BRENDA - Enzyme Database show
show all sequences of 1.1.1.69

Crystallization and properties of 5-keto-D-gluconate reductase from Gluconobacter suboxydans

Adachi, O.; Shinagawa, E.; Matsushita, K.; Ameyama, M.; Agric. Biol. Chem. 43, 75-83 (1979)
No PubMed abstract available

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
-
Gluconobacter oxydans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Hg2+
-
Gluconobacter oxydans
PCMB
-
Gluconobacter oxydans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
NADPH
-
Gluconobacter oxydans
0.02
-
NADP+
-
Gluconobacter oxydans
0.9
-
5-Dehydro-D-gluconate
-
Gluconobacter oxydans
20
-
D-gluconate
-
Gluconobacter oxydans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
4 * 25000, SDS-PAGE
Gluconobacter oxydans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-dehydro-D-gluconate + NADPH
Gluconobacter oxydans
the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
D-gluconate + NADP+
-
Gluconobacter oxydans
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gluconobacter oxydans
-
IFO 12528
-
Purification (Commentary)
Commentary
Organism
-
Gluconobacter oxydans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
69.69
-
-
Gluconobacter oxydans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-dehydro-D-gluconate + NADPH
-
285823
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
-
5-dehydro-D-gluconate + NADPH
the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
285823
Gluconobacter oxydans
D-gluconate + NADP+
-
285823
Gluconobacter oxydans
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 25000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
reduction of 5-dehydro-D-gluconate and oxidation of D-gluconate
Gluconobacter oxydans
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
thermal stability is enhanced by addition of either D-gluconate or 5-keto-D-gluconate, or both
Gluconobacter oxydans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
reduction of 5-dehydro-D-gluconate
Gluconobacter oxydans
10
-
oxidation of D-gluconate in presence of NADP+
Gluconobacter oxydans
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
cofactor
Gluconobacter oxydans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
cofactor
Gluconobacter oxydans
Crystallization (Commentary) (protein specific)
Crystallization
Organism
-
Gluconobacter oxydans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Hg2+
-
Gluconobacter oxydans
PCMB
-
Gluconobacter oxydans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.006
-
NADPH
-
Gluconobacter oxydans
0.02
-
NADP+
-
Gluconobacter oxydans
0.9
-
5-Dehydro-D-gluconate
-
Gluconobacter oxydans
20
-
D-gluconate
-
Gluconobacter oxydans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
4 * 25000, SDS-PAGE
Gluconobacter oxydans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-dehydro-D-gluconate + NADPH
Gluconobacter oxydans
the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
D-gluconate + NADP+
-
Gluconobacter oxydans
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Gluconobacter oxydans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
69.69
-
-
Gluconobacter oxydans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-dehydro-D-gluconate + NADPH
-
285823
Gluconobacter oxydans
D-gluconate + NADP+
-
-
-
-
5-dehydro-D-gluconate + NADPH
the suggested physiological role of the enzyme is to reduce 5-dehydro-D-gluconate to D-gluconate to supply a carbon source and regenerate NADP+
285823
Gluconobacter oxydans
D-gluconate + NADP+
-
285823
Gluconobacter oxydans
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 25000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
reduction of 5-dehydro-D-gluconate and oxidation of D-gluconate
Gluconobacter oxydans
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
thermal stability is enhanced by addition of either D-gluconate or 5-keto-D-gluconate, or both
Gluconobacter oxydans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
reduction of 5-dehydro-D-gluconate
Gluconobacter oxydans
10
-
oxidation of D-gluconate in presence of NADP+
Gluconobacter oxydans
Other publictions for EC 1.1.1.69
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)
738550
Chen
Genomic identification of nitr ...
Klebsiella pneumoniae subsp. pneumoniae, Klebsiella pneumoniae subsp. pneumoniae DSM 30104T, Klebsiella pneumoniae subsp. rhinoscleromatis, Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884T, Klebsiella quasipneumoniae subsp. quasipneumoniae 01A030T, Klebsiella quasipneumoniae subsp. quasipneumoniae, Klebsiella quasipneumoniae subsp. similipneumoniae 07A044T, Klebsiella quasipneumoniae subsp. similipneumoniae, Klebsiella variicola, Klebsiella variicola DSM 15968T
J. Basic Microbiol.
56
78-84
2016
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20
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16
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20
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10
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10
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20
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20
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-
739569
Shi
Gluconate 5-dehydrogenase (Ga5 ...
Streptococcus suis 05ZYH33, Streptococcus suis
Protein Cell
5
761-769
2014
-
-
1
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-
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4
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3
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1
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4
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2
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1
2
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4
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1
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4
-
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-
-
-
-
-
-
-
1
1
-
-
-
701109
Zhang
Structural insight into the ca ...
Streptococcus suis
Protein Sci.
18
294-303
2009
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-
1
1
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3
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3
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-
1
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1
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1
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1
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3
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1
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-
-
1
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-
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-
-
-
685666
Saichana
Preparation of enzymes require ...
Gluconobacter oxydans
Biosci. Biotechnol. Biochem.
71
2478-2486
2007
-
1
1
-
-
-
-
-
-
-
-
1
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3
-
-
1
-
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-
1
2
-
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-
1
-
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-
1
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
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-
-
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667291
Merford
High-yield 5-keto-D-gluconic a ...
Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
73
443-4051
2006
-
-
-
-
-
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2
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3
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2
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2
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3
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669549
Merford
Modification of the membrane-b ...
Gluconobacter oxydans, Gluconobacter oxydans DSM2343 (ATCC 621H)
J. Biotechnol.
1
556-563
2006
1
1
-
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1
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3
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6
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2
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1
1
-
2
-
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1
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-
6
-
-
-
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-
-
-
-
-
-
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-
-
-
-
654319
Elfari
A Gluconobacter oxydans mutant ...
Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
66
668-674
2005
1
1
-
-
-
-
-
-
-
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1
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-
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3
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2
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1
1
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2
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3
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-
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654315
Herrmann
Biotransformation of glucose t ...
Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
64
86-90
2004
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1
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-
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1
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1
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654316
Salusjarvi
Cloning of a gluconate/polyol ...
Gluconobacter oxydans, Gluconobacter oxydans IFO 12528
Appl. Microbiol. Biotechnol.
65
306-314
2004
-
-
-
-
-
-
-
3
1
-
1
-
-
7
-
-
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-
-
-
1
-
13
1
-
-
-
-
1
-
2
2
-
-
-
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-
2
-
-
-
-
-
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3
1
-
1
-
-
-
-
-
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-
1
-
13
1
-
-
-
-
1
-
2
-
-
-
-
-
-
-
389572
Klasen
-
Investigation of 5-ketoglucona ...
Gluconobacter oxydans
DECHEMA Biotechnol. Conf.
5
109-112
1992
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-
1
-
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-
1
2
1
1
1
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1
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1
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-
1
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3
1
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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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2
1
1
1
-
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1
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1
-
3
1
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-
2
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-
5693
Pitt
Enzymes of gluconate metabolis ...
Penicillium chrysogenum
Antonie van Leeuwenhoek
51
353-364
1985
-
-
-
-
-
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2
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1
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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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389566
Ameyama
-
5-keto-D-Gluconate reductase f ...
Gluconobacter oxydans
Methods Enzymol.
89
198-202
1982
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1
2
4
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3
2
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1
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1
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1
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4
1
1
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3
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2
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2
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2
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1
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2
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4
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3
2
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1
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1
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4
1
1
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3
-
2
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285823
Adachi
-
Crystallization and properties ...
Gluconobacter oxydans
Agric. Biol. Chem.
43
75-83
1979
-
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1
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2
4
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1
1
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1
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1
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1
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2
1
1
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1
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2
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1
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1
1
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2
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4
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1
1
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1
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1
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2
1
1
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1
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2
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285822
Chiyonobu
-
Distribution of 2-ketogluconat ...
Acetobacter aceti, Acetobacter acetigenus, Acetobacter ascendens, Acetobacter orleanensis, Acetobacter pasteurianus, Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter oxydans, Gluconobacter roseus, Gluconobacter sphaericus, Komagataeibacter xylinus
Agric. Biol. Chem.
39
2425-2427
1975
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14
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14
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14
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14
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14
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389569
Ameyama
-
Purification and properties of ...
Gluconacetobacter liquefaciens
Agric. Biol. Chem.
38
1377-1382
1974
1
-
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1
6
3
-
4
1
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1
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1
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1
1
5
-
1
-
2
-
2
2
-
2
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1
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2
-
-
1
-
6
-
3
-
4
1
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1
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1
1
5
-
1
-
2
-
2
2
-
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-
389568
De Ley
-
5-Ketogluconic acid reductase ...
Escherichia coli, Gluconobacter oxydans, Klebsiella sp.
Methods Enzymol.
9
200-203
1966
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3
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3
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1
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9
-
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6
-
-
5
-
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-
-
5
-
-
-
-
-
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-
-
-
3
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1
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9
-
-
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-
-
6
-
-
-
-
-
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-