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Literature summary extracted from

  • Zafar, M.N.; Beden, N.; Leech, D.; Sygmund, C.; Ludwig, R.; Gorton, L.
    Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells (2012), Anal. Bioanal. Chem., 402, 2069-2077.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.1.5.9 analysis possible use of the enzyme as amperometric glucose biosensor Komagataella pastoris
1.1.5.9 analysis possible use of the enzyme as amperometric glucose biosensor Colletotrichum gloeosporioides
1.1.5.9 analysis possible use of the enzyme as amperometric glucose biosensor Aspergillus sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.9 recombinant expression in Pichia pastoris Colletotrichum gloeosporioides

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.9 additional information the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview Komagataella pastoris
1.1.5.9 additional information the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview Colletotrichum gloeosporioides
1.1.5.9 additional information the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview Aspergillus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.9 67000
-
x * 67000, deglycosylated recombinant enzyme, SDS-PAGE Aspergillus sp.
1.1.5.9 88000 131000
-
Komagataella pastoris
1.1.5.9 95000 135000 recombinant enzyme Colletotrichum gloeosporioides
1.1.5.9 97000
-
deglycosylated enzyme, gel filtration Aspergillus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.9 D-glucose + a quinone Komagataella pastoris
-
D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 D-glucose + a quinone Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 D-glucose + a quinone Aspergillus sp.
-
D-glucono-1,5-lactone + a quinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.9 Aspergillus sp.
-
-
-
1.1.5.9 Colletotrichum gloeosporioides
-
-
-
1.1.5.9 Komagataella pastoris
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.5.9 glycoprotein
-
Komagataella pastoris
1.1.5.9 glycoprotein
-
Colletotrichum gloeosporioides
1.1.5.9 glycoprotein
-
Aspergillus sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.5.9 commercial preparation
-
Aspergillus sp.
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.9 795
-
pH and temperature not specified in the publication Aspergillus sp.
1.1.5.9 836
-
pH and temperature not specified in the publication Komagataella pastoris
1.1.5.9 878
-
pH and temperature not specified in the publication Colletotrichum gloeosporioides

Storage Stability

EC Number Storage Stability Organism
1.1.5.9 GcGDH/Os-polymer modified electrode under storage conditions of 50 mM phosphate buffer, pH 7.4, 4 °C, injection of 0.05 ml of a 5 mM glucose solution into the electrochemical cell for 6 days, the biosensor keeps more than 90% of its initial activity after the first day Colletotrichum gloeosporioides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.9 2-deoxy-D-glucose + a quinone
-
Colletotrichum gloeosporioides 2-deoxy-D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 cellobiose + a quinone low activity Colletotrichum gloeosporioides ? + a quinol
-
?
1.1.5.9 D-glucose + a quinone
-
Komagataella pastoris D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 D-glucose + a quinone
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 D-glucose + a quinone
-
Aspergillus sp. D-glucono-1,5-lactone + a quinol
-
?
1.1.5.9 D-xylose + ferricenium ion
-
Colletotrichum gloeosporioides D-xylono-1,5-lactone + ferrocenium ion
-
?
1.1.5.9 glutamine + a quinone low activity Colletotrichum gloeosporioides ? + a quinol
-
?
1.1.5.9 additional information substrate specificity, overview. Lactose, gluconic acid, mannose, mannitol, sorbitol, galactose, sucrose, maltose, arabinose, xylitol, rhamnose, fucose, trehalose, and fructose are poor or no substrates Colletotrichum gloeosporioides ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.5.9 ? x * 67000, deglycosylated recombinant enzyme, SDS-PAGE Aspergillus sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.5.9 FAD-dependent glucose dehydrogenase
-
Komagataella pastoris
1.1.5.9 FAD-dependent glucose dehydrogenase
-
Colletotrichum gloeosporioides
1.1.5.9 FAD-dependent glucose dehydrogenase
-
Aspergillus sp.
1.1.5.9 FADGDH
-
Komagataella pastoris
1.1.5.9 FADGDH
-
Colletotrichum gloeosporioides
1.1.5.9 FADGDH
-
Aspergillus sp.
1.1.5.9 flavin adenine dinucleotide-dependent glucose dehydrogenase
-
Komagataella pastoris
1.1.5.9 flavin adenine dinucleotide-dependent glucose dehydrogenase
-
Colletotrichum gloeosporioides
1.1.5.9 flavin adenine dinucleotide-dependent glucose dehydrogenase
-
Aspergillus sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.9 FAD dependent on Komagataella pastoris
1.1.5.9 FAD dependent on Colletotrichum gloeosporioides
1.1.5.9 FAD dependent on Aspergillus sp.