.0 and 45°C
0.074
phenazine methosulfate
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membrane-bound enzyme form
0.00012
pyrroloquinoline quinone
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C-terminal periplasmic domain of glucose dehydrogenase
additional information
additional information
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kinetic study, enzyme follows Michaelis-Menten kinetics using artificial electron transfer mediator system based on ruthenium(III) compounds for activity assays
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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
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additional information
additional information
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electrochemical data and kinetics for quinone derivatives as redocx mediators
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additional information
additional information
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predicted binding energy of wild-type and mutant enzymes
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additional information
additional information
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kinetics, cooperativity in the recombinant chimeric mutant enzyme which possesses only 1 active subunit derived from the wild-type enzyme
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additional information
additional information
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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
215
3-O-methyl-D-glucose
-
recombinant mutant D167E/N452T, pH 7.0
3011
3-O-methyl-D-glucose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
121.5
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37°C