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

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
1.1.5.2
-
RECOMMENDED NAME
GeneOntology No.
glucose 1-dehydrogenase (PQQ, quinone)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
hexa uni ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
ping-pong mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
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
show the reaction diagram
catalytic mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
active site structure from crystal structure, and detailed catalytic mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
active site structure
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
active site structure, putative catalytic mechanism and cycle involving Asp466 and Lys493
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
active site structure
P15877
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
catalytic mechanism, His144, Arg228, and Asn229 are involved
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
ping pong reaction mechanism
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
ping-pong mechanism
Acinetobacter calcoaceticus LMD 79.41
-
-
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
glucose and glucose-1-phosphate degradation
-
glucose degradation (oxidative)
-
L-ascorbate biosynthesis VI (engineered pathway)
-
Metabolic pathways
-
Pentose phosphate pathway
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldose sugar dehydrogenase
-
-
beta-D-glucose:(acceptor) 1-oxidoreductase
-
-
D-glucose:(pyrroloquinoline-quinone) 1-oxidoreductase
-
-
-
-
dehydrogenase, glucose (pyrroloquinoline-quinone)
-
-
-
-
EC 1.1.99.17
-
-
formerly
-
GDH
-
-
-
-
GDH
Erwinia sp. 34-1
-
-
-
GDH
P15877
-
GDH-B
Acinetobacter calcoaceticus LMD79.41
-
-
-
glucose dehydrogenase
-
-
glucose dehydrogenase
P13650
-
glucose dehydrogenase
-
-
glucose dehydrogenase
-
-
glucose dehydrogenase
Escherichia coli YU423
-
-
-
glucose dehydrogenase (PQQ dependent)
-
-
-
-
glucose dehydrogenase (pyrroloquinoline-quinone)
-
-
-
-
glucose dehydrogenase Amano 5
-
-
m-GDH
-
-
m-GDH
Erwinia sp. 34-1
-
-
-
membrane glucose dehydrogenase
P15877
-
membrane-bound glucose dehydrogenase
-
-
membrane-bound glucose dehydrogenase
Escherichia coli YU423
-
-
-
membrane-bound PQQ-dependent glucose dehydrogenase
-
-
mGDH
Escherichia coli YU423
-
-
-
mGDH
D4P700
-
mGDH
Pantoea ananatis SC17(0)
D4P700
-
-
PQQ glucose dehydrogenase
-
-
PQQ glucose dehydrogenase
P13650
-
PQQ glucose dehydrogenase
Acinetobacter calcoaceticus LMD79.41
-
-
-
PQQ-dependent GDH
-
-
PQQ-dependent GDH
-
-
PQQ-dependent glucose dehydrogenase
-
-
PQQ-dependent glucose dehydrogenase
-
-
PQQ-dependent glucose dehydrogenase
Erwinia sp. 34-1
-
-
-
PQQ-dependent glucose dehydrogenase
D4P700
-
PQQ-dependent glucose dehydrogenase
Pantoea ananatis SC17(0)
D4P700
-
-
PQQ-dependent mGDH
D4P700
-
PQQ-dependent mGDH
Pantoea ananatis SC17(0)
D4P700
-
-
PQQ-dependent soluble glucose dehydrogenase
-
-
PQQ-GDH
Acinetobacter calcoaceticus L.M.D.
-
-
-
PQQ-GDH
-
-
PQQ-GDH
Erwinia sp. 34-1
-
-
-
PQQ-glucose dehydrogenase
-
-
PQQ-glucose dehydrogenase
Acinetobacter calcoaceticus L.M.D.
-
-
-
PQQ-glucose dehydrogenase
-
-
PQQ-glucose dehydrogenase
Erwinia sp. 34-1
-
-
-
PQQ-linked GCD
Q92RB3
-
PQQGDH
-
-
-
-
PQQGDH
Acinetobacter calcoaceticus L.M.D. 79.41
-
-
-
pyrroloquinoline quinone dependent glucose dehydrogenase
-
-
pyrroloquinoline quinone dependent glucose dehydrogenase
-
-
-
pyrroloquinoline quinone glucose dehydrogenase
-
-
pyrroloquinoline quinone-dependent glucose dehydrogenase
-
-
pyrroloquinoline quinone-dependent glucose dehydrogenase
Acinetobacter calcoaceticus L.M.D. 79.41
-
-
-
QGDH
Serratia marcescens CMS2526
-
-
-
quinone-dependent glucose dehydrogenase
D4P700
-
quinone-dependent glucose dehydrogenase
Pantoea ananatis SC17(0)
D4P700
-
-
quinoprotein aldose sugar dehydrogenase
Q8ZUN8
-
quinoprotein D-glucose dehydrogenase
-
-
-
-
quinoprotein glucose dehydrogenase
-
-
-
-
quinoprotein glucose dehydrogenase
-
-
quinoprotein glucose dehydrogenase
P13650
-
quinoprotein glucose dehydrogenase
-
-
quinoprotein glucose dehydrogenase
-
-
quinoprotein glucose dehydrogenase
Serratia marcescens CMS2526
-
-
-
quinoprotein glucose dehydrogenase
-
-
quinoprotein glucose DH
-
-
-
-
s-GDH
Acinetobacter calcoaceticus L.M.D.
-
-
-
soluble glucose dehydrogenase
-
-
water-soluble PQQ glucose dehydrogenase
-
-
water-soluble pyrroquinoline quinone glucose dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
81669-60-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
2 enzyme forms, a soluble and a membrane-bound one
-
-
Manually annotated by BRENDA team
2 isozymes PQQGDH-A and PQQGDH-B
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
isozyme PQQGDH-B
SwissProt
Manually annotated by BRENDA team
isozyme PQQGDH-B
-
-
Manually annotated by BRENDA team
LMD 70.9 and LMD 79.39
-
-
Manually annotated by BRENDA team
LMD 79.41; type II enzyme
-
-
Manually annotated by BRENDA team
soluble enzyme form sGDH
-
-
Manually annotated by BRENDA team
strain L.M.D. 79.41, enzyme s-GDH
-
-
Manually annotated by BRENDA team
strain LMD79.41
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus L.M.D.
strain L.M.D. 79.41, enzyme s-GDH
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus L.M.D. 79.41
-
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus LMD 79.41
LMD 79.41
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus LMD79.41
strain LMD79.41
-
-
Manually annotated by BRENDA team
type I enzyme
-
-
Manually annotated by BRENDA team
strain 34-1
-
-
Manually annotated by BRENDA team
strain 34-1, m-GDH
-
-
Manually annotated by BRENDA team
Erwinia sp. 34-1
strain 34-1
-
-
Manually annotated by BRENDA team
Erwinia sp. 34-1
strain 34-1, m-GDH
-
-
Manually annotated by BRENDA team
; strain YU423
-
-
Manually annotated by BRENDA team
isozyme PQQGDH-B
-
-
Manually annotated by BRENDA team
type I enzyme
-
-
Manually annotated by BRENDA team
Escherichia coli YU423
strain YU423
-
-
Manually annotated by BRENDA team
gene gox0265 or mgdh
-
-
Manually annotated by BRENDA team
type II enzyme
-
-
Manually annotated by BRENDA team
gene gcd, encoded in the operon pqqABCDEF together with cofactor pyrroloquinoline quinone, PQQ
UniProt
Manually annotated by BRENDA team
Pantoea ananatis SC17(0)
gene gcd, encoded in the operon pqqABCDEF together with cofactor pyrroloquinoline quinone, PQQ
UniProt
Manually annotated by BRENDA team
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa P4
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
strain ATCC 13525
-
-
Manually annotated by BRENDA team
type I enzyme
-
-
Manually annotated by BRENDA team
gene gdhS
-
-
Manually annotated by BRENDA team
Serratia marcescens CMS2526
gene gdhS
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
D4P700
essential role of pqqABCDEF in pyrroloquinoline quinone biosynthesis
physiological function
Escherichia coli YU423
-
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
Pantoea ananatis SC17(0)
-
essential role of pqqABCDEF in pyrroloquinoline quinone biosynthesis
-
physiological function
Serratia marcescens CMS2526
-
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
-
malfunction
Q92RB3
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
additional information
-
the purified recombinant PQQGDH shows thermal stability and substrate specificity as the native enzyme
additional information
Acinetobacter calcoaceticus L.M.D. 79.41
-
the purified recombinant PQQGDH shows thermal stability and substrate specificity as the native enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-amino-D-glucose + pyrroloquinoline quinone
2-amino-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol
2-deoxy-D-glucono-1,5-lactone + ?
show the reaction diagram
P13650
-
-
-
?
2-deoxy-D-glucose + 2,6-dichlorophenolindophenol
2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
3% activity compared to D-glucose
-
-
?
2-deoxy-D-glucose + oxidized N-methylphenazonium methyl sulfate
2-deoxy-D-glucono-1,5-lactone + ruduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + pyrroloquinoline quinone
2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
low activity
-
-
?
2-deoxy-D-glucose + ubiquinone
2-deoxy-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
low activity, recombinant isozyme PQQGDH-B
-
-
?
3-deoxy-D-glucose + pyrroloquinoline quinone
3-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
show the reaction diagram
P13650
-
-
-
?
3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
3-O-methyl-D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
3-O-methyl-D-glucose + pyrroloquinoline quinone
3-O-methyl-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
3-O-methyl-D-glucose + ubiquinone
3-O-methyl-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
6-deoxy-D-glucose + pyrroloquinoline quinone
6-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
allose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
P13650
-
-
-
?
allose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
-
-
-
-
?
allose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
allose + ubiquinone
? + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
beta-D-glucose + ubiquinone
beta-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-, redox-related structural changes, overview
-
-
?
cellobiose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
P13650
-
-
-
?
cellobiose + pyrroloquinoline quinone
?
show the reaction diagram
-
70% of the activity with D-glucose
-
-
?
cellobiose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
cellobiose + ubiquinone
? + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
cellobiose + ubiquinone
? + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus L.M.D.
-
-
-
-
?
D-allose + 2,6-dichlorophenolindophenol
D-allono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
85% activity compared to D-glucose
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-allose + pyrroloquinoline quinone
D-allono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-allose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
D-cellobiose + 2,6-dichloroindophenol
D-cellobiono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-fructose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-fucose + N-ethylphenazonium ethyl sulfate
6-deoxy-D-galactono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-fucose + oxidized N-methylphenazonium methyl sulfate
6-deoxy-D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
D-fucose + pyrrolquinoline quinone
6-deoxy-D-galactono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-fucose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
D-galactose + 2,6-dichloroindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
show the reaction diagram
P13650
-
-
-
?
D-galactose + 2,6-dichlorophenolindolphenol
D-galactono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-galactose + 2,6-dichlorophenolindophenol
D-galactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
71% activity compared to D-glucose
-
-
?
D-galactose + oxidized N-methylphenazonium methyl sulfate
D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
6.5% of the activity with D-glucose
-
-
?
D-galactose + pyrroloquinoline quinone
D-galactono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
30% of the activity with D-glucose
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
-
low activity, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
D-galactose + ubiquinone
D-galactono-1,5-lactone + ubiquinol
show the reaction diagram
Erwinia sp. 34-1, Acinetobacter calcoaceticus L.M.D.
-
-
-
-
?
D-galactose + ubiquinone
?
show the reaction diagram
P13650
-
-
-
?
D-glucose + 1,4-naphthoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
Erwinia sp., Erwinia sp. 34-1
-
-
-
-
?
D-glucose + 2,3-dichloro-1,4-naphthoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
Erwinia sp., Erwinia sp. 34-1
-
2,3-dichloro-1,4-naphthoquinone shows low effectivity as redox mediator
-
-
?
D-glucose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichloroindophenol
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenol-indophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
show the reaction diagram
P13650
best substrate
-
-
?
D-glucose + 2,6-dichlorophenolindolphenol
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus LMD79.41
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
100% activity
-
-
?
D-glucose + 2-methyl-6-methoxy-1,4-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
Erwinia sp., Erwinia sp. 34-1
-
-
-
-
?
D-glucose + 4-(4-ferrocenylimino-methyl)phenol
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus L.M.D.
-
-
-
-
?
D-glucose + 4-ferrocenylnitrophenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 4-ferrocenylphenol
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + 9,10-phenanthrenequinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
9,10-phenanthrenequinone shows low effectivity as redox mediator
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
show the reaction diagram
-
physiological electron acceptor in not known
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
show the reaction diagram
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
show the reaction diagram
-
-
-
-
?
D-glucose + ferricyanide
D-glucono-1,5-lactone + ferrocyanide
show the reaction diagram
-
-
-
-
?
D-glucose + N-ethylphenazonium ethyl sulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + oxidized N-methylphenazonium methyl sulfate
D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
-
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + phenazine methosulfate
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
-
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
enzyme donates electrons directly to ubiquinone in the respiratory chain
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
linked to the respiratory chain of a wide variety of bacteria
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Escherichia coli YU423
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + trimethyl-1,4-benzoquinone
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P13650
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
D4P700
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P13650
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
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
show the reaction diagram
P15877
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
best substrate, recombinant wild-type and mutant isozymes PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
with ubiquinone-8 as minor compound, PQQ acts in electron transfer between enzyme and ubiquinone
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
D4P700
assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Erwinia sp. 34-1
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Erwinia sp. 34-1
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus LMD79.41
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Serratia marcescens CMS2526
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus L.M.D.
-
best substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus L.M.D. 79.41
-
preferred substrate, preferred substrate, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Pantoea ananatis SC17(0)
D4P700
-, assayed with the electron acceptors phenazine methosulfate and dichlorphenolindophenol
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q1
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q2
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
D-glucose + ubiquinone Q4
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
-
D-glucose + ubiquinone Q4
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q6
D-glucono-1,5-lactone + ?
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone +
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone Q9
D-glucono-1,5-lactone +
show the reaction diagram
-
-
-
-
?
D-lactose + 2,6-dichlorophenolindophenol
D-lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
91% activity compared to D-glucose
-
-
?
D-maltose + 2,6-dichlorophenolindophenol
D-maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
71% activity compared to D-glucose
-
-
?
D-maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
D-mannose + 2,6-dichloroindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-mannose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
P13650
-
-
-
?
D-mannose + 2,6-dichlorophenolindophenol
D-mannono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
36% activity compared to D-glucose
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
no activity
-
-
-
D-mannose + pyrroloquinoline quinone
D-mannono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
8.6% of the activity with D-glucose
-
-
?
D-mannose + ubiquinone
? + ubiquinol
show the reaction diagram
P15877
-
-
-
?
D-mannose + ubiquinone
? + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
D-melibiose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
D-melibiose + pyrroloquinoline quinone
?
show the reaction diagram
-
10% of the activity with D-glucose
-
-
?
D-ribose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-ribose + pyrroloquinoline quinone
D-ribono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-ribose + ubiquinone
? + ubiquinol
show the reaction diagram
P15877
-
-
-
?
D-xylose + 2,6-dichloroindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-xylose + 2,6-dichlorophenolindolphenol
D-xylono-1,5-lactone + ?
show the reaction diagram
P13650
-
-
-
?
D-xylose + 2,6-dichlorophenolindophenol
D-xylono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
86% activity compared to D-glucose
-
-
?
D-xylose + N-ethylphenazonium ethyl sulfate
D-xylono-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
D-xylose + oxidized N-methylphenazonium methyl sulfate
D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
no activity
-
-
-
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
13% of the activity with D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
20% of the activity with D-glucose
-
-
?
D-xylose + pyrroloquinoline quinone
D-xylono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
D-xylose + ubiquinone
D-xylono-1,5-lactone + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
L-arabinose + 2,6-dichloroindophenol
? + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
L-arabinose + 2,6-dichlorophenolindophenol
L-arabinono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
97% activity compared to D-glucose
-
-
?
L-arabinose + N-ethylphenazonium ethyl sulfate
L-arabino-1,5-lactone + ?
show the reaction diagram
-
-
-
-
?
L-arabinose + oxidized N-methylphenazonium methyl sulfate
L-arabino-1,5-lactone + reduced N-methylphenazonium methyl sulfate
show the reaction diagram
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
-
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
2.8% of the activity with D-glucose
-
-
-
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
35% of the activity with D-glucose
-
-
?
L-arabinose + pyrroloquinoline quinone
L-arabino-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
show the reaction diagram
P15877
-
-
-
?
L-arabinose + ubiquinone
L-arabino-1,5-lactone + ubiquinol
show the reaction diagram
Erwinia sp. 34-1
-
-
-
-
?
L-lyxose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
no activity
-
-
-
L-rhamnose + pyrroloquinoline quinone
L-rhamnono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
7.5% of the activity with D-glucose
-
-
?
lactose + 2,6-dichlorophenol-indophenol
?
show the reaction diagram
-
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
-
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
P13650
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
-
-
-
-
?
lactose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
Acinetobacter calcoaceticus LMD79.41
-
-
-
-
?
lactose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
lactose + pyrroloquinoline quinone
?
show the reaction diagram
-
no activity
-
-
-
lactose + pyrroloquinoline quinone
?
show the reaction diagram
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
-
65% of the activity with D-glucose
-
-
?
lactose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
-
lactose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
lactose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
lactose + ubiquinone
? + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
lactose + ubiquinone
?
show the reaction diagram
P13650
-
-
-
?
maltose + 2,6-dichloroindophenol
maltono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
-
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
P13650
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
-
-
-
-
?
maltose + 2,6-dichlorophenolindolphenol
?
show the reaction diagram
Acinetobacter calcoaceticus LMD79.41
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
-
-
-
?
maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
3.2% of the activity with D-glucose
-
-
?
maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
5% of the activity with D-glucose
-
-
?
maltose + pyrroloquinoline quinone
?
show the reaction diagram
-
90% of the activity with D-glucose
-
-
?
maltose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
-
maltose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
maltose + ubiquinone
? + ubiquinol
show the reaction diagram
-
-
-
-
?
maltose + ubiquinone
? + ubiquinol
show the reaction diagram
-
recombinant isozyme PQQGDH-B
-
-
?
maltose + ubiquinone
?
show the reaction diagram
P13650
-
-
-
?
phenazine methosulfate + 2,6-dichlorophenol indophenol
?
show the reaction diagram
Escherichia coli, Escherichia coli YU423
-
-
-
-
?
melibiose + 2,6-dichlorophenol-indophenol
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
-
activity of the enzyme is regulated by both the glucose dehydrogenase apo-enzyme synthesis and the synthesis of the cofactor pyrroloquinoline quinone
-
-
-
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
?
-
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
-
additional information
?
-
P13650
substrate specificities of recombinant wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
substrate specificities of wild-type and mutant isozyme PQQGDH-B, overview
-
-
-
additional information
?
-
-
substrate specificity of native and immobilized enzyme
-
-
-
additional information
?
-
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
-
additional information
?
-
P15877
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
?
-
-
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
?
-
-
the enzyme catalyzes only oxidation of D-aldoses and aldose derivatives
-
-
-
additional information
?
-
Erwinia sp. 34-1
-
2-hydroxy-1,4-naphthoquinone, tetramethyl-1,4-benzoquinone, and 2-methyl-1,4-naphthoquinone are no redox mediators for the enzyme
-
-
-
additional information
?
-
Erwinia sp. 34-1
-
substrate specificity of native and immobilized enzyme, maltose is a poor substrate
-
-
-
additional information
?
-
Acinetobacter calcoaceticus LMD 79.41
-
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
?
-
Acinetobacter calcoaceticus L.M.D.
-
substrate specificity of native and immobilized enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucose + ubiquinone
beta-D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ?
D-glucono-1,5-lactone + ?
show the reaction diagram
-
physiological electron acceptor in not known
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-, Q8ZUN8
-
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
enzyme donates electrons directly to ubiquinone in the respiratory chain
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
-
linked to the respiratory chain of a wide variety of bacteria
-
-
?
D-glucose + pyrroloquinoline quinone
D-glucono-1,5-lactone + pyrroloquinoline quinol
show the reaction diagram
Acinetobacter calcoaceticus LMD 79.41
-
membrane-bound enzyme functions by linking to the respiratory chain via ubiquinone
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
P13650
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
D4P700
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
-
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
show the reaction diagram
P15877
transfers electrons to the cytochrome oxidase through ubiquinone in the electron transport chain
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus LMD79.41
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Serratia marcescens CMS2526
-
-
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Acinetobacter calcoaceticus L.M.D. 79.41
-
preferred substrate
-
-
?
D-glucose + ubiquinone
D-glucono-1,5-lactone + ubiquinol
show the reaction diagram
Pantoea ananatis SC17(0)
D4P700
-
-
-
?
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
?
-
-
activity of the enzyme is regulated by both the glucose dehydrogenase apo-enzyme synthesis and the synthesis of the cofactor pyrroloquinoline quinone
-
-
-
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
each subunit of the dimer contains one molecule of pyrroloquinoline quinone; prosthetic group
pyrroloquinoline quinone
-
prosthetic group; type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
prosthetic group; type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
prosthetic group; type II enzyme: pyrroloquinoline quinone can not be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
prosthetic group; type I enzyme: pyrroloquinoline quinone can be removed by dialysis against EDTA-containg buffers
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
organisms with an active holoenzyme
pyrroloquinoline quinone
-
organisms with an inactive apoenzyme
pyrroloquinoline quinone
-
organisms with an active holoenzyme
pyrroloquinoline quinone
-
organisms with an inactive apoenzyme
pyrroloquinoline quinone
-
organisms with an active holoenzyme
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
prosthetic group
pyrroloquinoline quinone
-
prosthetic group; Sinorhizobium meliloti is unable to synthesize pyrroloquinoline quinone, synthesis of the holoenzyme in alfalfa nodules
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; prosthetic group
pyrroloquinoline quinone
-
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
-
cofactor required
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
-
prosthetic group
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, dependent on exogenous PQQ, since Escherichia coli does not synthesize PQQ itself
pyrroloquinoline quinone
P15877
i.e. PQQ, dependent on, Escherichia coli needs to be reconstituted with PQQ for activity
pyrroloquinoline quinone
-
i.e. PQQ, dependent on
pyrroloquinoline quinone
-
i.e. PQQ
pyrroloquinoline quinone
-
prosthetic group
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
-
i.e. PQQ, dependent on
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
PQQ
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
-
dependent on
pyrroloquinoline quinone
-
; coenzyme
pyrroloquinoline quinone
-
contains one pyrroloquinoline quinone per subunit
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-, Q8ZUN8
-
pyrroloquinoline quinone
-
i.e. 2,7,9,-tricarboxyl-1H-pyrrolo[2,3-f]quinoline-4,5-dione
pyrroloquinoline quinone
-
required for activity
pyrroloquinoline quinone
-
quinoprotein, required for QGDH activity
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
required for catalysis, one molecule per enzyme subunit
pyrroloquinoline quinone
D4P700
PQQ, essential cofactor for enzyme activity, essential role of pqqABCDEF in PQQ biosynthesis, overview
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
additional information
-
ruthenium(III) bispyridine compounds and ruthenium(III) 4-methyl-bispyridine compounds can act as artificial electron transfer mediator system
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
P15877
mutants D354N, N355D, and D354N/N355D
Ca2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Ca2+
-
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+
-
catalytic activity of the membrane-bound enzyme with Ca2+ is very similar to that with Mg2+
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+
-
required for structure stabilization of the holoform
Ca2+
-
required, interacts with PQQ cofactor
Ca2+
P15877
mutants D354N, N355D, and D354N/N355D
Ca2+
-
required
Ca2+
-
required
Ca2+
-
required for activity
Ca2+
-
contains three Ca2+ ions per subunit
Ca2+
-
Ca2+ is needed for the correct folding and for the functionalization of pyrroloquinoline quinone as cofactor
Ca2+
-
three ions per enzyme subunit
Ca2+
-
apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
Cd2+
-
can replace Ca2+ in reactivation after thermal inactivation
Mg2+
-
in vivo reconstitution of apoenzyme with the prosthetic group is dependent on the presence of Ca2+ or Mg2+
Mg2+
-
Km: 0.022 mM for the wild-type enzyme
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+
-
Mg2+ anchors pyrroloquinoline quinone cofactor to the enzyme protein and activates the bound cofactor
Mg2+
P15877
required, bound at the active site, cannot be substituted by Ca2+, Sr2+, or Ba2+
Mn2+
-
can replace Ca2+ in reactivation after thermal inactivation
Sr2+
P15877
mutants D354N, N355D, and D354N/N355D
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
aptameric enzyme subunit
-
the aptameric enzyme subunit inhibits PQQGDH in the presence of adenosine
-
Ba2+
P15877
competitive to Mg2+, wild-type enzyme
Ca2+
P15877
competitive to Mg2+, wild-type enzyme
D-glucose
-
substrate inhibition at high concentrations
D-glucose
-
substrate inhibition
EDTA
-
3.3 mM, complete inhibition
methylhydrazine
-
competitive
methylhydrazine
-, Q8ZUN8
-
p-benzoquinone
-
1.7 mM, complete inhibition
PGa4
-
aptamer PGa4 reduces enzymatic activity to 80% at 25 nM
-
pyrroloquinoline quinone
-
substrate inhibition at high concentrations
Sr2+
P15877
competitive to Mg2+, wild-type enzyme
Mg2+
P15877
competitive to Ca2+, Sr2+, or Ba2+, mutants D354N, N355D, and D354N/N355D
additional information
-
purified enzyme is inactivated upon removal of detergent by acetone treatment. The detergent-depleted enzyme is partially activated by Triton X-100
-
additional information
-
the protein region responsible for complete EDTA tolerance is located between 32% and 59% from the N-terminus, A27 region
-
additional information
-
poor inhibition of isozyme PQQGDH-B by 5 mM EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
D4P700
exogenously added cofector slightly activates the enzyme activity
Mag2
-
the PQQGDH aptameric enzyme subunit Mag2 increases activity of the enzyme by 20%
-
additional information
-
the aptameric enzyme subunit does not activate PQQGDH in the absence of adenosine
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.6
-
2,6-dichlorophenolindophenol
-
pH 8.8, 25C
9.5
-
2-amino-D-glucose
-
wild-type enzyme
1.6
-
2-deoxy-D-glucose
-
wild-type enzyme
3.5
-
2-deoxy-D-glucose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
13.6
-
2-deoxy-D-glucose
-
-
22
-
2-deoxy-D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
32
-
2-deoxy-D-glucose
-
mutant enzyme H262
88
-
2-deoxy-D-glucose
-
pH 7.0, mutant enzyme E277K
90
-
2-deoxy-D-glucose
-
pH 7.0, wild-type enzyme
10.8
-
3-deoxy-D-glucose
-
wild-type enzyme
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
-
3-O-methyl-D-glucose
-
pH 7.0, mutant enzyme E277K
27.6
-
3-O-methyl-D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
27.6
-
3-O-methyl-D-glucose
-
recombinant mutant N452T, pH 7.0
28.7
-
3-O-methyl-D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
28.7
-
3-O-methyl-D-glucose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
28.8
-
3-O-methyl-D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
41
-
3-O-methyl-D-glucose
-
recombinant wild-type enzyme, pH 7.0, 25C
46
-
3-O-methyl-D-glucose
-
pH 7.0, wild-type enzyme
53
-
3-O-methyl-D-glucose
-
recombinant tagged enzyme, pH 7.0, 25C
56
-
3-O-methyl-D-glucose
-
recombinant triple mutant enzyme, pH 7.0, 25C
79
-
3-O-methyl-D-glucose
-
wild-type enzyme
79
-
3-O-methyl-D-glucose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
99
-
3-O-methyl-D-glucose
-
recombinant mutant D167E, pH 7.0
198
-
3-O-methyl-D-glucose
-
recombinant mutant D167E/N452T, pH 7.0
0.73
-
4-(4-ferrocenylimino-methyl)phenol
-
s-GDH
2.43
-
4-(4-ferrocenylimino-methyl)phenol
-
m-GDH
0.89
-
4-ferrocenylnitrophenol
-
s-GDH
2.73
-
4-ferrocenylnitrophenol
-
m-GDH
0.83
-
4-ferrocenylphenol
-
m-GDH
1
-
4-ferrocenylphenol
-
s-GDH
1.3
-
6-deoxy-D-glucose
-
wild-type enzyme
21
-
allose
-
pH 7.0, mutant enzyme E277K
32.5
-
allose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
34
-
allose
-
recombinant Arg-tagged enzyme, pH 7.0
35.5
-
allose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
35.5
-
allose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
36
-
allose
-
recombinant chimeric mutant enzyme, pH 7.0
38.7
-
allose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
38.7
-
allose
-
recombinant mutant N452T, pH 7.0
63
-
allose
-
recombinant wild-type enzyme, pH 7.0, 25C
75
-
allose
-
recombinant tagged enzyme, pH 7.0, 25C
76
-
allose
-
recombinant triple mutant enzyme, pH 7.0, 25C
182
-
allose
-
recombinant mutant D167E/N452T, pH 7.0
199
-
allose
-
recombinant mutant D167E, pH 7.0
14
-
cellobiose
-
recombinant wild-type isozyme PQQGDH-B and mutant N452T, pH 7.0
16
-
cellobiose
-
recombinant mutant D167E/N452T, pH 7.0
17
-
cellobiose
-
recombinant mutant D167E, pH 7.0
2.5
-
D-Allose
-
wild-type enzyme
29
-
D-Allose
-
pH 7.0, wild-type enzyme
810
-
D-Allose
-
mutant enzyme H262Y
390
-
D-fructose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
5
-
D-fucose
-
pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor
8.3
-
D-fucose
-
wild-type enzyme
12
-
D-fucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
2
-
D-galactose
-
recombinant wild-type enzyme, pH 7.0, 25C
2.7
-
D-galactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
3.7
-
D-galactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
3.7
-
D-galactose
-
recombinant mutant N452T, pH 7.0
4
-
D-galactose
-
recombinant tagged enzyme, pH 7.0, 25C
5
-
D-galactose
-
recombinant triple mutant enzyme, pH 7.0, 25C
5.3
-
D-galactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
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
8
-
D-galactose
-
recombinant Arg-tagged enzyme, pH 7.0
9
-
D-galactose
-
recombinant chimeric mutant enzyme, pH 7.0
17.5
-
D-galactose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
19
-
D-galactose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor
39
-
D-galactose
-
wild-type enzyme
145
-
D-galactose
-
recombinant mutant D167E/N452T, pH 7.0
390
-
D-galactose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
0.23
-
D-glucose
-
pH 8.5, reaction with 2,6-dichlorophenolindophenol as electron acceptor
0.3
-
D-glucose
-
pH 7.0, mutant enzyme E277G
0.47
-
D-glucose
-
pH 6.0, 25C, reaction with 2,6-dichlorophenolindophenol
0.8
-
D-glucose
-
pH 7.0, 25C, mutant enzyme N607A
0.8
-
D-glucose
-
25C, mutant enzyme D730 N
0.9
-
D-glucose
-
pH 7.0, 25C, wild-type enzyme
0.91
-
D-glucose
-
25C, wild-type enzyme
0.95
-
D-glucose
-
wild-type enzyme
0.98
-
D-glucose
-
C-terminal periplasmic domain of glucose dehydrogenase
1
-
D-glucose
-
25C, mutant enzyme S357L
1.2
-
D-glucose
-
pH 7.0, 25C, mutant W404A
1.2
-
D-glucose
-
mutant E277N
1.3
-
D-glucose
-
25C, mutant enzyme H775R
1.4
-
D-glucose
-
pH 7.0, 25C, mutant K493A
1.4
-
D-glucose
-
25C, mutant enzyme G689D
1.5
-
D-glucose
-
pH 7.0, 25C, mutant K493R
1.5
-
D-glucose
-
mutant enzyme E277A
2
3
D-glucose
-
recombinant cytochrome c-fusion protein, pH 7.0
2
3
D-glucose
-
recombinant Arg-tagged enzyme, pH 7.0
2
-
D-glucose
-
pH 7.0, 21C, mutant W404F
2.1
-
D-glucose
-
wild-type enzyme
2.4
-
D-glucose
-
wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37C
2.5
-
D-glucose
-
pH 7.0, mutant enzyme E277V
2.8
-
D-glucose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
3
-
D-glucose
-
pH 7.0, 25C, mutant D466E
4
-
D-glucose
-
pH 8.5, reaction with N-methylphenazonium methyl sulfate or N-ethylphenazonium ethal sulfate as electron acceptor
4.2
-
D-glucose
-
membrane-bound enzyme form
4.3
-
D-glucose
-
pH 7.0, mutant enzyme E277Q
5.9
-
D-glucose
-
pH 8.5, reaction with Wurster Blue as electron acceptor
5.9
-
D-glucose
-
recombinant Strep-tagged enzyme, pH 6.0, 25C
7
-
D-glucose
-
pH 7.0, mutant enzyme I278F
7.2
-
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37C
7.4
-
D-glucose
-
pH 7.0, mutant enzyme E277D
7.6
-
D-glucose
-
mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
7.7
-
D-glucose
-
pH 7.0, mutant enzyme E277H
8.8
-
D-glucose
-
pH 7.0, mutant enzyme E277K
8.9
-
D-glucose
-
pH 7.0, mutant enzyme E277K
10
-
D-glucose
-
pH 7.0, 25C, mutant H262A
10.6
-
D-glucose
-
mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
11
-
D-glucose
-
mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
11.3
-
D-glucose
-
mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
12
-
D-glucose
-
pH 7.0, 25C, mutant D466N
12.3
-
D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
12.5
-
D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
12.5
-
D-glucose
-
recombinant mutant N452T, pH 7.0
15.7
-
D-glucose
-
pH 7.0, mutant enzyme N279H
16
-
D-glucose
-
recombinant mutant T416V/T417V, pH 7.0, 25C
20
-
D-glucose
-
pH 7.0, 25C, linked dimeric enzyme
20
-
D-glucose
-
recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25C
22
-
D-glucose
-
recombinant chimeric mutant enzyme, pH 7.0
22.6
-
D-glucose
-
mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37C
24
-
D-glucose
-
pH 7.0, mutant enzyme D275E and D276E
24.5
-
D-glucose
-
soluble enzyme
25
-
D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
25
-
D-glucose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
25
-
D-glucose
-
recombinant triple mutant enzyme, pH 7.0, 25C
26
-
D-glucose
-
pH 7.0, wild-type enzyme
27
-
D-glucose
-
recombinant wild-type enzyme and tagged enzyme, pH 7.0, 25C
41.4
-
D-glucose
-
mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37C
48
-
D-glucose
-
recombinant mutant D167E/N452T, pH 7.0
55
-
D-glucose
-
recombinant mutant D167E, pH 7.0
154
-
D-glucose
-
recombinant mutant H168Q, pH 7.0
193
-
D-glucose
-
recombinant mutant H168C, pH 7.0
400
-
D-glucose
-
-
460
-
D-glucose
-
mutant enzyme H262Y
680
-
D-glucose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
22
-
D-mannose
-
pH 7.0, wild-type enzyme and mutant enzyme E277K
78
-
D-mannose
-
wild-type enzyme
116
-
D-mannose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
910
-
D-mannose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
17.7
-
D-melibiose
-
wild-type enzyme
110
-
D-ribose
-
wild-type enzyme
166
-
D-ribose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
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
14.3
-
D-xylose
-
pH 7.0, wild-type enzyme
17
-
D-xylose
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
22
-
D-xylose
-
wild-type enzyme
34
-
D-xylose
-
pH 7.0, mutant enzyme E277K
500
-
D-xylose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
0.69
-
ferricyanide
-
pH 8.8, 25C
0.118
-
L-arabinose
-
pH 8.5, reaction with D-glucose
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
P15877
recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25C
46
-
L-arabinose
-
wild-type enzyme
100
-
L-Lyxose
-
wild-type enzyme
7.5
-
lactose
-
pH 7.0, mutant enzyme E277K
12
-
lactose
-
pH 7.0, 25C, linked dimeric enzyme
14.3
-
lactose
-
pH 7.0, wild-type enzyme
18
-
lactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
18.9
-
lactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
18.9
-
lactose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
19
-
lactose
-
recombinant cytochrome c-fusion protein, pH 7.0
20
-
lactose
-
recombinant Arg-tagged enzyme, and recombinant chimeric mutant enzyme, pH 7.0
25
-
lactose
-
recombinant wild-type enzyme, pH 7.0, 25C
26
-
lactose
-
recombinant tagged enzyme, pH 7.0, 25C
26.7
-
lactose
-
soluble enzyme
33.6
-
lactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
33.6
-
lactose
-
recombinant mutant N452T, pH 7.0
36
-
lactose
-
recombinant triple mutant enzyme, pH 7.0, 25C
55
-
lactose
-
recombinant mutant D167E/N452T, pH 7.0
77
-
lactose
-
recombinant mutant D167E, pH 7.0
10
-
maltose
-
recombinant wild-type enzyme, pH 7.0, 25C
11
-
maltose
-
recombinant tagged enzyme, pH 7.0, 25C
13
-
maltose
-
recombinant triple mutant enzyme, pH 7.0, 25C
13
-
maltose
-
recombinant chimeric mutant enzyme, pH 7.0
14
-
maltose
-
recombinant Arg-tagged enzyme, pH 7.0
14.3
-
maltose
-
pH 7.0, mutant enzyme E277K
15
-
maltose
-
recombinant cytochrome c-fusion protein, pH 7.0
16
-
maltose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
16
-
maltose
-
recombinant mutant D167E/N452T, pH 7.0
26
-
maltose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
26
-
maltose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
30.9
-
maltose
-
pH 7.0, wild-type enzyme
46.5
-
maltose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
46.5
-
maltose
-
recombinant mutant N452T, pH 7.0
156
-
maltose
-
recombinant mutant D167E, pH 7.0
170
-
maltose
-
-
600
-
maltose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
150
-
maltotriose
-
-
0.56
-
N,N,N,N-tetramethyl-o-phenylenediamine
-
pH 8.8, 25C
0.268
-
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-xylose
0.278
-
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-glucose
0.291
-
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with D-fucose
0.292
-
N-ethylphenazonium ethyl sulfate
-
pH 8.5, reaction with L-arabinose
0.064
-
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-galactose
0.156
-
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-xylose
0.178
-
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-glucose
0.22
-
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with D-fucose
0.362
-
N-methylphenazonium methyl sulfate
-
pH 8.5, reaction with 2-deoxy-D-glucose
0.074
-
phenazine methosulfate
-
membrane-bound enzyme form
0.13
-
phenazine methosulfate
-
pH 8.8, 25C
1.9
-
phenazine methosulfate
-
soluble enzyme form
0.00011
-
pyrroliquinoline quinone
-
pH 7.0, 25C, wild-type enzyme
0.00005
-
pyrroloquinoline quinone
-
,pH 7.0, 25C, mutant K493A
0.00009
-
pyrroloquinoline quinone
-
25C, wild-type enzyme
0.00012
-
pyrroloquinoline quinone
-
C-terminal periplasmic domain of glucose dehydrogenase
0.00012
-
pyrroloquinoline quinone
-
25C, mutant enzyme D730N
0.00014
-
pyrroloquinoline quinone
-
pH 7.0, 21C, mutant D466E and D466N
0.00022
-
pyrroloquinoline quinone
-
pH 7.0, 25C, mutant W607A
0.0005
-
pyrroloquinoline quinone
-
25C, mutant enzyme S357L
0.00064
-
pyrroloquinoline quinone
-
25C, mutant enzyme G689D
0.00088
-
pyrroloquinoline quinone
-
pH 7.0, 25C, mutant H262A
0.006
-
pyrroloquinoline quinone
-
pH 7.0, 25C, mutant W404A
0.016
-
pyrroloquinoline quinone
-
pH 7.0, 25C, mutant K493R
0.02
-
pyrroloquinoline quinone
-
pH 7.0, 25C, mutant W404F
0.021
-
pyrroloquinoline quinone
-
25C, mutant enzyme H775R
0.12
-
pyrroloquinoline quinone
-
-
0.78
-
pyrroloquinoline quinone
-
-
0.06
-
ubiquinone Q1
-
pH 8.8, 25C
0.148
-
ubiquinone Q1
-
membrane-bound enzyme form
0.178
-
ubiquinone Q1
-
soluble enzyme form
0.012
-
ubiquinone Q2
-
membrane-bound enzyme form
0.0177
-
ubiquinone Q2
-
soluble enzyme form
0.025
-
ubiquinone Q2
-
wild-type enzyme
0.03
-
ubiquinone Q2
-
C-terminal periplasmic domain of glucose dehydrogenase
0.04
-
ubiquinone Q2
-
pH 6.5, 25C
0.061
-
ubiquinone Q2
-
pH 8.8, 25C
0.028
-
ubiquinone Q4
-
pH 6.5, 25C
0.031
-
ubiquinone Q4
-
pH 8.8, 25C
0.0034
-
ubiquinone Q6
-
membrane-bound enzyme form
0.0097
-
ubiquinone Q6
-
pH 8.8, 25C
0.019
-
ubiquinone Q6
-
pH 6.5, 25C
0.0044
-
ubiquinone Q9
-
membrane-bound enzyme form
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
P15877
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
-
electrochemical data and kinetics for quinone derivatives as redocx mediators
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
predicted binding energy of wild-type and mutant enzymes
-
additional information
-
additional information
-
kinetics, cooperativity in the recombinant chimeric mutant enzyme which possesses only 1 active subunit derived from the wild-type enzyme
-
additional information
-
additional information
-
detailed kinetic analysis of wild-type and mutant enzymes, substrate inhibition and cooperativity effects, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
331
-
2-deoxy-D-glucose
-
pH 7.0, wild-type enzyme
1060
-
2-deoxy-D-glucose
-
pH 7.0, mutant enzyme E277K
215
-
3-O-methyl-D-glucose
-
recombinant mutant D167E/N452T, pH 7.0
541
-
3-O-methyl-D-glucose
-
recombinant mutant D167E, pH 7.0
1064
-
3-O-methyl-D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
1253
-
3-O-methyl-D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
1253
-
3-O-methyl-D-glucose
-
recombinant mutant N452T, pH 7.0
1450
-
3-O-methyl-D-glucose
-
pH 7.0, wild-type enzyme
3011
-
3-O-methyl-D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
3011
-
3-O-methyl-D-glucose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
3200
-
3-O-methyl-D-glucose
-
pH 7.0, mutant enzyme E277K
73
-
allose
-
recombinant mutant D167E/N452T, pH 7.0
558
-
allose
-
recombinant mutant D167E, pH 7.0
949
-
allose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
949
-
allose
-
recombinant mutant N452T, pH 7.0
1035
-
allose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
2509
-
allose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
2509
-
allose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
226
-
cellobiose
-
recombinant mutant D167E/N452T, pH 7.0
1060
-
cellobiose
-
recombinant mutant D167E, pH 7.0
1073
-
cellobiose
-
recombinant mutant N452T, pH 7.0
1355
-
cellobiose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1440
-
D-Allose
-
pH 7.0, wild-type enzyme
4560
-
D-Allose
-
pH 7.0, mutant enzyme E277K
4.3
-
D-galactose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
69
-
D-galactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
72
-
D-galactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
72
-
D-galactose
-
recombinant mutant N452T, pH 7.0
89
-
D-galactose
-
recombinant mutant D167E/N452T, pH 7.0
121
-
D-galactose
-
pH 7.0, wild-type enzyme
232
-
D-galactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
232
-
D-galactose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
630
-
D-galactose
-
pH 7.0, mutant enzyme E277K
0.8
-
D-glucose
-
recombinant mutant H168Q, pH 7.0
2.5
-
D-glucose
-
recombinant mutant H168C, pH 7.0
4.1
-
D-glucose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
121.5
-
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37C
197.1
-
D-glucose
-
mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
227.2
-
D-glucose
-
mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
305.9
-
D-glucose
-
mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
341.6
-
D-glucose
-
mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37C
445.1
-
D-glucose
-
mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37C
1114
-
D-glucose
-
mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
1193
-
D-glucose
-
recombinant mutant D167E/N452T, pH 7.0
1399
-
D-glucose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
1550
-
D-glucose
-
pH 7.0, temperature not specified in the publication, wild-type enzyme
1724
-
D-glucose
-
recombinant mutant D167E, pH 7.0
1779
-
D-glucose
-
wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37C
1791
-
D-glucose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
1791
-
D-glucose
-
recombinant mutant N452T, pH 7.0
3070
-
D-glucose
-
pH 7.0, mutant enzyme E277K
3178
-
D-glucose
-
recombinant cytochrome c-fusion protein, pH 7.0
3360
-
D-glucose
-
-
3440
-
D-glucose
-
pH 7.0, wild-type enzyme
3778
-
D-glucose
-
recombinant Arg-tagged enzyme, pH 7.0
3860
-
D-glucose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
3860
-
D-glucose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
4424
-
D-glucose
-
recombinant chimeric mutant enzyme, pH 7.0
3.1
-
D-mannose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
267
-
D-mannose
-
pH 7.0, wild-type enzyme
861
-
D-mannose
-
pH 7.0, mutant enzyme E277K
3.2
-
D-xylose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
201
-
D-xylose
-
pH 7.0, wild-type enzyme
678
-
D-xylose
-
pH 7.0, mutant enzyme E277K
167
-
lactose
-
recombinant mutant D167E/N452T, pH 7.0
478
-
lactose
-
recombinant mutant D167E, pH 7.0
574
-
lactose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
669
-
lactose
-
pH 7.0, wild-type enzyme
1038
-
lactose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
1038
-
lactose
-
recombinant mutant N452T, pH 7.0
1659
-
lactose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
1659
-
lactose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
1800
-
lactose
-
pH 7.0, mutant enzyme E277K
2.3
-
maltose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
65
-
maltose
-
recombinant mutant D167E/N452T, pH 7.0
436
-
maltose
-
recombinant mutant D167E, pH 7.0
588
-
maltose
-
N462H mutant isozyme PQQGDH-B, pH 7.0, 25C
785
-
maltose
-
pH 7.0, wild-type enzyme
1002
-
maltose
-
N452T mutant isozyme PQQGDH-B, pH 7.0, 25C
1002
-
maltose
-
recombinant mutant N452T, pH 7.0
1020
-
maltose
-
pH 7.0, mutant enzyme E277K
1930
-
maltose
-
wild-type isozyme PQQGDH-B, pH 7.0, 25C
1930
-
maltose
-
recombinant wild-type isozyme PQQGDH-B, pH 7.0
2870
-
maltose
-
-
2270
-
maltotriose
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2900
-
D-cellobiose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9114
400
-
D-fructose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9137
11000
-
D-galactose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9162
8.2
-
D-glucose
-
mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
16.8
-
D-glucose
-
mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
18
-
D-glucose
-
mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
19.7
-
D-glucose
-
mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
21.7
-
D-glucose
-
mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
27
-
D-glucose
-
mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
146.6
-
D-glucose
-
mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
744
-
D-glucose
-
wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37C
9202
2100
-
D-glucose
-
pH 7.0, temperature not specified in the publication, wild-type enzyme
9202
6100
-
D-glucose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9202
3400
-
D-mannose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9286
1700
-
D-ribose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9348
6500
-
D-xylose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
9403
4100
-
L-arabinose
-, Q8ZUN8
in 50 mM Bis-Tris propane (pH 8.0), at 50C
12082
3900
-
maltose
-, Q8ZUN8
in 50 mM Bis-ris propane (pH 8.0), at 50C
12854
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
P15877
inhibitory effects of the different metal ions on recombinant wild-type and mutant enzymes
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00245
-
D4P700
native enzyme in cells of strain SC17(0), pH 6.5, temperature not specified in the publication
0.0197
-
D4P700
native enzyme in cells of strain SC17(0) in presence of 0.01 mM pyrroloquinoline quinone, pH 6.5, temperature not specified in the publication
0.037
-
-
cells grown on a phosphate-sufficient minimal medium M9
0.058
-
-
cells grown on a phosphate-deficient medium TRP
0.77
-
-, Q8ZUN8
purified enzyme,in 50 mM BisTris propane (pH 8.0), at 50C
12
-
-
purified enzyme
12
-
-
purified native m-GDH
150
-
-
purified recombinant Strep-tagged enzyme, pH 6.0, 25C
250
-
-
purified native s-GDH
570
-
-
membrane bound enzyme form
2209
-
-
soluble enzyme form
2500
-
-
mutant N340F/Y418I
2642
-
-
purified recombinant mutant chimeric isozyme PQQGDH-B
2800
-
-
mutant T416V/T417V
3030
-
-
wild-type isozyme PQQGDH-B
3100
-
-
mutant N340F/Y418F
4512
-
-
purified recombinant Arg-tagged isozyme PQQGDH-B
4610
-
-
purified recombinant wild-type isozyme PQQGDH-B
5080
-
-
purified recombinant isozyme PQQGDH-B
5811
-
-
purified recombinant His-tagged enzyme, pH 7.0, 25C
7400
-
-
recombinant enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
gluconate production and analysis of whole cells
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
reaction with potassium ferricyanide
5.5
-
-
native m-GDH
6
9
-
immobilized s-GDH, broad maximum
6
-
-
reaction with 2,6-dichlorophenol-indophenol
6
-
-
reaction with phenazine methosulfate, 2,6-dichlorophenol indophenol and pyrroloquinoline quinone
6
-
-
immobilized m-GDH
6.5
-
-
soluble enzyme
6.5
-
P15877
assay at
6.5
-
D4P700
assay at
7
-
-
D-glucose oxidation
7
-
-
assay at
7
-
-
native s-GDH
7
-
-
assay at
7
-
P13650
activity assay
7
-
-
activity assay
7.5
-
-
the highest activity is observed with 42 mM sodium potassium phosphate buffer at pH 7.5
8
-
-, Q8ZUN8
the optimum pH for D-glucose oxidation at 50C is around pH 8.0
8.5
-
-
membrane-bound enzyme
9
-
-
reaction with pyrroloquinoline quinone
additional information
-
-
pH-dependence of native and immobilized enzyme
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
-
pH 4.0: about 50% of maximal activity, pH 8.0: about 35% of maximal activity
7.5
9.5
-
pH 7.5: about 40% of maximal activity, pH 9.5: about 85% of maximal activity, membrane-bound enzyme, reaction with phenazine methosulfate, 2,6-dichlorophenol indophenol and pyrroloquinoline quinone
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
P15877
assay at
25
-
-
activity assay
25
-
-
assay at
75
-
-, Q8ZUN8
above 75C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
40
-
at 25C the enzyme activity is reduced to 50%, whereas at 40C the activity is only reduced to 90% compared to the activity at 37C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.6
4.7
-
calculated, recombinant cytochrome c-fusion protein; calculated, wild-type GDH-B
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
effects of different carbon sources and glucose concentrations on the cell growth and sPQQGDH production, overview
Manually annotated by BRENDA team
additional information
Acinetobacter calcoaceticus L.M.D. 79.41
-
effects of different carbon sources and glucose concentrations on the cell growth and sPQQGDH production, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
outer surface of the cytoplasmic membrane
-
Manually annotated by BRENDA team
-
outer surface of the cytoplasmic membrane
-
Manually annotated by BRENDA team
-
enzyme exists as a soluble form and a membrane-bound form
Manually annotated by BRENDA team
-
outer surface of cytoplasmic membrane
Manually annotated by BRENDA team
-
bound to; it is likely that the C-terminal periplasmic domain of glucose dehydrogenase possesses a ubiquinone-reacting site and transfers electrons directly to ubiquinone
Manually annotated by BRENDA team
-
inner membrane, 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
Manually annotated by BRENDA team
-
bound, enzyme mGDH
Manually annotated by BRENDA team
-
bound enzyme m-GDH
Manually annotated by BRENDA team
-
the enzyme is a membrane integral quinoprotein
Manually annotated by BRENDA team
Acinetobacter calcoaceticus LMD 79.41
-
enzyme exists as a soluble form and a membrane-bound form
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus L.M.D. 79.41
-
isozyme mPQQGDH
-
Manually annotated by BRENDA team
Erwinia sp. 34-1
-
bound enzyme m-GDH
-
Manually annotated by BRENDA team
-
soluble isozyme sPQQGDH
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus L.M.D. 79.41
-
soluble isozyme sPQQGDH
-
-
Manually annotated by BRENDA team
-
isoyzme PQQGDH-B
-
Manually annotated by BRENDA team
-
water-soluble enzyme PQQGDH
-
Manually annotated by BRENDA team
-
isozyme PQQGDH-B, water-soluble quinoprotein
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus L.M.D.
-
enzyme s-GDH
-
-
Manually annotated by BRENDA team
Acinetobacter calcoaceticus LMD79.41, Acinetobacter calcoaceticus LMD 79.41
-
-
-
-
Manually annotated by BRENDA team
Escherichia coli YU423, Pantoea ananatis SC17(0)
-
-
-
Manually annotated by BRENDA team
additional information
-
there are two types of PQQGDH, the membrane-bound glucose dehydrogenase and the soluble glucose dehydrogenase
-
Manually annotated by BRENDA team
additional information
Acinetobacter calcoaceticus L.M.D. 79.41
-
there are two types of PQQGDH, the membrane-bound glucose dehydrogenase and the soluble glucose dehydrogenase
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-, Q8ZUN8
gel filtration
40000
-
-
determined by SDS-PAGE
40000
-
-, Q8ZUN8
dynamic light scattering
50000
-
P13650
monomer
56000
-
-
calculated from amino acid sequence
63000
-
-
recombinant enzyme, SDS-PAGE
87000
-
-
sucrose density gradient centrifugation
90000
-
-
SDS-PAGE
93000
-
-
sucrose density gradient centrifugation
94000
-
-
gel filtration
110000
-
-
equilibrium sedimentation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 55000, soluble enzyme SDS-PAGE; x * 83000, soluble enzyme, SDS-PAGE
?
-
x * 55000, soluble enzyme SDS-PAGE
?
-
x * 65000, recombinant cytochrome c-fusion protein, SDS-PAGE
?
-
x * 89000, recombinant Strep-tagged enzyme, SDS-PAGE
?
Acinetobacter calcoaceticus LMD 79.41
-
x * 55000, soluble enzyme SDS-PAGE
-
?
Acinetobacter calcoaceticus LMD79.41
-
x * 65000, recombinant cytochrome c-fusion protein, SDS-PAGE
-
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
-
(alpha)2, functional subunit composition, domain and overall structure analysis
dimer
-
structure analysis, 6-blade beta-propeller protein with each blade consisting of a 4-stranded anti-parallel beta-sheet
dimer
-
2 * 50000, deglycosylated recombinant isozyme PQQGDH-B, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
apo-GDH can be fully reconstituted in the dimeric holoform in the presence of pyrroloquinoline quinone and Ca2+
dimer
Acinetobacter calcoaceticus LMD 79.41
-
2 * 48000, SDS-PAGE
-
homodimer
P13650
2 * 50000 Da
homodimer
-
2 * 50000
homodimer
-
2 * 50000, SDS-PAGE
homodimer
Acinetobacter calcoaceticus L.M.D. 79.41
-
2 * 50000, SDS-PAGE
-
monomer
-
1 * 83000, membrane-bound enzyme form, mainly monomeric in detergent solution
monomer
-
1 * 87000, urea-SDS-PAGE
monomer
-
functional subunit composition, domain and overall structure analysis
monomer
-, Q8ZUN8
1 * 32000, SDS-PAGE; 1 * 38452, calculated from amino acid sequence
monomer
Acinetobacter calcoaceticus LMD 79.41
-
1 * 83000, membrane-bound enzyme form, mainly monomeric in detergent solution
-
additional information
-
3D-model prediction for wild-type and mutant isozyme PQQGDH-B
additional information
-
redox-related structural changes, overview
additional information
-
the monomeric enzyme is not active, 3D models of wild-type and mutant enzymes
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
secreted recombinant isozyme PQQGDH-B expressed in Pichia pastoris
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
apo form of the soluble glucose dehydrogenase
-
crystal structure analysis of enzyme in ternary complex with beta-D-glucose and PQQ
-
crystallization by microseeding
-
ternary complex of the enzyme with pyrroloquinoline quinone and methylhydrazine
-
apo- and holoenzyme at a resolution of 1.5 A
-
crystallization by microseeding, data set is collected at 2.0 A resolution
-
apoform and pyrroloquinoline quinone-bound holoenzyme, sitting drop vapor diffusion method, using 1.5 M ammonium sulfate and 0.1 M Tris/HCl buffer (pH 8.4), at 25C
-, Q8ZUN8
crystallization by microseeding, data set is collected at 1.8 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
11
-, Q8ZUN8
when heated at 70C for 30 min, the apo- and holoenzymes do not lose activity at pHs in the ranges of 4-11 and 3-11, respectively
6
-
-
activity with phenazine methosulfate, 2,6-dichlorophenol indophenol and pyrroloquinoline quinone
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
65
-
100% activity at 25-30C, about 90% activity at 35C, about 80% activity at 40-45C, about 750% activity at 50C, about 60% activity at 55C, after incubation at 60C for 1 h the enzyme still has 27% of its initial activity while loosing nearly all activity after treatment at 65C
35
-
-
pH 6, 10 min, in absence of Ca2+, stable below, reversible inactivation above
40.5
-
P15877
10 min, 50% inactivation of recombinant mutant D354N apoenzyme
40.8
-
P15877
10 min, 50% inactivation of recombinant wild-type apoenzyme
41
-
P15877
10 min, 50% inactivation of recombinant mutant D354N/N355D apoenzyme
43.2
-
P15877
10 min, 50% inactivation of recombinant mutant N355D apoenzyme
45
-
-
20 min, 20% loss of activity of native enzyme, about 50% loss of activity of linked-dimeric enzyme
48
-
-
activity decreases at 48C and above
48.6
-
P15877
10 min, 50% inactivation of recombinant mutant D354N/N355D holoenzyme
49
-
P15877
10 min, 50% inactivation of recombinant mutant D354N holoenzyme
50
-
-
pH 6, 10 min, in presence of Ca2+, inactivation above
51
-
P15877
10 min, 50% inactivation of recombinant wild-type holoenzyme
55
-
-
t1/2: 10 min for wild-type enzyme and mutant enzyme E277K, 4 min for mutant enzymes E277Q and N279H, 25 min for mutant enzyme I278F, less than 2 min for mutant enzymes E277G, E277A, E277D, E277H, E277N, E277V, D275E and D276E
55
-
P15877
10 min, 50% inactivation of recombinant mutant N355D holoenzyme
55
-
-
thermal stability of wild-type and mutant isozymes PQQGDH-B, overview
55
-
-
recombinant tagged wild-type enzyme and mutant enzyme show about 90% remaining activity after 10 min, the nontagged wild-type enzyme shows about 40% remaining activity after 10 min
55
-
-
wild-type isozyme PQQGDH-B: half-life 9.5 min
55
-
-
isozyme PQQGDH-B, 50% residual activity after 10 min
55
-
-
purified recombinant enzyme, 10 min, stable
70
-
-
10 min, mutant S145C retaines 90% of wild-type activity
100
-
-, Q8ZUN8
the enzyme is extremely thermostable, and the activity of the pyrroloquinoline quinone-bound holoenzyme is not lost after incubation at 100 C for 10 min, while the apoenzyme retains full activity at up to 80C under the same conditions
additional information
-
-
the C-terminal 3% region, A3 region, plays an important role in the increase of thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the soluble enzyme is less stable than the membrane-bound form
-
PQQ-dependent GDH immobilized on single-walled carbon nanotubes retains its enzymatic activity for glucose oxidation
-
the membrane-bound enzyme is more stable than the soluble form
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
optimization of the purification process involving cation exchange chromatography in presence of Zn2+
-
recombinant cytochrome c fusion protein from Escherichia coli
-
recombinant isozyme PQQGDH-B from Pichia pastoris culture medium, optimization of down-stream processing
-
recombinant soluble His-tagged enzyme 11.3fold from Escherichia coli strain BL21 (DE3)by nickel affinity chromatography
-
soluble enzyme and membrane-bound enzyme
-
using a His Microspin purification module
P13650
the enzyme is purified (not further specified). The enzyme stock solution has an activity of 64 U/ml and a concentration of 20 mg protein/ml. For the GDH immobilization, 2 ml of the enzyme stock solution in the 0.05 M phosphate buffer (pH 6) are applied onto the active area of the Prussian Blue-modified graphite electrode. After air-drying the electrode is incubated for 10 min in glutaraldehyde vapor 25% solution, and then kept in refrigerator
-
DEAE-Toyopearl column chromatography and hydroxyapatite column chromatography; using two column chromatographies of DEAE-Toyopearl and ceramic hydroxyapatite
-
linked-dimeric enzyme
-
mutant enzymes
-
Ni-NTA column chromatography
-
using a Ni-NTA column, the hexahistidine tag is removed by cleavage with tobacco edge virus protease, cleaved protein is purified by gel filtration
-
wild-type and mutant enzyme H262Y
-
recombinant Strep-tagged membrane-bound glucose dehydrogenase from from membranes of the expressing Gluconobacter oxydans strain by streptactin affinity chromatography to homogeneity
-
HiPrep 16/10 SP XL column chromatography
-, Q8ZUN8
HisTrap column chromatography, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expression in the periplasm of Escherichia coli strain PP2418, with and without a C-terminal tag of 3 Arg residues
-
expression of isozyme PQQGDH-B with and without an polyarginine tail in Escherichia coli strain PP2418, and of mutant H168Q
-
expression of isozyme PQQGDH-B, in Pichia pastoris using the alpha-factor signal sequence of Saccharomyces cerevisiae, recombinant enzyme is secreted to the medium, optimization of enzyme production
-
expression of the apoenzyme in Escherichia coli
-
expression of wild-type and mutant isozyme PQQGDH-B
-
expression of wild-type isozyme PQQGDH-B and mutant enzymes in Escherichia coli
-
gene gdhB, expression of the enzyme GDH-B as fusion protein C-terminally fused to cytochrome c domain from Comamonas testosteroni in Escherichia coli DH5alpha
-
into a His-tagged vector for expression in Escherichia coli JM109
P13650
recombinant high-level production of soluble His-tagged pyrroloquinoline quinone-dependent glucose dehydrogenase in Escherichia coli strain BL21 (DE3), 6fold improvement improvement of sPQQGDH expression in MMBL medium
-
expressed in Escherichia coli AT15 cells
-
expression of wild-type and mutant isozymes PQQGDH-B
-
into the pET M-11 vector for transformation of DH5alpha and BL21DE3 cells
-
mutants are expressed in Escherichia coli YU423 cells
-
random peptide ligands M13-phage library display is used to expresss the enzyme in presence of peptide ligands, overview
-
gene gox0265 or mgdh, overexpression of Strep-tagged membrane-bound glucose dehydrogenase from vector pBBR1p452 in membranes of an enzyme-deficient Gluconobacter oxydans strain, that shows 9fold higher enzyme expression level and 5fold increased mGDH activity, and 3fold increased oxygen consumption rates, compared to the wild-type strain, gluconate production and analysis of whole cells, overview
-
operon qqqABCDEF, gene gcd
D4P700
expressed in Escherichia coli BL21(DE3) Codon Plus RIL cells
-, Q8ZUN8
gene gdhS, expressionin Escherichia coli strain S17-1
-
expressed in Escherichia coli NovaBlue (DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Using a Sinorhizobium meliloti strain carrying a gcdlacZ transcriptional fusion, gcd expression is detected from very early stages of plantbacteria interactions, at the rhizosphere level, and during further stages of nodule development
Q92RB3
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A71P/N454S
P13650
mutant, relative activity vs wild type, substrate glucose 0.95, substrate maltose 0.75
A98G/K126R/L445I/N454S
P13650
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
D167A
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167C
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167E
-
site-directed mutagenesis, substrate binding residue mutation, slightly reduced activity compared to the wild-type enzyme
D167E/N452T
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D167G
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167H
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167K
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167N
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Q
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167R
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167S
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167V
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167W
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D167Y
-
site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme
D276E
-
drastic decrease in EDTA tolerance
E277A
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277D
-
decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277G
-
drastic decrease in EDTA tolerance
E277H
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277K
-
decreased Km value for glucose and altered substrate specificity, significantly increased catalytic efficiency compared with the wild-type enzyme
E277N
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277Q
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
E277V
-
decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme
G100R
P13650
mutant, relative activity vs wild type, substrate glucose 0.35, substrate maltose 0.26
G100W/G320E/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.55, substrate maltose 0.20
G320D/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.51, substrate maltose 0.16; mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.24
G320E
P13650
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.70
G320E/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.25
G320F/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.48, substrate maltose 0.17
G320Y/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.49, substrate maltose 0.16
H168C
-
site-directed mutagenesis, catalytic residue mutation, highly reduced activity compared to the wild-type enzyme
H168Q
-
site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant
H168Q
-
site-directed mutagenesis, inactive mutant, a heterodimeric chimeric enzyme consisiting of 1 wild-type subunit and 1 mutant subunit shows decreased activity and a substrate specificity similar to the wild-type enzyme
K166E
-
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166G
-
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K166I
-
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
K3E/E278G/G392C
P13650
mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.53
L194F/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.39, substrate maltose 0.075
L194F/G320E/M367P
P13650
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.14
L194F/G320E/M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.36, substrate maltose 0.051
L194F/G320F
P13650
mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.060
L194Q
P13650
mutant, relative activity vs wild type, substrate glucose 0.22, substrate maltose 0.15
N275E
-
drastic decrease in EDTA tolerance
N340F/Y418F
-
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55C and unaltered catalytic efficiency compared to the wild-type enzyme
N340F/Y418I
-
site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55C and unaltered catalytic efficiency compared to the wild-type enzyme
N428C
-
site-directed mutagenesis, at relatively high concentrations of mediator and substrate, catalysis by the mutant type may be more efficient than with the wild-type
N452T
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
N454S
P13650
mutant, relative activity vs wild type, substrate glucose 0.87, substrate maltose 0.69
Q169E
-
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q169K
-
site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme
Q193H
P13650
mutant, relative activity vs wild type, substrate glucose 0.41, substrate maltose 0.23
Q193S/G320E
P13650
mutant, relative activity vs wild type, substrate glucose 0.56, substrate maltose 0.19
Q209R/N240R/T389R
-
site-directed mutagenesis, increased thermal stability compared to the wild-type enzyme
S231C
-
increase in thermal stability
S231D
-
increase in thermal stability
S231H
-
increase in thermal stability
S231K
-
more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme, retains catalytic activity similar to the wild-type enzyme
S231L
-
increase in thermal stability
S231M
-
increase in thermal stability
S231N
-
increase in thermal stability
T348G
-
mutant crystallized by microseeding, data set is collected at 2.36 A resolution
T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.15 A resolution
T416V/T417V
-
site-directed mutagenesis, mutation of resides of the hydrophobic region, 2fold increased thermal stability at 55C and unaltered catalytic efficiency compared to the wild-type enzyme
V157I/M367V/T463S
P13650
mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78
V91A/W372R
P13650
mutant, relative activity vs wild type, substrate glucose 0.44, substrate maltose 0.22
Y171G/E245D/M341V/T348G/N428P
-
mutant crystallized by microseeding, data set is collected at 2.20 A resolution
Y248F/N342D/A376T/A418V
P13650
mutant, relative activity vs wild type, substrate glucose 0.74, substrate maltose 0.43
D204A
-
no GDH activity
D354N
P15877
site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D354N
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
D354N/N355D
P15877
site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
D448N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D456N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D457N
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
D466E
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme
D466E
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
D466N
-
very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone
D466N
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
D730A
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730N
-
low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate
D730R
-
reduced affnity for pyrroloquinoline quinone
E217A
-
no GDH activity
E217L
-
no GDH activity
E217Q
-
the mutant retains its function similar to that of wild type GDH
E591K
-
no GDH activity
E591L
-
no GDH activity
E591Q
-
no GDH activity
E742G/P757L
-
slightly higher Km value for Mg2+
G689D
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
G776A
-
the mutant retains its function similar to that of wild type GDH
G776D
-
no GDH activity
G776K
-
no GDH activity
G776L
-
no GDH activity
H262A
-
reduced affinity both for glucose, 11fold, and pyrroloquinoline quinone, 8fold, without significant effect on glucose oxidase activity
H262Y
-
greatly diminished catalytic efficiency for all substrates, rate of electron transfer to oxygen is unaffected, 230fold increased Km value for glucose
H775A
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone
H775R
-
pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone, 230fold higher Km than wild-type enzyme
K493A
-
very low glucose oxidase activity, without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493A
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
K493R
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type
K493R
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
L712R
-
no GDH activity
N355D
P15877
site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme
N452D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452I
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N452T
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B
N462D
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462H
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462K
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
N462Y
-
site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B
R201A
-
no GDH activity
R266E
-
no GDH activity
R266Q
-
no GDH activity
S145C
-
site-directed mutagenesis, introduction of a Cys residue in each monomer of the enzyme leads to formation of an intersubunit disulfide bridge at the dimer interface resulting in 30fold increased thermal stability at 55C compared to the wild-type enzyme
S357L
-
significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+
W404A
-
pronounced reduction of affinity for pyrroloquinoline quinone, very low glucose oxidase activity and phenazine methosulfate reductase activity compared with wild-type enzyme
W404F
-
pronounced reduction of affinity for pyrroloquinoline quinone, very weak activity of phenazine methosulfate reductase but still retains glucose oxidase activity equivalent to that of the wild-type
D354N
Escherichia coli YU423
-
mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity
-
D466E
Escherichia coli YU423
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
D466N
Escherichia coli YU423
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
K493A
Escherichia coli YU423
-
mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme
-
Q126E
-
the mutant shows 25.6% relative activity on maltose
Q126R
-
the mutant shows 11.4% relative activity on maltose
Q126S
-
the mutant shows 12.4% relative activity on maltose
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
Q219K/F220C
-
the mutant shows 20% relative activity on maltose
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
Q219N/F220K
-
the mutant shows 11.7% relative activity on maltose
Q126E
-
the mutant shows 25.6% relative activity on maltose
-
Q126R
-
the mutant shows 11.4% relative activity on maltose
-
Q126S
-
the mutant shows 12.4% relative activity on maltose
-
Q219E/F220E
-
the mutant shows 5.2% relative activity on maltose
-
Q219K/F220K
-
the mutant shows 29.3% relative activity on maltose
-
M367P/A376T
P13650
mutant, relative activity vs wild type, substrate glucose 0.65, substrate maltose 0.24
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
additional information
-
engineering PQQ glucose dehydrogenase with improved substrate specificity
Y302H
P13650
mutant, relative activity vs wild type, substrate glucose 0.47, substrate maltose 0.35
additional information
Acinetobacter calcoaceticus LMD79.41
-
the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview
-
L712W
-
no GDH activity
additional information
-
improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins
additional information
-
construction of a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region and production of a linked-dimeric enzyme, the linked-dimeric enzyme shows higher thermal stability than native dimeric enzyme
additional information
-
co-expression of peptide ligands in a random phage diplay modifies the substrate specificity of the enzyme towards mono- and disaccharides, overview
additional information
-
studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH
K493R
Escherichia coli YU423
-
mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme
-
additional information
D4P700
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
additional information
Pantoea ananatis SC17(0)
-
construction of DELTAgcd and DELTApqq mutants. qqqABCDEF is cloned in vivo and integrated into the chromosomes of Pantoea ananatis and Escherichia coli according to the Dual In/Out strategy. Introduction of a second copy of pqqABCDEF to Pantoea ananatis strain SC17(0) doubles the accumulation of PQQ. Integration of the operon into Escherichia coli strain MG1655DptsGDmanXY restores the growth of bacteria on glucose, overview
-
additional information
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
additional information
Serratia marcescens CMS2526
-
complementation of the rig-10 mutant, DELTAcrp gdhS, glucose insensitivity phenotype using the wild-type Serratia marcescens gdhS gene or the Escherichia coli gcd gene expressed from a medium-copy-number plasmid
-
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
protein dissociation and redimerization of recombinant wild-type and Arg-tagged enzyme, and the mutant H168Q, overview
-
protein refolding is started on the column during elution in the presence of Ca2+. Refolding is finished by dialysis against 50 mM sodium potassium phosphate buffer pH 7.5 containing 0.003 mM CaCl2 and 0.002 mM pyrroloquinoline quinone. Refolding without Ca2+ and pyrroloquinoline quinone leads to an inactive enzyme
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
enzyme is used as coupling enzyme for monitoring carbohydrate-transport reactions, the method is particularly suited for determining transport reactions that are not coupled to any form of metabolic energy such as uniport reactions, or for characterizing mutant proteins with a defective energy-coupling mechanism or system with high-affinity constants for sugars
analysis
-
application of mutant enzyme S231K as a glucose sensor constituent. The mutant has more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme and retains catalytic activity similar to the wild-type enzyme
analysis
-
because of its high turnover number, PQQ-GDH is proposed as an enzyme label for the development of sensitive electrochemical enzyme-amplified bioaffinity assays. It has, for example, been applied to the amperometric detection of DNA hybrids or sandwich DNA aptamers at the surface of a carbon electrode
biotechnology
-
engineering of the soluble enzyme GDH-B to enable the electron transfer to the electrode in absence of artificial electron mediator by mimicking the domain structure of the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni, which is composed of a PQQ-containing catalytic domain and a cytochrome c domain
biotechnology
-
engineering PQQ glucose dehydrogenase with improved substrate specificity
biotechnology
-
surface charge engineering of the enzyme for optimization of downstream processing in large scale enzyme production
biotechnology
-
enzyme has a great potential for application as glucose sensor constituent
biotechnology
-
optimization of an expression system using Pichia pastoris for use in industrial level production
biotechnology
-
the enzyme is used for glucose biosensor diagnosis
diagnostics
-
enzyme is industrially used as glucose sensor with high catalytic activity and insensitivity to oxygen
diagnostics
-
purified enzyme is immobilized on carbon electrodes modified with 4-ferrocenylphenol, 4-(4-ferrocenylimino-methyl)phenol, or 4-ferrocenylnitrophenol, for use as glucose biosensors, kinetic behaviour during immobilization
diagnostics
-
the enzyme is attractive for application in glucose detection in clinic diagnosis and industrial bioprocess controls
diagnostics
Acinetobacter calcoaceticus L.M.D.
-
purified enzyme is immobilized on carbon electrodes modified with 4-ferrocenylphenol, 4-(4-ferrocenylimino-methyl)phenol, or 4-ferrocenylnitrophenol, for use as glucose biosensors, kinetic behaviour during immobilization
-
diagnostics
Acinetobacter calcoaceticus L.M.D. 79.41
-
the enzyme is attractive for application in glucose detection in clinic diagnosis and industrial bioprocess controls
-
biotechnology
Acinetobacter calcoaceticus LMD79.41
-
engineering of the soluble enzyme GDH-B to enable the electron transfer to the electrode in absence of artificial electron mediator by mimicking the domain structure of the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni, which is composed of a PQQ-containing catalytic domain and a cytochrome c domain
-
diagnostics
Acinetobacter calcoaceticus LMD79.41
-
enzyme is industrially used as glucose sensor with high catalytic activity and insensitivity to oxygen
-
analysis
-
apoenzyme is used as a biological test system for the detection of very low amounts of pyrroloquinoline quinone
biotechnology
-
a Glucose sensitive biosensor containing GDH immobilized on Prussian blue (PB)-modified graphite electrode is designed. Properties of the biosensor are investigated in the cathodic and anodic response detection regions. It is shown, that anodic response of the biosensor is sum of two signals: direct electron transport from reduced pyrroloquinoline quinine to the electrode and by formation of the pyrroloquinoline quinone-oxygen-Prussion blue-carbon ternary complex. Cathodic response of the biosensor is based on the oxidation of the reduced pyrroloquinoline quinone by Prussian blue-oxygen-Prussian blue complex. Electrochemical regeneration of the enzyme does not produce free hydrogen peroxide
diagnostics
-
purified enzyme is immobilized on carbon electrodes modified with 4-ferrocenylphenol, 4-(4-ferrocenylimino-methyl)-phenol, or 4-ferrocenylnitrophenol, for use as glucose biosensors, kinetic behaviour during immobilization
diagnostics
Erwinia sp. 34-1
-
purified enzyme is immobilized on carbon electrodes modified with 4-ferrocenylphenol, 4-(4-ferrocenylimino-methyl)-phenol, or 4-ferrocenylnitrophenol, for use as glucose biosensors, kinetic behaviour during immobilization
-
biotechnology
-
bioengineering of water-soluble isozyme PQQGDH-B production at industrial level
analysis
-
apoenzyme is used as a biological test system for the detection of very low amounts of pyrroloquinoline quinone