Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.5.2 extracted from

  • Tanaka, S.; Igarashi, S.; Ferri, S.; Sode, K.
    Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface (2005), BMC Biochem., 6, 1.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology enzyme has a great potential for application as glucose sensor constituent Acinetobacter calcoaceticus

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type isozyme PQQGDH-B and mutant enzymes in Escherichia coli Acinetobacter calcoaceticus

Protein Variants

Protein Variants Comment Organism
N340F/Y418F site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme Acinetobacter calcoaceticus
N340F/Y418I site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme Acinetobacter calcoaceticus
T416V/T417V site-directed mutagenesis, mutation of resides of the hydrophobic region, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme Acinetobacter calcoaceticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information predicted binding energy of wild-type and mutant enzymes Acinetobacter calcoaceticus
16
-
D-glucose recombinant mutant T416V/T417V, pH 7.0, 25°C Acinetobacter calcoaceticus
20
-
D-glucose recombinant wild-type enzyme and mutants N340F/Y418F and N340F/Y418I, pH 7.0, 25°C Acinetobacter calcoaceticus

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Acinetobacter calcoaceticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + ubiquinone Acinetobacter calcoaceticus
-
D-glucono-1,5-lactone + ubiquinol
-
?

Organism

Organism UniProt Comment Textmining
Acinetobacter calcoaceticus P13650 isozyme PQQGDH-B
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2500
-
mutant N340F/Y418I Acinetobacter calcoaceticus
2800
-
mutant T416V/T417V Acinetobacter calcoaceticus
3030
-
wild-type isozyme PQQGDH-B Acinetobacter calcoaceticus
3100
-
mutant N340F/Y418F Acinetobacter calcoaceticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + 2,6-dichlorophenolindolphenol
-
Acinetobacter calcoaceticus D-glucono-1,5-lactone + ?
-
?
D-glucose + ubiquinone
-
Acinetobacter calcoaceticus D-glucono-1,5-lactone + ubiquinol
-
?

Subunits

Subunits Comment Organism
dimer structure analysis, 6-blade beta-propeller protein with each blade consisting of a 4-stranded anti-parallel beta-sheet Acinetobacter calcoaceticus
More the monomeric enzyme is not active, 3D models of wild-type and mutant enzymes Acinetobacter calcoaceticus

Synonyms

Synonyms Comment Organism
PQQ glucose dehydrogenase
-
Acinetobacter calcoaceticus
PQQGDH-B
-
Acinetobacter calcoaceticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Acinetobacter calcoaceticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
wild-type isozyme PQQGDH-B: half-life 9.5 min Acinetobacter calcoaceticus

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
Acinetobacter calcoaceticus