BRENDA - Enzyme Database
show all sequences of 1.1.5.9

Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris

Sygmund, C.; Staudigl, P.; Klausberger, M.; Pinotsis, N.; Djinovic-Carugo, K.; Gorton, L.; Haltrich, D.; Ludwig, R.; Microb. Cell Fact. 10, 106 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
Commentary
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]
Commentary
Organism
67000
-
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Colletotrichum gloeosporioides
-
anamorph Colletotrichum gloeosporoides
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
-
Colletotrichum gloeosporioides
Purification (Commentary)
Commentary
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]
Commentary
Organism
836
-
purified recombinant enzyme expressed from Pichia pastoris, pH 7.5, 30°C
Colletotrichum gloeosporioides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + a quinone
-
725879
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + ferricenium ion
-
725879
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + ferrocenium ion
-
-
-
?
D-xylose + ferricenium ion
-
725879
Colletotrichum gloeosporioides
D-xylono-1,5-lactone + ferrocenium ion
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
Colletotrichum gloeosporioides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
46
-
recombinant enzyme expressed from Pichia pastoris
Colletotrichum gloeosporioides
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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
Commentary
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
Commentary
Organism
7.5
-
recombinant enzyme
Colletotrichum gloeosporioides
pH Stability
pH Stability
pH Stability Maximum
Commentary
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
Commentary
Organism
Structure
FAD
dependent on
Colletotrichum gloeosporioides
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Colletotrichum gloeosporioides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
67000
-
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
-
Colletotrichum gloeosporioides
Purification (Commentary) (protein specific)
Commentary
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] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
836
-
purified recombinant enzyme expressed from Pichia pastoris, pH 7.5, 30°C
Colletotrichum gloeosporioides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + a quinone
-
725879
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + ferricenium ion
-
725879
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + ferrocenium ion
-
-
-
?
D-xylose + ferricenium ion
-
725879
Colletotrichum gloeosporioides
D-xylono-1,5-lactone + ferrocenium ion
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 67000, deglycosylated recombinant enzyme expressed from Pichia pastoris, SDS-PAGE
Colletotrichum gloeosporioides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
46
-
recombinant enzyme expressed from Pichia pastoris
Colletotrichum gloeosporioides
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
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] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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 (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
recombinant enzyme
Colletotrichum gloeosporioides
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
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
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
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
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
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
Other publictions for EC 1.1.5.9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739924
Ozawa
Identification and characteriz ...
Rasamsonia emersonii, Rasamsonia emersonii NBRC 31232, Thermoascus crustaceus, Thermoascus crustaceus NBRC 9129
Appl. Microbiol. Biotechnol.
101
173-183
2017
-
-
2
-
-
-
-
-
-
-
2
-
-
11
-
2
2
-
-
-
-
-
20
2
2
-
2
-
2
-
2
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
2
-
-
-
2
2
-
-
-
-
20
2
2
-
2
-
2
-
2
-
-
-
-
-
-
-
740195
Sode
Novel fungal FAD glucose dehyd ...
Aspergillus niger
Biosens. Bioelectron.
87
305-311
2017
-
-
1
-
-
-
-
2
-
-
1
-
-
4
-
-
-
-
1
-
-
-
3
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741496
Iwasa
-
Thermophilic Talaromyces emer ...
Rasamsonia emersonii
ACS Omega
2
1660-1665
2017
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741724
Ozawa
Identification and characteri ...
Rasamsonia emersonii, Thermoascus crustaceus, Thermoascus crustaceus NBRC 9129
Appl. Microbiol. Biotechnol.
101
173-183
2017
-
-
2
-
-
-
-
4
2
-
-
-
-
10
-
2
-
-
-
-
2
-
6
2
4
4
8
-
3
-
4
2
-
-
-
-
-
2
2
-
-
-
-
-
-
4
2
-
-
-
-
-
2
-
-
-
2
-
6
2
4
4
8
-
3
-
4
-
-
-
-
-
-
-
740120
Shiota
An Fe-S cluster in the conserv ...
Burkholderia cepacia
Bioelectrochemistry
112
178-183
2016
-
-
-
-
4
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
4
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740363
Iwasa
-
Thermostable FAD-dependent glu ...
Thermoascus aurantiacus, Thermoascus aurantiacus NBRC 6766, Thermoascus aurantiacus NBRC 9748
Electrochemistry
84
342-348
2016
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
20
-
1
-
1
-
2
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
20
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
739817
Komori
Crystallographic analysis of F ...
Aspergillus terreus
Acta Crystallogr. Sect. F
71
1017-1019
2015
-
-
1
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740224
Sakai
Stabilization of fungi-derived ...
Aspergillus flavus
Biotechnol. Lett.
37
1091-1099
2015
-
-
1
-
1
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
-
-
3
1
-
-
1
2
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
1
-
-
2
-
-
-
-
1
-
-
-
-
3
1
-
-
1
2
-
-
-
-
-
-
-
-
1
1
740778
Satake
Novel glucose dehydrogenase fr ...
Mucor circinelloides, Mucor circinelloides NISL0103
J. Biosci. Bioeng.
120
498-503
2015
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
1
1
-
-
1
-
-
14
1
1
1
1
1
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
1
-
-
14
1
1
1
1
1
1
-
1
-
-
-
-
-
-
-
741412
Yoshida
Structural analysis of fungus- ...
Aspergillus flavus, Aspergillus flavus ATCC 200026
Sci. Rep.
5
13498
2015
-
-
1
1
2
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740853
Yang
Efficient expression, purifica ...
Aspergillus terreus, Aspergillus terreus NIH2624
J. Microbiol. Biotechnol.
24
1516-1524
2014
-
-
1
-
-
-
-
1
-
-
-
-
-
7
-
-
1
-
-
-
-
-
13
1
1
1
1
-
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1
1
1
-
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-
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-
1
-
-
-
-
13
1
1
1
1
-
1
1
1
-
-
-
-
-
-
-
726109
Fapyane
High performance enzyme fuel c ...
Burkholderia cepacia
Phys. Chem. Chem. Phys.
15
9508-9512
2013
-
-
1
-
1
-
-
1
-
-
2
1
-
4
-
-
1
-
-
-
-
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1
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-
-
-
-
3
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
740387
Yamashita
Direct electron transfer type ...
Burkholderia cepacia
Enzyme Microb. Technol.
52
123-128
2013
-
-
1
-
38
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
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-
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-
1
-
-
-
-
-
1
1
-
38
-
-
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-
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-
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-
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-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723928
Zafar
Characterization of different ...
Aspergillus sp., Colletotrichum gloeosporioides, Komagataella pastoris
Anal. Bioanal. Chem.
402
2069-2077
2012
-
3
1
-
3
-
-
-
-
-
4
3
-
6
-
3
-
-
-
1
3
1
8
1
-
-
-
-
-
-
-
3
-
-
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-
3
1
3
-
3
-
-
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4
3
-
-
3
-
-
1
3
1
8
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723944
Zafar
Electron-transfer studies with ...
Colletotrichum gloeosporioides
Anal. Chem.
84
334-341
2012
-
-
1
-
1
-
-
-
1
-
-
1
-
3
-
-
1
-
-
-
-
-
1
-
1
-
-
-
1
-
-
1
-
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-
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-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
724876
Monosik
Amperometric glucose biosensor ...
Aspergillus oryzae
Enzyme Microb. Technol.
50
227-232
2012
-
2
-
-
1
-
-
1
-
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
1
-
1
-
-
-
-
2
-
1
-
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
1
-
-
-
1
1
-
-
-
724639
Mori
Screening of Aspergillus-deriv ...
Aspergillus oryzae, Aspergillus terreus
Biotechnol. Lett.
33
2255-2263
2011
-
-
2
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
725879
Sygmund
Heterologous overexpression of ...
Colletotrichum gloeosporioides
Microb. Cell Fact.
10
106
2011
-
-
1
-
-
-
-
8
-
-
1
1
-
6
-
1
1
-
-
-
1
-
3
1
1
-
1
8
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
8
-
-
1
1
-
-
1
1
-
-
1
-
3
1
1
-
1
8
1
-
1
-
-
-
-
-
8
8
725906
Sygmund
Reduction of quinones and phen ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides DSM 62728
Microbiology
157
3203-3212
2011
-
-
1
-
-
-
-
-
1
-
2
2
-
7
-
1
1
-
-
-
2
-
11
1
1
-
-
-
2
-
-
1
-
1
-
-
-
1
1
-
-
-
-
-
-
-
1
-
2
2
-
-
1
1
-
-
2
-
11
1
1
-
-
-
2
-
-
1
-
2
2
-
-
-
685757
Yamaoka
Site directed mutagenesis stud ...
Burkholderia cepacia
Biotechnol. Lett.
30
1967-1972
2008
-
1
1
-
38
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
9
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
38
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
9
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
696897
Okuda-Shimazaki
Biofuel cell system employing ...
Burkholderia cepacia, Burkholderia cepacia SM4
Biotechnol. Lett.
30
1753-1758
2008
-
1
1
-
-
-
-
-
1
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668023
Tsujimura
Novel FAD-dependent glucose de ...
Aspergillus terreus
Biosci. Biotechnol. Biochem.
70
654-659
2006
-
-
-
-
-
-
1
1
-
2
-
-
-
2
-
-
-
-
-
-
-
-
1
-
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
1
-
1
-
-
-
-
-
-
-
-
696891
Yamaoka
Essential role of the small su ...
Burkholderia cepacia, Burkholderia cepacia SM4
Biotechnol. Lett.
26
1757-1761
2004
-
-
1
-
-
-
-
-
-
-
4
-
-
5
-
-
1
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348279
Lovallo
Alteration in FAD-glucose dehy ...
Manduca sexta
J. Insect Physiol.
45
1037-1048
1999
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348280
Yamazaki
-
Increased thermal stability of ...
Bacteria
Biotechnol. Lett.
21
199-202
1999
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
2
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
2
2
1
-
-
-
-
-
-
-
-
-
-
-
695715
Yamazaki
-
Subunit Analyses of a Novel Th ...
Burkholderia cepacia
Appl. Biochem. Biotechnol.
77-79
325-335
1999
-
-
-
-
-
-
1
4
-
-
2
-
-
1
-
-
1
-
-
-
1
-
2
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
2
-
-
-
-
1
-
-
1
-
2
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
697670
Sode
-
A novel thermostable glucose d ...
Burkholderia cepacia
Enzyme Microb. Technol.
19
82-85
1996
-
-
-
-
-
-
-
-
1
-
5
-
-
1
-
-
1
-
-
-
3
-
1
2
2
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
1
-
-
3
-
1
2
2
2
2
-
-
-
-
-
-
-
-
-
-
-
348278
Cox-Foster
-
Induction of localization of F ...
Manduca sexta
J. Insect Physiol.
40
235-249
1994
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348276
Matsushita
-
Gluconsäure bildende Enzyme b ...
Pseudomonas sp.
Agric. Biol. Chem.
44
1505-1512
1980
-
-
-
-
-
-
1
7
1
-
2
-
-
1
-
-
1
-
-
-
1
-
11
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
7
1
-
2
-
-
-
-
1
-
-
1
-
11
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
348275
Müller
Gluconic acid forming enzymes ...
Aspergillus niger
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg.
132
14-24
1977
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
348274
Bak
Studies on glucose dehydrogena ...
Aspergillus oryzae
Biochim. Biophys. Acta
139
277-293
1967
-
-
-
-
-
1
-
-
-
-
2
-
-
1
-
1
1
-
-
2
1
1
1
-
-
-
3
-
-
-
2
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
2
-
-
-
1
1
-
2
1
1
1
-
-
-
3
-
-
-
2
-
-
-
-
-
-
-
348277
Hauge
Glucose dehydrogenase of Bacte ...
Acinetobacter baumannii
J. Biol. Chem.
239
3630-3639
1964
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
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1
-
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-
-
1
-
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-
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1
-
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1
-
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-
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1
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-