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Literature summary for 1.1.5.9 extracted from

  • Sygmund, C.; Staudigl, P.; Klausberger, M.; Pinotsis, N.; Djinovic-Carugo, K.; Gorton, L.; Haltrich, D.; Ludwig, R.
    Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris (2011), Microb. Cell Fact., 10, 106.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression in Escherichia coli strains Rosetta 2, T7 Express and T7 Express (pGro7) and Pichia pastoris strain X-33, with a much higher expression level and 4800fold higher enzyme activity in Pichia pastoris, fed-batch cultivation of a Pichia pastoris transformant, method evaluation, overview Colletotrichum gloeosporioides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2 3 D-xylose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
10.1
-
D-glucose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
10.2
-
D-glucose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
17.1
-
D-glucose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
19
-
D-glucose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
21
-
D-xylose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
24
-
D-xylose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
26
-
D-xylose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67000
-
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE 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
-
anamorph Colletotrichum gloeosporoides
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Colletotrichum gloeosporioides

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Pichia pastoris strain X-33 5.1fold by hydrophobic interaction and anion exchange chromatography Colletotrichum gloeosporioides

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
836
-
purified recombinant enzyme expressed from Pichia pastoris, pH 7.5, 30┬░C 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
-
?
D-glucose + ferricenium ion
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + ferrocenium ion
-
?
D-xylose + ferricenium ion
-
Colletotrichum gloeosporioides D-xylono-1,5-lactone + ferrocenium ion
-
?

Subunits

Subunits Comment Organism
? x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE Colletotrichum gloeosporioides

Synonyms

Synonyms Comment Organism
D-glucose:acceptor 1-oxidoreductase
-
Colletotrichum gloeosporioides
FAD-dependent glucose dehydrogenase
-
Colletotrichum gloeosporioides

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
46
-
recombinant enzyme expressed from Pichia pastoris Colletotrichum gloeosporioides

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
56
-
pH-dependent thermal stability with the highest Tm values in the acidic range of pH 4.5 to pH 6.4. The maximum Tm value of 56┬░C is measured in 50 mM sodium acetate buffer pH 5.0 and in 50 mM MES buffer pH 5.8 Colletotrichum gloeosporioides

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
40
-
D-xylose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
53
-
D-xylose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
60
-
D-xylose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
61
-
D-xylose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
179
-
D-glucose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
180
-
D-glucose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
380
-
D-glucose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
418
-
D-glucose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
recombinant enzyme Colletotrichum gloeosporioides

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 5.8 pH-dependent thermal stability with the highest Tm values in the acidic range of pH 4.5 to pH 6.4. The maximum Tm value of 56┬░C is measured in 50 mM sodium acetate buffer pH 5.0 and in 50 mM MES buffer pH 5.8 Colletotrichum gloeosporioides

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Colletotrichum gloeosporioides

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.9
-
D-xylose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
2
-
D-xylose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
2.5
-
D-xylose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
2.7
-
D-xylose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
17.6
-
D-glucose native enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
17.7
-
D-glucose recombinant enzyme, pH 5.5, 30┬░C Colletotrichum gloeosporioides
20
-
D-glucose native enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides
24.5
-
D-glucose recombinant enzyme, pH 7.5, 30┬░C Colletotrichum gloeosporioides