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Literature summary extracted from

  • Igarashi, S.; Hirokawa, T.; Sode, K.
    Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase (2004), Biomol. Eng., 21, 81-89.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.5.2 biotechnology engineering PQQ glucose dehydrogenase with improved substrate specificity Acinetobacter calcoaceticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.2 expression of wild-type and mutant isozyme PQQGDH-B Acinetobacter calcoaceticus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.2 D167A site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167C site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167E site-directed mutagenesis, substrate binding residue mutation, slightly reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167E/N452T site-directed mutagenesis, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167G site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167H site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167K site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167N site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167Q site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167R site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167S site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167V site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167W site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 D167Y site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 H168C site-directed mutagenesis, catalytic residue mutation, highly reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 H168Q site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant Acinetobacter calcoaceticus
1.1.5.2 K166E site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 K166G site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 K166I site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 additional information engineering PQQ glucose dehydrogenase with improved substrate specificity Acinetobacter calcoaceticus
1.1.5.2 N452T site-directed mutagenesis, reduced activity compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 Q169E site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme Acinetobacter calcoaceticus
1.1.5.2 Q169K site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme Acinetobacter calcoaceticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.2 3.7
-
 D-galactose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 5.3
-
 D-galactose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 12.5
-
 D-glucose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 14
-
 cellobiose recombinant wild-type isozyme PQQGDH-B and mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 16
-
 cellobiose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 16
-
 maltose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 17
-
 cellobiose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 18.9
-
 lactose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 25
-
 D-glucose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 26
-
 maltose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 27.6
-
 3-O-methyl-D-glucose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 28.7
-
 3-O-methyl-D-glucose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 33.6
-
 lactose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 35.5
-
 allose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 38.7
-
 allose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 46.5
-
 maltose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 48
-
 D-glucose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 55
-
 D-glucose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 55
-
 lactose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 77
-
 lactose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 99
-
 3-O-methyl-D-glucose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 145
-
 D-galactose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 154
-
 D-glucose recombinant mutant H168Q, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 156
-
 maltose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 182
-
 allose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 193
-
 D-glucose recombinant mutant H168C, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 198
-
 3-O-methyl-D-glucose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 199
-
 allose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.2 soluble isozyme PQQGDH-B Acinetobacter calcoaceticus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.2 Ca2+ required Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.2 Acinetobacter calcoaceticus P13650 isozyme PQQGDH-B
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.2 additional information
-
-
 Acinetobacter calcoaceticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.2 2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus 2-deoxy-D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 3-O-methyl-D-glucose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus 3-O-methyl-D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 allose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus ?
-
 ?
1.1.5.2 cellobiose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus ?
-
 ?
1.1.5.2 D-galactose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus D-galactono-1,5-lactone + ?
-
 ?
1.1.5.2 D-glucose + 2,6-dichlorophenolindolphenol best substrate Acinetobacter calcoaceticus D-glucono-1,5-lactone + ?
-
 ?
1.1.5.2 D-glucose + ubiquinone best substrate Acinetobacter calcoaceticus D-glucono-1,5-lactone + ubiquinol
-
 ?
1.1.5.2 D-mannose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus ?
-
 ?
1.1.5.2 D-xylose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus D-xylono-1,5-lactone + ?
-
 ?
1.1.5.2 lactose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus ?
-
 ?
1.1.5.2 maltose + 2,6-dichlorophenolindolphenol
-
 Acinetobacter calcoaceticus ?
-
 ?
1.1.5.2 additional information substrate specificities of recombinant wild-type and mutant enzymes, overview Acinetobacter calcoaceticus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.2 PQQ glucose dehydrogenase
-
 Acinetobacter calcoaceticus
1.1.5.2 PQQGDH-B
-
 Acinetobacter calcoaceticus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.2 55
-
 thermal stability of wild-type and mutant isozymes PQQGDH-B, overview Acinetobacter calcoaceticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.5.2 0.8
-
 D-glucose recombinant mutant H168Q, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 2.5
-
 D-glucose recombinant mutant H168C, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 65
-
 maltose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 72
-
 D-galactose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 73
-
 allose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 89
-
 D-galactose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 167
-
 lactose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 215
-
 3-O-methyl-D-glucose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 226
-
 cellobiose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 232
-
 D-galactose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 436
-
 maltose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 478
-
 lactose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 541
-
 3-O-methyl-D-glucose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 558
-
 allose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 949
-
 allose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1002
-
 maltose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1038
-
 lactose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1060
-
 cellobiose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1073
-
 cellobiose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1193
-
 D-glucose recombinant mutant D167E/N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1253
-
 3-O-methyl-D-glucose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1355
-
 cellobiose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1659
-
 lactose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1724
-
 D-glucose recombinant mutant D167E, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1791
-
 D-glucose recombinant mutant N452T, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 1930
-
 maltose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 2509
-
 allose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 3011
-
 3-O-methyl-D-glucose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus
1.1.5.2 3860
-
 D-glucose recombinant wild-type isozyme PQQGDH-B, pH 7.0 Acinetobacter calcoaceticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.2 7
-
 assay at Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.2 pyrroloquinoline quinone i.e. PQQ, dependent on Acinetobacter calcoaceticus