BRENDA - Enzyme Database show
show all sequences of 1.1.1.215

Characterization of enzymes involved in the central metabolism of Gluconobacter oxydans

Rauch, B.; Pahlke, J.; Schweiger, P.; Deppenmeier, U.; Appl. Microbiol. Biotechnol. 88, 711-718 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Gluconobacter oxydans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADPH
below 0.01 mM, pH 7.0, 25°C
Gluconobacter oxydans
0.051
-
NADH
pH 7.0, 25°C
Gluconobacter oxydans
5.16
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33200
-
6 * 33200, SDS-PAGE
Gluconobacter oxydans
200000
-
PAGE
Gluconobacter oxydans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxo-D-gluconate + NADPH + H+
Gluconobacter oxydans
-
D-gluconate + NADP+
-
-
?
2-oxo-D-gluconate + NADPH + H+
Gluconobacter oxydans 621H
-
D-gluconate + NADP+
-
-
?
2-oxo-L-gulonate + NADPH + H+
Gluconobacter oxydans
-
L-idonate + NADP+
-
-
?
2-oxo-L-gulonate + NADPH + H+
Gluconobacter oxydans 621H
-
L-idonate + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gluconobacter oxydans
Q5FTU6
-
-
Gluconobacter oxydans 621H
Q5FTU6
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxo-D-gluconate + NADH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans
D-gluconate + NAD+
-
-
-
?
2-oxo-D-gluconate + NADH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans 621H
D-gluconate + NAD+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
-
721369
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
-
721369
Gluconobacter oxydans 621H
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans 621H
D-gluconate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
-
721369
Gluconobacter oxydans
L-idonate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
-
721369
Gluconobacter oxydans 621H
L-idonate + NADP+
-
-
-
?
Subunits
Subunits
Commentary
Organism
hexamer
6 * 33200, SDS-PAGE
Gluconobacter oxydans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
48.2
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Gluconobacter oxydans
NADPH
-
Gluconobacter oxydans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Gluconobacter oxydans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Gluconobacter oxydans
NADPH
-
Gluconobacter oxydans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADPH
below 0.01 mM, pH 7.0, 25°C
Gluconobacter oxydans
0.051
-
NADH
pH 7.0, 25°C
Gluconobacter oxydans
5.16
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33200
-
6 * 33200, SDS-PAGE
Gluconobacter oxydans
200000
-
PAGE
Gluconobacter oxydans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-oxo-D-gluconate + NADPH + H+
Gluconobacter oxydans
-
D-gluconate + NADP+
-
-
?
2-oxo-D-gluconate + NADPH + H+
Gluconobacter oxydans 621H
-
D-gluconate + NADP+
-
-
?
2-oxo-L-gulonate + NADPH + H+
Gluconobacter oxydans
-
L-idonate + NADP+
-
-
?
2-oxo-L-gulonate + NADPH + H+
Gluconobacter oxydans 621H
-
L-idonate + NADP+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxo-D-gluconate + NADH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans
D-gluconate + NAD+
-
-
-
?
2-oxo-D-gluconate + NADH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans 621H
D-gluconate + NAD+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
-
721369
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
-
721369
Gluconobacter oxydans 621H
D-gluconate + NADP+
-
-
-
?
2-oxo-D-gluconate + NADPH + H+
enzyme shows dual cofactor specificity, being able to use both NADPH and NADH
721369
Gluconobacter oxydans 621H
D-gluconate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
-
721369
Gluconobacter oxydans
L-idonate + NADP+
-
-
-
?
2-oxo-L-gulonate + NADPH + H+
-
721369
Gluconobacter oxydans 621H
L-idonate + NADP+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
hexamer
6 * 33200, SDS-PAGE
Gluconobacter oxydans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
48.2
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
9.34
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
9.34
-
2-oxo-D-gluconate
pH 7.0, 25°C
Gluconobacter oxydans
Other publictions for EC 1.1.1.215
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)
721369
Rauch
Characterization of enzymes in ...
Gluconobacter oxydans, Gluconobacter oxydans 621H
Appl. Microbiol. Biotechnol.
88
711-718
2010
-
-
1
-
-
-
-
3
-
-
2
4
-
6
-
-
-
-
-
-
-
-
8
1
-
-
-
1
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
3
-
-
2
4
-
-
-
-
-
-
-
-
8
1
-
-
-
1
-
-
-
-
-
-
-
-
1
1
695779
De Werra
Role of gluconic acid producti ...
Pseudomonas fluorescens, Pseudomonas fluorescens CHA0
Appl. Environ. Microbiol.
75
4162-4174
2009
-
-
1
-
1
-
-
-
1
-
-
-
-
12
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700265
Pajaniappan
A temperature-regulated Campyl ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Mol. Microbiol.
68
474-491
2008
1
1
1
-
1
-
-
-
1
-
2
-
-
13
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
2
-
1
1
1
1
-
1
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
684567
Toyama
Membrane-bound, 2-keto-D-gluco ...
Gluconobacter frateurii, Gluconobacter frateurii IFO 3271
Appl. Environ. Microbiol.
73
6551-6556
2007
-
-
1
-
-
-
-
-
1
1
3
2
-
3
-
-
1
-
-
-
1
-
4
1
1
-
-
-
1
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
-
1
1
3
2
-
-
-
1
-
-
1
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
685666
Saichana
Preparation of enzymes require ...
Gluconobacter oxydans, Gluconobacter oxydans 621H
Biosci. Biotechnol. Biochem.
71
2478-2486
2007
-
-
1
-
-
-
-
-
1
1
-
2
-
5
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286278
Yum
Purification and characterizat ...
Brevibacterium ketosoreductum
Biosci. Biotechnol. Biochem.
62
154-156
1998
-
-
-
-
-
-
-
2
-
-
2
4
-
3
-
-
1
-
-
-
1
-
8
1
-
-
-
-
1
-
1
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
2
4
-
-
-
1
-
-
1
-
8
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
286279
Yum
The yiaE gene, located at 80.1 ...
Escherichia coli
J. Bacteriol.
180
5984-5988
1998
-
-
1
-
-
-
-
-
1
-
2
2
-
4
-
-
1
-
-
-
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
2
2
-
-
-
1
-
-
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5693
Pitt
Enzymes of gluconate metabolis ...
Penicillium chrysogenum, Penicillium chrysogenum Westling
Antonie van Leeuwenhoek
51
353-364
1985
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
2
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286275
Ameyama
-
2-keto-D-Gluconate reductase f ...
Acetobacter ascendens, Acetobacter pasteurianus, Gluconacetobacter liquefaciens, Gluconobacter oxydans
Methods Enzymol.
89
203-210
1982
-
-
-
3
-
-
8
-
4
4
5
3
-
4
-
-
3
-
-
-
3
4
31
2
-
-
4
-
8
-
4
12
-
-
-
-
-
-
12
3
-
-
-
8
-
-
4
4
5
3
-
-
-
3
-
-
3
4
31
2
-
-
4
-
8
-
4
-
-
-
-
-
-
-
286274
Adachi
Crystalline 2-ketogluconate re ...
Acetobacter ascendens
Agric. Biol. Chem.
42
2057-2062
1978
-
-
-
1
-
3
1
4
1
1
2
-
-
1
-
-
1
-
-
-
1
1
7
1
1
1
3
-
2
2
-
2
-
-
-
-
-
-
2
1
-
3
-
1
-
4
1
1
2
-
-
-
-
1
-
-
1
1
7
1
1
1
3
-
2
2
-
-
-
-
-
-
-
-
286276
Shinagawa
-
Distribution of gluconate dehy ...
acetic acid bacteria, no activity in a number of oxidative or aerobic bacteria
Agric. Biol. Chem.
42
1055-1057
1978
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
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2
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1
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2
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-
-
-
-
-
-
-
-
-
-
-
286273
Chiyonobu
-
Purification, crystallization ...
Acetobacter pasteurianus
Agric. Biol. Chem.
40
175-184
1976
-
-
-
1
-
2
9
12
1
1
2
1
-
1
-
-
1
-
-
-
1
2
10
1
1
1
2
-
2
2
1
2
-
-
-
-
-
-
2
1
-
2
-
9
-
12
1
1
2
1
-
-
-
1
-
-
1
2
10
1
1
1
2
-
2
2
1
-
-
-
-
-
-
-