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.

Search for more literature for 1.1.5.9

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 [µmol/min/mg]	Specific Activity Maximum [µmol/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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)