BRENDA - Enzyme Database show
show all sequences of 1.1.5.2

2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization

Xue, Q.; Wei, Z.; Sun, W.; Cui, F.; Yu, S.; Zhou, Q.; Liu, J.; Molecules 20, 846-862 (2015)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
n-hexane
92.1% increase of activity at 80% (v/v)
Arthrobacter globiformis
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
slight inhibitory effect
Arthrobacter globiformis
Cu2+
complete inhibition at 10 mM
Arthrobacter globiformis
D-gluconic acid
non-competitive inhibitor to D-glucose and competitive inhibitor to N-methylphenazonium methyl sulfate
Arthrobacter globiformis
D-glucose
-
Arthrobacter globiformis
EDTA
complete inhibition at 0.5 mM
Arthrobacter globiformis
ethanol
3.6% residual activity at 80% (v/v)
Arthrobacter globiformis
Fe3+
complete inhibition at 10 mM
Arthrobacter globiformis
methanol
-
Arthrobacter globiformis
Mn2+
slight inhibitory effect
Arthrobacter globiformis
N-methylphenazonium methyl sulfate
-
Arthrobacter globiformis
Zn2+
slight inhibitory effect
Arthrobacter globiformis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
D-glucose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.34
-
D-xylose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.4
-
N-methylphenazonium methyl sulfate
with D-glucose as cosubstrate, at pH 5.0 and 45°C
Arthrobacter globiformis
0.46
-
D-galactose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.59
-
maltose
at pH 5.0 and 45°C
Arthrobacter globiformis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Arthrobacter globiformis
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
20% increase of activity at 1 mM
Arthrobacter globiformis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
87000
-
x * 87000, SDS-PAGE
Arthrobacter globiformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + ubiquinone
Arthrobacter globiformis
preferred substrate
D-glucono-1,5-lactone + ubiquinol
-
-
?
D-glucose + ubiquinone
Arthrobacter globiformis C224
preferred substrate
D-glucono-1,5-lactone + ubiquinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arthrobacter globiformis
-
-
-
Arthrobacter globiformis C224
-
-
-
Purification (Commentary)
Commentary
Organism
Triton X-114 phase precipitation, acetone precipitation, polyethylene glcyol 6000 precipitation, ethanol precipitation, and hydroxylapatite column chromatography
Arthrobacter globiformis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.5
-
crude extract, at pH 5.0 and 45°C
Arthrobacter globiformis
88.1
-
after 183.5fold purification, at pH 5.0 and 45°C
Arthrobacter globiformis
Storage Stability
Storage Stability
Organism
4°C, at pH 4.0 or 9.0, 2 days, complete loss of activity
Arthrobacter globiformis
4°C, at pH 6.0-7.0, 2 days, no loss of activity
Arthrobacter globiformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + N-methylphenazonium methyl sulfate
8.0% activity compared to D-glucose
741032
Arthrobacter globiformis
D-arabinono-1,5-lactone + ?
-
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
8.0% activity compared to D-glucose
741032
Arthrobacter globiformis C224
D-arabinono-1,5-lactone + ?
-
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
20% activity compared to D-glucose
741032
Arthrobacter globiformis
D-galactono-1,5-lactone + ?
-
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
20% activity compared to D-glucose
741032
Arthrobacter globiformis C224
D-galactono-1,5-lactone + ?
-
-
-
?
D-glucose + ferricyanide
D-glucose is the preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ferrocyanide
-
-
-
?
D-glucose + ferricyanide
D-glucose is the preferred substrate
741032
Arthrobacter globiformis C224
D-glucono-1,5-lactone + ferrocyanide
-
-
-
?
D-glucose + N-methylphenazonium methyl sulfate
D-glucose is the preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ?
-
-
-
?
D-glucose + ubiquinone
preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
preferred substrate
741032
Arthrobacter globiformis C224
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-xylose + N-methylphenazonium methyl sulfate
22% activity compared to D-glucose
741032
Arthrobacter globiformis
D-xylono-1,5-lactone + ?
-
-
-
?
maltose + N-methylphenazonium methyl sulfate
17% activity compared to D-glucose
741032
Arthrobacter globiformis
maltono-1,5-lactone + ?
-
-
-
?
additional information
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
741032
Arthrobacter globiformis
?
-
-
-
-
additional information
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
741032
Arthrobacter globiformis C224
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 87000, SDS-PAGE; x * 87067, calculated from amino acid sequence
Arthrobacter globiformis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Arthrobacter globiformis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
85
the enzyme reaches to the maximum activity with the increase of reaction temperature from 15 to 45 °C, and follows the sharp decline of activity to 30% at 55°C, and shows no activity at 85°C
Arthrobacter globiformis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
50
low temperature of below 40°C has the stable and highest enzyme activity after kept for 120 min. Increase of storage temperature to over 50°C inhibits the activity of above 58% after 10 min treatment, while no activity is detected after incubation for 60 min at 60 or 70°C
Arthrobacter globiformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Arthrobacter globiformis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
6
the enzyme relative activity decreases from optimum at pH 5.0 to approximately 51% or 36% when the pH drops to 4.0 or increases to 6.0, respectively
Arthrobacter globiformis
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
11.4
-
N-methylphenazonium methyl sulfate
at pH 5.0 and 45°C
Arthrobacter globiformis
14.8
-
D-glucose
at pH 5.0 and 45°C
Arthrobacter globiformis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
n-hexane
92.1% increase of activity at 80% (v/v)
Arthrobacter globiformis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
slight inhibitory effect
Arthrobacter globiformis
Cu2+
complete inhibition at 10 mM
Arthrobacter globiformis
D-gluconic acid
non-competitive inhibitor to D-glucose and competitive inhibitor to N-methylphenazonium methyl sulfate
Arthrobacter globiformis
D-glucose
-
Arthrobacter globiformis
EDTA
complete inhibition at 0.5 mM
Arthrobacter globiformis
ethanol
3.6% residual activity at 80% (v/v)
Arthrobacter globiformis
Fe3+
complete inhibition at 10 mM
Arthrobacter globiformis
methanol
-
Arthrobacter globiformis
Mn2+
slight inhibitory effect
Arthrobacter globiformis
N-methylphenazonium methyl sulfate
-
Arthrobacter globiformis
Zn2+
slight inhibitory effect
Arthrobacter globiformis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
11.4
-
N-methylphenazonium methyl sulfate
at pH 5.0 and 45°C
Arthrobacter globiformis
14.8
-
D-glucose
at pH 5.0 and 45°C
Arthrobacter globiformis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.21
-
D-glucose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.34
-
D-xylose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.4
-
N-methylphenazonium methyl sulfate
with D-glucose as cosubstrate, at pH 5.0 and 45°C
Arthrobacter globiformis
0.46
-
D-galactose
at pH 5.0 and 45°C
Arthrobacter globiformis
0.59
-
maltose
at pH 5.0 and 45°C
Arthrobacter globiformis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Arthrobacter globiformis
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
20% increase of activity at 1 mM
Arthrobacter globiformis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
87000
-
x * 87000, SDS-PAGE
Arthrobacter globiformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + ubiquinone
Arthrobacter globiformis
preferred substrate
D-glucono-1,5-lactone + ubiquinol
-
-
?
D-glucose + ubiquinone
Arthrobacter globiformis C224
preferred substrate
D-glucono-1,5-lactone + ubiquinol
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
Triton X-114 phase precipitation, acetone precipitation, polyethylene glcyol 6000 precipitation, ethanol precipitation, and hydroxylapatite column chromatography
Arthrobacter globiformis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.5
-
crude extract, at pH 5.0 and 45°C
Arthrobacter globiformis
88.1
-
after 183.5fold purification, at pH 5.0 and 45°C
Arthrobacter globiformis
Storage Stability (protein specific)
Storage Stability
Organism
4°C, at pH 4.0 or 9.0, 2 days, complete loss of activity
Arthrobacter globiformis
4°C, at pH 6.0-7.0, 2 days, no loss of activity
Arthrobacter globiformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + N-methylphenazonium methyl sulfate
8.0% activity compared to D-glucose
741032
Arthrobacter globiformis
D-arabinono-1,5-lactone + ?
-
-
-
?
D-arabinose + N-methylphenazonium methyl sulfate
8.0% activity compared to D-glucose
741032
Arthrobacter globiformis C224
D-arabinono-1,5-lactone + ?
-
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
20% activity compared to D-glucose
741032
Arthrobacter globiformis
D-galactono-1,5-lactone + ?
-
-
-
?
D-galactose + N-methylphenazonium methyl sulfate
20% activity compared to D-glucose
741032
Arthrobacter globiformis C224
D-galactono-1,5-lactone + ?
-
-
-
?
D-glucose + ferricyanide
D-glucose is the preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ferrocyanide
-
-
-
?
D-glucose + ferricyanide
D-glucose is the preferred substrate
741032
Arthrobacter globiformis C224
D-glucono-1,5-lactone + ferrocyanide
-
-
-
?
D-glucose + N-methylphenazonium methyl sulfate
D-glucose is the preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ?
-
-
-
?
D-glucose + ubiquinone
preferred substrate
741032
Arthrobacter globiformis
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-glucose + ubiquinone
preferred substrate
741032
Arthrobacter globiformis C224
D-glucono-1,5-lactone + ubiquinol
-
-
-
?
D-xylose + N-methylphenazonium methyl sulfate
22% activity compared to D-glucose
741032
Arthrobacter globiformis
D-xylono-1,5-lactone + ?
-
-
-
?
maltose + N-methylphenazonium methyl sulfate
17% activity compared to D-glucose
741032
Arthrobacter globiformis
maltono-1,5-lactone + ?
-
-
-
?
additional information
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
741032
Arthrobacter globiformis
?
-
-
-
-
additional information
no activity with D-gluconate, D-sorbose, D-mannose, D-fructose, malic acid, sucrose, and citric acid
741032
Arthrobacter globiformis C224
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 87000, SDS-PAGE; x * 87067, calculated from amino acid sequence
Arthrobacter globiformis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Arthrobacter globiformis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
85
the enzyme reaches to the maximum activity with the increase of reaction temperature from 15 to 45 °C, and follows the sharp decline of activity to 30% at 55°C, and shows no activity at 85°C
Arthrobacter globiformis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
50
low temperature of below 40°C has the stable and highest enzyme activity after kept for 120 min. Increase of storage temperature to over 50°C inhibits the activity of above 58% after 10 min treatment, while no activity is detected after incubation for 60 min at 60 or 70°C
Arthrobacter globiformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Arthrobacter globiformis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
6
the enzyme relative activity decreases from optimum at pH 5.0 to approximately 51% or 36% when the pH drops to 4.0 or increases to 6.0, respectively
Arthrobacter globiformis
Other publictions for EC 1.1.5.2
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)
739914
An
Regulation of pyrroloquinoline ...
Pseudomonas putida, Pseudomonas putida KT 2240
Appl. Environ. Microbiol.
82
4955-4964
2016
-
-
1
-
-
-
-
4
1
-
-
2
-
46
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
1
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740304
Guo
Engineering PQQ-glucose dehydr ...
Acinetobacter calcoaceticus
Chem. Commun. (Camb.)
52
485-488
2016
-
1
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740441
Duine
The cooperativity effect in th ...
Acinetobacter calcoaceticus
FEBS J.
283
3604-3612
2016
-
-
1
-
-
-
-
-
1
1
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740577
Guo
Engineered PQQ-glucose dehydro ...
Acinetobacter calcoaceticus
J. Am. Chem. Soc.
138
10108-10111
2016
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
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1
-
-
-
-
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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740933
Nakashima
Amphiphilic polymer mediators ...
Acinetobacter calcoaceticus
Langmuir
32
12986-12994
2016
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
746918
Kim
Biochemical and structural ch ...
Thermus thermophilus, Thermus thermophilus HJ6
Arch. Biochem. Biophys.
608
20-26
2016
-
2
1
-
2
-
-
39
-
-
3
-
-
5
-
-
1
-
-
-
-
-
22
1
1
3
1
41
1
1
-
1
-
-
-
-
2
1
1
-
2
-
-
-
-
39
-
-
3
-
-
-
-
1
-
-
-
-
22
1
1
3
1
41
1
1
-
-
-
-
-
-
41
41
729480
Sakamoto
Construction of a biocathode u ...
Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523
Biotechnol. Lett.
37
1399-1404
2015
-
1
-
-
-
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-
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2
-
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-
-
-
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1
-
-
-
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-
-
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-
-
-
-
-
-
-
-
-
741032
Xue
2-Keto-D-gluconate-yielding me ...
Arthrobacter globiformis, Arthrobacter globiformis C224
Molecules
20
846-862
2015
1
-
-
-
-
-
11
5
1
1
1
2
-
2
-
-
1
-
-
-
2
2
13
1
1
1
1
-
1
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Mustafa
Function of a bound ubiquinone ...
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Laurinavicius
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Erwinia sp.
Electroanalysis
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Bernardelli
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Improved specificity of reagen ...
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Ivnitski
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Ikebukuro
Selection of DNA aptamers that ...
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Hamamatsu
Modified substrate specificity ...
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Southall
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Increasing stability of water- ...
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PQQ glucose dehydrogenase with ...
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Lapenaite
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Some quinone derivatives as re ...
Erwinia sp., Erwinia sp. 34-1
Biologia (Bratisl. )
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Igarashi
Engineering PQQ glucose dehydr ...
Acinetobacter calcoaceticus
Biomol. Eng.
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2004
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29
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655791
Reddy
Mechanism of glucose oxidation ...
Acinetobacter calcoaceticus
J. Am. Chem. Soc.
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2431-2438
2004
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1
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655929
Igarashi
Construction and characterizat ...
Acinetobacter calcoaceticus
J. Biochem. Biophys. Methods
61
331-338
2004
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1
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1
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12
1
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1
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3
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7
1
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2
1
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654780
Ivanova
Comparative kinetic study of D ...
Erwinia sp.
Biochemistry
68
407-415
2003
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1
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654863
Oubrie
Structure and mechanism of sol ...
Acinetobacter calcoaceticus
Biochim. Biophys. Acta
1647
143-151
2003
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2
1
-
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654864
Yamada
Escherichia coli PQQ-containin ...
Acinetobacter calcoaceticus, Escherichia coli
Biochim. Biophys. Acta
1647
185-192
2003
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2
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6
2
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654865
James
The metal ion in the active si ...
Escherichia coli
Biochim. Biophys. Acta
1647
200-205
2003
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3
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4
9
3
4
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1
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2
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1
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8
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1
9
3
4
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1
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10
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8
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1
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654938
Laurinavicius
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Comparative characterization o ...
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Biologia (Bratisl. )
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31-34
2003
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2
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6
2
2
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6
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6
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2
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23
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6
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655097
Koh
Surface charge engineering of ...
Acinetobacter calcoaceticus
Biotechnol. Lett.
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2003
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7
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1
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1
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1
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655101
Yoshida
Improved substrate specificity ...
Escherichia coli
Biotechnol. Lett.
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301-305
2003
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1
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9
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1
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9
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1
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656767
Igarashi
Stabilization of quaternary st ...
Escherichia coli
Mol. Biotechnol.
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97-104
2003
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1
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1
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654398
Sode
-
Construction of engineered wat ...
Escherichia coli
Biocatal. Biotransform.
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2002
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12
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7
1
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18
1
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655363
Yoshida
-
Secretion of water soluble pyr ...
Acinetobacter calcoaceticus
Enzyme Microb. Technol.
30
312-318
2002
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1
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11
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1
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1
1
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1
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1
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11
1
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1
-
1
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-
-
-
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639206
Bernardelli
Periplasmic PQQ-dependent gluc ...
Rhizobium tropici, Sinorhizobium meliloti
Curr. Microbiol.
42
310-315
2001
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-
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1
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639207
Elias
C-terminal periplasmic domain ...
Escherichia coli
J. Biol. Chem.
276
48356-48361
2001
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6
1
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1
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3
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-
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639208
Elias
Functions of amino acid residu ...
Escherichia coli
J. Biol. Chem.
275
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2000
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7
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7
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17
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2
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639214
Heuberger
A spectroscopic assay for the ...
Acinetobacter calcoaceticus
Eur. J. Biochem.
267
228-234
2000
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1
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3
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1
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3
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-
-
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639215
Iswantini
-
Kinetics and thermodynamics of ...
Escherichia coli
Biochem. J.
350
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2000
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4
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1
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1
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2
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4
-
-
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-
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-
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-
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639218
Sode
Increasing the thermal stabili ...
Acinetobacter calcoaceticus
Enzyme Microb. Technol.
26
491-496
2000
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1
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7
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1
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7
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-
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-
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-
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639204
Oubrie
The 1.7 A crystal structure of ...
Acinetobacter calcoaceticus
J. Mol. Biol.
289
319-333
1999
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-
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1
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1
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-
-
-
-
-
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-
-
-
-
-
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-
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639205
Yoshida
Engineering a chimeric pyrrolo ...
Acinetobacter calcoaceticus, Escherichia coli
Protein Eng.
12
63-70
1999
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-
-
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2
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1
-
-
-
-
-
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5
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1
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2
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1
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-
-
-
-
-
-
-
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1
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-
639212
Sode
-
Construction and characterizat ...
Escherichia coli
Biotechnol. Lett.
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707-710
1999
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1
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2
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1
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1
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1
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1
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1
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2
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1
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1
-
-
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1
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639213
Cozier
-
Characterization of the membra ...
Escherichia coli
Biochem. J.
340
639-647
1999
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15
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1
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1
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1
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15
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639216
Igarashi
Construction and characterizat ...
Acinetobacter calcoaceticus
Biochem. Biophys. Res. Commun.
264
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1999
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10
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10
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1
18
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10
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27
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10
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1
18
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639220
Oubrie
Active-site structure of the s ...
Acinetobacter calcoaceticus
Proc. Natl. Acad. Sci. USA
96
11787-11791
1999
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21
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1
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11
-
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639209
Olsthoorn
On the mechanism and specifici ...
Acinetobacter calcoaceticus
Biochemistry
37
13854-13861
1998
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1
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1
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1
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1
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639210
Yamada
Mutant isolation of the Escher ...
Escherichia coli
J. Biol. Chem.
273
22021-22027
1998
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1
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8
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1
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8
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10
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1
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1
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1
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639219
Dewanti
Reconstitution of membrane.int ...
Acinetobacter calcoaceticus
Biochemistry
37
6810-6818
1998
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1
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1
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1
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1
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1
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639217
Olsthoorn
Production, characterization, ...
Acinetobacter calcoaceticus
Arch. Biochem. Biophys.
336
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1996
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1
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1
1
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1
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1
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639211
Yamada
Topological analysis of quinop ...
Escherichia coli
J. Biol. Chem.
268
12812-12817
1993
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1
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1
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639192
Cleton-Jansen
Cloning, mapping, and sequenci ...
Escherichia coli
J. Bacteriol.
172
6308-6315
1990
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3
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1
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1
1
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639193
Hommes
The separate roles of PQQ and ...
Klebsiella pneumoniae
Arch. Microbiol.
151
257-260
1989
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-
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1
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1
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1
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1
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1
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1
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1
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-
639196
Matsushita
Reactivity with ubiquinone of ...
Gluconobacter oxydans
J. Biochem.
105
633-637
1989
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-
-
-
-
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1
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2
-
4
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1
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1
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4
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1
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1
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1
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2
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1
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1
-
4
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-
639197
Matsushita
Quinoprotein D-glucose dehydro ...
Acinetobacter calcoaceticus
Biochemistry
28
6276-6280
1989
-
-
-
-
-
-
-
5
1
-
2
-
-
3
-
-
1
-
-
-
1
-
2
2
-
-
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-
2
1
-
1
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1
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5
1
-
2
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-
1
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-
1
-
2
2
-
-
-
-
2
1
-
-
-
-
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-
-
-
639198
Geiger
Reversible thermal inactivatio ...
Acinetobacter calcoaceticus
Biochem. J.
261
415-421
1989
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3
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2
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1
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2
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3
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1
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2
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-
639199
Matsushita
Quinoprotein D-glucose dehydro ...
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41
Antonie van Leeuwenhoek
56
63-72
1989
-
-
-
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11
2
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2
2
-
5
-
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1
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2
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11
2
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2
1
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11
2
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2
2
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1
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2
-
11
2
-
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-
2
1
-
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-
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-
639194
Van Schie
-
PQQ-dependent production of gl ...
Acinetobacter lwoffii, Agrobacterium tumefaciens, Azotobacter vinelandii, Rhizobium leguminosarum
J. Gen. Microbiol.
133
867-875
1987
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4
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4
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4
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4
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4
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639195
Dokter
-
The in vivo and in vitro subst ...
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41, Pseudomonas sp.
FEMS Microbiol. Lett.
43
195-200
1987
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7
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6
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1
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13
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7
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1
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13
-
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639190
Geiger
-
Crystalline quinoprotein gluco ...
Acinetobacter calcoaceticus
Biochemistry
25
6043-6048
1986
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1
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2
2
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-
2
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1
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1
1
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-
1
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1
1
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1
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1
1
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2
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2
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2
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1
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1
-
1
1
-
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-
639191
Dokter
Purification and characterizat ...
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus LMD 79.41, Escherichia coli, Gluconobacter oxydans, Klebsiella aerogenes, Pseudomonas sp.
Biochem. J.
239
163-167
1986
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2
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-
2
-
-
16
-
-
1
1
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-
1
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21
1
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2
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5
-
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5
-
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2
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2
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-
1
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1
-
21
1
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-
2
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-
639200
Matsushita
-
Immunological evidence for two ...
Acetobacter aceti, Acinetobacter calcoaceticus, Escherichia coli, Gluconobacter oxydans, Klebsiella pneumoniae, Pseudomonas aeruginosa
FEMS Microbiol. Lett.
37
141-144
1986
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7
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6
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6
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6
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7
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-
639189
Duine
Detection and determination of ...
Klebsiella aerogenes, Pseudomonas aeruginosa
Anal. Biochem.
133
239-243
1983
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2
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3
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2
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-
639201
Matsushita
-
D-Glucose dehydrogenase from P ...
Pseudomonas fluorescens
Methods Enzymol.
89
149-154
1982
-
-
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-
2
9
2
-
2
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1
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1
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1
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11
1
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1
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1
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2
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9
2
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2
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1
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1
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11
1
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-
639202
Matsushita
-
Membrane-bound, electron trans ...
Pseudomonas fluorescens
Agric. Biol. Chem.
46
1007-1011
1982
-
-
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1
3
2
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1
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1
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6
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1
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1
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1
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3
2
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1
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6
-
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-
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-
639203
Ameyama
-
L-Glucose dehydrogenase of Glu ...
Gluconobacter oxydans
Agric. Biol. Chem.
45
851-861
1981
-
-
-
-
-
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1
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1
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1
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1
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9
-
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2
1
1
1
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1
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1
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1
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1
-
9
-
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-
2
1
1
-
-
-
-
-
-
-
639188
Duine
Glucose dehydrogenase from Aci ...
Acinetobacter calcoaceticus
FEBS Lett.
108
443-446
1979
-
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1
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1
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1
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1
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1
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