BRENDA - Enzyme Database show
show all sequences of 1.1.1.76

Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli

Takusagawa, Y.; Otagiri, M.; Ui, S.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.; Biosci. Biotechnol. Biochem. 65, 1876-1878 (2001)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
Ba2+, Ca2+, Mn2+, Mg2+ and Co2+ activate enzyme 1.6-1.8 fold at a concentration of 5 mM
Corynebacterium glutamicum
Application
Application
Commentary
Organism
synthesis
preparation of chiral acetoinic compounds, enzymic identification for chiral acetoinic compounds or as model enzyme for studying the interrelation between enzymic stereospecificity and structure
Corynebacterium glutamicum
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli JM109/pLBD2-CTC; L-butanediol gene containing plasmid pLBD2-CTC is expressed in Escherichia coli JM109
Corynebacterium glutamicum
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
competitive inhibition; competitive inhibitor
Corynebacterium glutamicum
acetate
slight inhibition at 5 mM
Corynebacterium glutamicum
Cu2+
5 mM, 89% inhibition; 89% inhibition at 5 mM
Corynebacterium glutamicum
formate
slight inhibition at 5 mM
Corynebacterium glutamicum
Hg2+
100% inhibition at 5 mM; 5 mM, 100% inhibition
Corynebacterium glutamicum
Lactate
slight inhibition at 5 mM
Corynebacterium glutamicum
additional information
slight inhibition of 10-20% by organic acids at concentrations of 5 mM: lactate, pyruvate, succinate, acetate and formate
Corynebacterium glutamicum
pyruvate
slight inhibition at 5 mM
Corynebacterium glutamicum
succinate
slight inhibition at 5 mM
Corynebacterium glutamicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
NAD+
pH 10.5; pH 6.0
Corynebacterium glutamicum
0.1
-
NADH
pH 6.0
Corynebacterium glutamicum
0.22
-
L-butanediol
pH 10.5
Corynebacterium glutamicum
0.22
-
(S,S)-butane-2,3-diol
pH 6.0
Corynebacterium glutamicum
0.44
-
L-acetoin
pH 6.0
Corynebacterium glutamicum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ba2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Ca2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Co2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Mg2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Mn2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
additional information
no significant changes in enzyme activity with 5 mM Ni2+, Zn2+ and Cd2+
Corynebacterium glutamicum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27107
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
30000
-
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
110000
-
gel filtration
Corynebacterium glutamicum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
-
C-1012
-
Corynebacterium glutamicum C-1012
-
C-1012
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme; streptomycin sulfate precipitation, affinity chromatography, gel filtration
Corynebacterium glutamicum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Corynebacterium glutamicum
277.6
-
-
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-pentanedione + NADH + H+
7% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum
?
-
-
-
r
2,3-pentanedione + NADH + H+
7% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum C-1012
?
-
-
-
r
diacetyl + NADH
also reduction of 2,3-pentanedione
389580
Corynebacterium glutamicum
L-acetoin + NAD+
-
389580
Corynebacterium glutamicum
?
diacetyl + NADH
also reduction of 2,3-pentanedione
389580
Corynebacterium glutamicum C-1012
L-acetoin + NAD+
-
389580
Corynebacterium glutamicum C-1012
?
diacetyl + NADH + H+
35% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum
?
-
-
-
r
L-acetoin + NADH
short chain dehydrogenase reductase family
389580
Corynebacterium glutamicum
L-2,3-butanediol
-
389580
Corynebacterium glutamicum
r
L-acetoin + NADH
no oxidadion of several alcohols
389580
Corynebacterium glutamicum
L-2,3-butanediol
-
389580
Corynebacterium glutamicum
r
L-acetoin + NADH
short chain dehydrogenase reductase family
389580
Corynebacterium glutamicum C-1012
L-2,3-butanediol
-
389580
Corynebacterium glutamicum C-1012
r
L-acetoin + NADH
no oxidadion of several alcohols
389580
Corynebacterium glutamicum C-1012
L-2,3-butanediol
-
389580
Corynebacterium glutamicum C-1012
r
L-acetoin + NADH + H+
100% activity
389580
Corynebacterium glutamicum
(S,S)-butane-2,3-diol + NAD+
-
-
-
r
additional information
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
389580
Corynebacterium glutamicum
?
-
-
-
-
additional information
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
389580
Corynebacterium glutamicum C-1012
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
37
40
The enzyme is stable up to 37C but rapidly inactivated over 40C
Corynebacterium glutamicum
37
-
up to, rapidly inactivated over 40C, 30 min incubation before the enzyme assay
Corynebacterium glutamicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction of L-acetoin
Corynebacterium glutamicum
10.5
-
oxidation of L-butanediol; oxidation of (S,S)-butane-2,3-diol
Corynebacterium glutamicum
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
9
; stable
Corynebacterium glutamicum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.28
-
2-mercaptoethanol
Dixon plot; pH 6.0
Corynebacterium glutamicum
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Corynebacterium glutamicum
isoelectric focussing
-
4.9
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
Ba2+, Ca2+, Mn2+, Mg2+ and Co2+ activate enzyme 1.6-1.8 fold at a concentration of 5 mM
Corynebacterium glutamicum
Application (protein specific)
Application
Commentary
Organism
synthesis
preparation of chiral acetoinic compounds, enzymic identification for chiral acetoinic compounds or as model enzyme for studying the interrelation between enzymic stereospecificity and structure
Corynebacterium glutamicum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli JM109/pLBD2-CTC; L-butanediol gene containing plasmid pLBD2-CTC is expressed in Escherichia coli JM109
Corynebacterium glutamicum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Corynebacterium glutamicum
NADH
-
Corynebacterium glutamicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
competitive inhibition; competitive inhibitor
Corynebacterium glutamicum
acetate
slight inhibition at 5 mM
Corynebacterium glutamicum
Cu2+
5 mM, 89% inhibition; 89% inhibition at 5 mM
Corynebacterium glutamicum
formate
slight inhibition at 5 mM
Corynebacterium glutamicum
Hg2+
100% inhibition at 5 mM; 5 mM, 100% inhibition
Corynebacterium glutamicum
Lactate
slight inhibition at 5 mM
Corynebacterium glutamicum
additional information
slight inhibition of 10-20% by organic acids at concentrations of 5 mM: lactate, pyruvate, succinate, acetate and formate
Corynebacterium glutamicum
pyruvate
slight inhibition at 5 mM
Corynebacterium glutamicum
succinate
slight inhibition at 5 mM
Corynebacterium glutamicum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
4.28
-
2-mercaptoethanol
Dixon plot; pH 6.0
Corynebacterium glutamicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.07
-
NAD+
pH 10.5; pH 6.0
Corynebacterium glutamicum
0.1
-
NADH
pH 6.0
Corynebacterium glutamicum
0.22
-
L-butanediol
pH 10.5
Corynebacterium glutamicum
0.22
-
(S,S)-butane-2,3-diol
pH 6.0
Corynebacterium glutamicum
0.44
-
L-acetoin
pH 6.0
Corynebacterium glutamicum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ba2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Ca2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Co2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Mg2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
Mn2+
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Corynebacterium glutamicum
additional information
no significant changes in enzyme activity with 5 mM Ni2+, Zn2+ and Cd2+
Corynebacterium glutamicum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27107
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
30000
-
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
110000
-
gel filtration
Corynebacterium glutamicum
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme; streptomycin sulfate precipitation, affinity chromatography, gel filtration
Corynebacterium glutamicum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
-
Corynebacterium glutamicum
277.6
-
-
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-pentanedione + NADH + H+
7% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum
?
-
-
-
r
2,3-pentanedione + NADH + H+
7% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum C-1012
?
-
-
-
r
diacetyl + NADH
also reduction of 2,3-pentanedione
389580
Corynebacterium glutamicum
L-acetoin + NAD+
-
389580
Corynebacterium glutamicum
?
diacetyl + NADH
also reduction of 2,3-pentanedione
389580
Corynebacterium glutamicum C-1012
L-acetoin + NAD+
-
389580
Corynebacterium glutamicum C-1012
?
diacetyl + NADH + H+
35% activity in comparison to L-acetoin
389580
Corynebacterium glutamicum
?
-
-
-
r
L-acetoin + NADH
short chain dehydrogenase reductase family
389580
Corynebacterium glutamicum
L-2,3-butanediol
-
389580
Corynebacterium glutamicum
r
L-acetoin + NADH
no oxidadion of several alcohols
389580
Corynebacterium glutamicum
L-2,3-butanediol
-
389580
Corynebacterium glutamicum
r
L-acetoin + NADH
short chain dehydrogenase reductase family
389580
Corynebacterium glutamicum C-1012
L-2,3-butanediol
-
389580
Corynebacterium glutamicum C-1012
r
L-acetoin + NADH
no oxidadion of several alcohols
389580
Corynebacterium glutamicum C-1012
L-2,3-butanediol
-
389580
Corynebacterium glutamicum C-1012
r
L-acetoin + NADH + H+
100% activity
389580
Corynebacterium glutamicum
(S,S)-butane-2,3-diol + NAD+
-
-
-
r
additional information
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
389580
Corynebacterium glutamicum
?
-
-
-
-
additional information
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
389580
Corynebacterium glutamicum C-1012
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
Corynebacterium glutamicum
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
37
40
The enzyme is stable up to 37C but rapidly inactivated over 40C
Corynebacterium glutamicum
37
-
up to, rapidly inactivated over 40C, 30 min incubation before the enzyme assay
Corynebacterium glutamicum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction of L-acetoin
Corynebacterium glutamicum
10.5
-
oxidation of L-butanediol; oxidation of (S,S)-butane-2,3-diol
Corynebacterium glutamicum
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
9
; stable
Corynebacterium glutamicum
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Corynebacterium glutamicum
isoelectric focussing
-
4.9
Other publictions for EC 1.1.1.76
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)
737478
Xu
Cloning, expression, and chara ...
Bacillus licheniformis
Appl. Biochem. Biotechnol.
178
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-
-
1
-
-
-
7
3
-
3
1
1
-
1
-
-
1
-
-
-
-
-
9
1
1
-
1
3
2
1
-
2
-
-
-
-
-
1
2
-
-
-
-
7
-
3
-
3
1
1
-
-
-
1
-
-
-
-
9
1
1
-
1
3
2
1
-
-
-
-
-
-
3
3
737540
Jojima
Promiscuous activity of (S,S)- ...
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
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99
1427-1433
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-
-
-
-
-
-
-
-
-
-
-
4
-
3
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
739596
Shimegi
Modification of chimeric (2S, ...
Corynebacterium glutamicum
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22
226-233
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-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
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-
-
-
-
-
-
1
-
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-
1
1
-
-
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-
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-
-
-
1
-
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-
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-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
721396
Wang
Characterization of a stereosp ...
Rhodococcus erythropolis, Rhodococcus erythropolis WZ010
Appl. Microbiol. Biotechnol.
98
641-650
2014
-
1
1
-
-
-
-
-
-
-
1
1
1
5
-
-
1
-
-
-
2
-
18
1
2
1
-
-
2
1
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
1
1
1
-
-
1
-
-
2
-
18
1
2
1
-
-
2
1
-
-
-
1
1
-
-
-
737381
Shimegi
Crystallization and preliminar ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
70
461-463
2014
-
-
1
1
-
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
737865
Takeda
Identification and characteriz ...
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Biosci. Biotechnol. Biochem.
78
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2014
-
-
-
-
-
-
-
1
-
-
1
-
-
3
-
-
-
-
-
-
-
-
4
1
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
4
1
-
-
-
1
-
-
-
2
-
-
-
-
1
1
739652
Wang
Engineering of cofactor regene ...
Corynebacterium glutamicum
Sci. Rep.
3
2643
2013
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
1
-
3
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
3
1
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Role of Saccharomyces cerevisi ...
Saccharomyces cerevisiae
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Otagiri
Structural basis for chiral su ...
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389578
Ui
Stereochemical applications of ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
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389579
Otagiri
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Crystallization and preliminar ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
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389580
Takusagawa
Purification and characterizat ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
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65
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2001
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389573
Ui
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Mechanism for the formation of ...
Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063
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1984
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389574
Ui
Separation and qunatitation of ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
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1984
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389575
Ui
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Laboratory-scale production of ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012, Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063, no activity in Pseudomonas sp., no activity in Pseudomonas sp. s4, Paenibacillus polymyxa, Paenibacillus polymyxa IAM 1189, Saccharomyces cerevisiae, Saccharomyces cerevisiae OC-2, Serratia marcescens, Serratia marcescens IAM 1022
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1984
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389576
Voloch
Reduction of acetoin to 2,3-bu ...
Klebsiella pneumoniae
Biotechnol. Bioeng.
25
173-183
1983
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389577
Taylor
Stereoisomeric specificities o ...
Aeromonas hydrophila, Bacillus subtilis, Bacillus subtilis Ford, Enterobacter aerogenes, Paenibacillus polymyxa
Biochim. Biophys. Acta
39
448-457
1960
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