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Literature summary for 1.1.5.9 extracted from

  • Zafar, M.N.; Wang, X.; Sygmund, C.; Ludwig, R.; Leech, D.; Gorton, L.
    Electron-transfer studies with a new flavin adenine dinucleotide dependent glucose dehydrogenase and osmium polymers of different redox potentials (2012), Anal. Chem., 84, 334-341.
    View publication on PubMed
Search for more literature for 1.1.5.9

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
additional information glucose-oxidizing properties of the enzyme on spectrographic graphite electrodes and as a recognition element in glucose biosensors, immobilization on spectrographic graphite electrode's surface, method, overiew. The ratio of GcGDH/Os polymer and the overall loading of the enzyme electrode significantly affect the performance of the enzyme electrode for glucose oxidation. Best suited matiral is osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+, evaluation of different Os polymers, coupled assay method with glucose oxidase, EC 1.1.3.4,overview Colletotrichum gloeosporioides

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Colletotrichum gloeosporioides
-
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Colletotrichum gloeosporioides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Pichia pastoris to homogeneity Colletotrichum gloeosporioides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + a quinone
-
 Colletotrichum gloeosporioides D-glucono-1,5-lactone + a quinol
-
 ?

Synonyms

Synonyms Comment Organism
flavin adenine dinucleotide dependent glucose dehydrogenase
-
 Colletotrichum gloeosporioides

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Colletotrichum gloeosporioides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Colletotrichum gloeosporioides

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Colletotrichum gloeosporioides