BRENDA - Enzyme Database show
show all sequences of 1.1.99.35

Designing a highly active soluble PQQ-glucose dehydrogenase for efficient glucose biosensors and biofuel cells

Durand, F.; Stines-Chaumeil, C.; Flexer, V.; Andre, I.; Mano, N.; Biochem. Biophys. Res. Commun. 402, 750-754 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Acinetobacter calcoaceticus
Engineering
Amino acid exchange
Commentary
Organism
N428C
the catalytic efficiency is increased by 47% compared to the wild type enzyme, the mutant shows increased affinity for pyrroloquinoline quinone and is twice more active toward D-glucose and more selective toward maltose than the wild type
Acinetobacter calcoaceticus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
43
-
D-glucose
wild type enzyme, at pH 7.0 and 37°C
Acinetobacter calcoaceticus
64
-
D-glucose
mutant enzyme N428C, at pH 7.0 and 37°C
Acinetobacter calcoaceticus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE
Acinetobacter calcoaceticus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + oxidized 2,6-dichlorophenolindophenol
Acinetobacter calcoaceticus
-
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter calcoaceticus
P13650
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + oxidized 2,6-dichlorophenolindophenol
-
724172
Acinetobacter calcoaceticus
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 50000, SDS-PAGE
Acinetobacter calcoaceticus
Cofactor
Cofactor
Commentary
Organism
Structure
pyrroloquinoline quinone
-
Acinetobacter calcoaceticus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Acinetobacter calcoaceticus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyrroloquinoline quinone
-
Acinetobacter calcoaceticus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
N428C
the catalytic efficiency is increased by 47% compared to the wild type enzyme, the mutant shows increased affinity for pyrroloquinoline quinone and is twice more active toward D-glucose and more selective toward maltose than the wild type
Acinetobacter calcoaceticus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
43
-
D-glucose
wild type enzyme, at pH 7.0 and 37°C
Acinetobacter calcoaceticus
64
-
D-glucose
mutant enzyme N428C, at pH 7.0 and 37°C
Acinetobacter calcoaceticus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
2 * 50000, SDS-PAGE
Acinetobacter calcoaceticus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + oxidized 2,6-dichlorophenolindophenol
Acinetobacter calcoaceticus
-
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glucose + oxidized 2,6-dichlorophenolindophenol
-
724172
Acinetobacter calcoaceticus
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 50000, SDS-PAGE
Acinetobacter calcoaceticus
Other publictions for EC 1.1.99.35
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
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1
1
1
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42
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4
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4
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1
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1
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739848
Flexer
Wired pyrroloquinoline quinone ...
Acinetobacter calcoaceticus
Anal. Chem.
86
2465-2473
2014
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-
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2
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1
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739872
Ben Farhat
Coexpression of the pyrroloqui ...
Serratia marcescens, Serratia marcescens CTM 50650
Appl. Biochem. Biotechnol.
170
1738-1750
2013
-
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1
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1
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4
-
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739873
Stredansky
Monitoring of PQQ-dependent gl ...
Acinetobacter calcoaceticus
Appl. Biochem. Biotechnol.
171
1032-1041
2013
-
-
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-
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-
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1
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13
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1
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1
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13
-
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12
12
724836
Schubart
-
A pyrroloquinolinequinone-depe ...
Acinetobacter calcoaceticus
Electrochim. Acta
82
224-232
2012
-
1
-
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1
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1
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1
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724852
Yu
-
High-level production of solub ...
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus L.M.D. 79.41
Eng. Life Sci.
12
574-582
2012
-
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1
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1
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1
10
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3
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1
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1
2
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10
1
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1
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1
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1
1
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1
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1
10
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1
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1
2
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10
1
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1
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723943
Flexer
Efficient direct electron tran ...
Acinetobacter calcoaceticus
Anal. Chem.
83
5721-5727
2011
-
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1
1
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1
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1
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2
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2
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1
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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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2
-
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-
-
-
-
-
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-
724172
Durand
Designing a highly active solu ...
Acinetobacter calcoaceticus
Biochem. Biophys. Res. Commun.
402
750-754
2010
-
-
1
-
1
-
-
2
-
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1
1
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1
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-
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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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2
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1
1
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1
1
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655127
Tanaka
Increasing stability of water- ...
Acinetobacter calcoaceticus
BMC Biochem.
6
1
2005
-
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3
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2
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1
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1
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5
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3
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2
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1
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5
-
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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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11
-
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1
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6
1
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1
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1
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11
-
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6
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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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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-
654398
Sode
-
Construction of engineered wat ...
Acinetobacter calcoaceticus
Biocatal. Biotransform.
20
405-412
2002
-
-
-
-
5
-
-
18
-
-
-
-
-
1
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-
6
-
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18
-
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-
5
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18
-
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6
-
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18
-
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18
18
655363
Yoshida
-
Secretion of water soluble pyr ...
Acinetobacter calcoaceticus
Enzyme Microb. Technol.
30
312-318
2002
-
1
1
-
1
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4
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1
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1
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1
1
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1
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4
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1
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2
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639218
Sode
Increasing the thermal stabili ...
Acinetobacter calcoaceticus
Enzyme Microb. Technol.
26
491-496
2000
-
-
-
-
7
-
-
2
-
-
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-
1
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2
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9
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1
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7
-
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2
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2
-
9
-
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-
1
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702202
Dewanti
Ca2+-assisted, direct hydride ...
Acinetobacter calcoaceticus
Biochemistry
39
9384-9392
2000
-
-
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2
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1
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702811
Kojima
-
The production of soluble pyrr ...
Acinetobacter calcoaceticus
Biotechnol. Lett.
22
1343-1347
2000
-
1
1
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1
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1
1
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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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639216
Igarashi
Construction and characterizat ...
Acinetobacter calcoaceticus
Biochem. Biophys. Res. Commun.
264
820-824
1999
-
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12
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16
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1
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9
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18
-
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12
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16
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9
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18
-
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18
18
639220
Oubrie
Active-site structure of the s ...
Acinetobacter calcoaceticus
Proc. Natl. Acad. Sci. USA
96
11787-11791
1999
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1
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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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16
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1
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16
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1
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17
17
703532
Olsthoorn
Negative cooperativity in the ...
Acinetobacter calcoaceticus
Eur. J. Biochem.
255
255-261
1998
-
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2
1
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2
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2
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1
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4
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3
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2
3
1
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2
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4
-
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703530
Olsthoorn
Ca2+ and its substitutes have ...
Acinetobacter calcoaceticus
Eur. J. Biochem.
247
659-665
1997
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