BRENDA - Enzyme Database show
show all sequences of 1.1.1.76

Cloning, expression, and characterization of budC gene encoding meso-2,3-butanediol dehydrogenase from Bacillus licheniformis

Xu, G.C.; Bian, Y.Q.; Han, R.Z.; Dong, J.J.; Ni, Y.; Appl. Biochem. Biotechnol. 178, 604-617 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Bacillus licheniformis
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ag+
strong inhibition
Bacillus licheniformis
Al3+
strong inhibition
Bacillus licheniformis
Cu2+
strong inhibition
Bacillus licheniformis
Fe3+
strong inhibition
Bacillus licheniformis
K+
slight inhibition
Bacillus licheniformis
additional information
not inhibited by EDTA
Bacillus licheniformis
Zn2+
slight inhibition
Bacillus licheniformis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.47
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
7.25
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
72.4
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
slight activation
Bacillus licheniformis
Mn2+
slight activation
Bacillus licheniformis
additional information
not influenced by Ni2+, Ba2+, Li+, Ca2+, and Na+
Bacillus licheniformis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
125000
-
gel filtration
Bacillus licheniformis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S,3S)-butane-2,3-diol + NAD+
Bacillus licheniformis
100% activity
(2S)-acetoin + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus licheniformis
-
-
-
Purification (Commentary)
Commentary
Organism
HisTrap column chromatography and Superdex 200 gel filtration
Bacillus licheniformis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-acetoin + NADH + H+
97% activity compared to diacetyl
737478
Bacillus licheniformis
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
100% activity
737478
Bacillus licheniformis
(2S)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
-
737478
Bacillus licheniformis
?
-
-
-
?
1,2-propanediol + NAD+
0.57% activity compared to (2S,3S)-butane-2,3-diol
737478
Bacillus licheniformis
?
-
-
-
?
2,3-hexanedione + NADH + H+
66% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
2,3-pentanedione + NADH + H+
69% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
3,4-hexanedione + NADH + H+
10% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
diacetyl + NADH + H+
100% activity
737478
Bacillus licheniformis
(2S)-acetoin + NAD+
-
-
-
?
additional information
the enzyme shows no activity toward racemic acetoin in the presence of NAD+ as well as no activity with NADPH, 1,4-butanediol, 2,5-hexanedione, 2,4-pentanedione, 2-butanone, methanol, mannitol, and glycerol
737478
Bacillus licheniformis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 30000, SDS-PAGE
Bacillus licheniformis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
at 50°C, the enzymatic activity drops rapidly to half of its initial activity within 40 min, then further decreases to 20% after 330 min
Bacillus licheniformis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
202
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
591
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
1222
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
for diacetyl reduction
Bacillus licheniformis
10
-
for 2,3-butanediol oxidation
Bacillus licheniformis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4.5
10
the enzyme shows a relatively high activity over a wide pH range from 5.0 to 8.0 for racemic acetoin reduction and more than 60% of activity is retained between pH 4.5 and 10.0
Bacillus licheniformis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus licheniformis
NADH
-
Bacillus licheniformis
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Bacillus licheniformis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Bacillus licheniformis
NADH
-
Bacillus licheniformis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ag+
strong inhibition
Bacillus licheniformis
Al3+
strong inhibition
Bacillus licheniformis
Cu2+
strong inhibition
Bacillus licheniformis
Fe3+
strong inhibition
Bacillus licheniformis
K+
slight inhibition
Bacillus licheniformis
additional information
not inhibited by EDTA
Bacillus licheniformis
Zn2+
slight inhibition
Bacillus licheniformis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.47
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
7.25
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
72.4
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
slight activation
Bacillus licheniformis
Mn2+
slight activation
Bacillus licheniformis
additional information
not influenced by Ni2+, Ba2+, Li+, Ca2+, and Na+
Bacillus licheniformis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
125000
-
gel filtration
Bacillus licheniformis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S,3S)-butane-2,3-diol + NAD+
Bacillus licheniformis
100% activity
(2S)-acetoin + NADH + H+
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
HisTrap column chromatography and Superdex 200 gel filtration
Bacillus licheniformis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-acetoin + NADH + H+
97% activity compared to diacetyl
737478
Bacillus licheniformis
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
100% activity
737478
Bacillus licheniformis
(2S)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
-
737478
Bacillus licheniformis
?
-
-
-
?
1,2-propanediol + NAD+
0.57% activity compared to (2S,3S)-butane-2,3-diol
737478
Bacillus licheniformis
?
-
-
-
?
2,3-hexanedione + NADH + H+
66% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
2,3-pentanedione + NADH + H+
69% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
3,4-hexanedione + NADH + H+
10% activity compared to diacetyl
737478
Bacillus licheniformis
?
-
-
-
?
diacetyl + NADH + H+
100% activity
737478
Bacillus licheniformis
(2S)-acetoin + NAD+
-
-
-
?
additional information
the enzyme shows no activity toward racemic acetoin in the presence of NAD+ as well as no activity with NADPH, 1,4-butanediol, 2,5-hexanedione, 2,4-pentanedione, 2-butanone, methanol, mannitol, and glycerol
737478
Bacillus licheniformis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 30000, SDS-PAGE
Bacillus licheniformis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Bacillus licheniformis
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
at 50°C, the enzymatic activity drops rapidly to half of its initial activity within 40 min, then further decreases to 20% after 330 min
Bacillus licheniformis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
202
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
591
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
1222
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
for diacetyl reduction
Bacillus licheniformis
10
-
for 2,3-butanediol oxidation
Bacillus licheniformis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4.5
10
the enzyme shows a relatively high activity over a wide pH range from 5.0 to 8.0 for racemic acetoin reduction and more than 60% of activity is retained between pH 4.5 and 10.0
Bacillus licheniformis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
16.9
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
81.5
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
432
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
16.9
-
diacetyl
at pH 5.0 and 30°C
Bacillus licheniformis
81.5
-
(R,R)-butane-2,3-diol
at pH 10.0 and 30°C
Bacillus licheniformis
432
-
(2S)-acetoin
at pH 10.0 and 30°C
Bacillus licheniformis
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
604-617
2016
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1
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7
3
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3
1
1
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1
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1
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9
1
1
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1
3
2
1
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2
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1
2
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7
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3
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3
1
1
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1
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9
1
1
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1
3
2
1
-
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-
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3
3
737540
Jojima
Promiscuous activity of (S,S)- ...
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
Appl. Microbiol. Biotechnol.
99
1427-1433
2015
-
-
-
-
-
-
-
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4
-
3
-
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8
-
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1
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1
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4
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8
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739596
Shimegi
Modification of chimeric (2S, ...
Corynebacterium glutamicum
Protein Pept. Lett.
22
226-233
2015
-
-
1
-
-
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1
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1
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1
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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
-
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2
1
-
1
-
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-
1
1
1
-
-
-
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-
-
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-
1
1
1
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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
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1
-
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1
1
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1
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1
1
1
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1
1
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1
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1
1
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-
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-
-
-
-
-
737865
Takeda
Identification and characteriz ...
Mycobacterium sp., Mycobacterium sp. B-009
Biosci. Biotechnol. Biochem.
78
1879-1886
2014
-
-
-
-
-
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1
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1
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3
-
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4
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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4
1
-
-
-
1
-
-
-
2
-
-
-
-
1
1
739652
Wang
Engineering of cofactor regene ...
Corynebacterium glutamicum
Sci. Rep.
3
2643
2013
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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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1
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3
1
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710944
Gonzalez
Role of Saccharomyces cerevisi ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
76
670-679
2010
-
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1
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-
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1
1
-
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-
712019
Otagiri
Structural basis for chiral su ...
Corynebacterium glutamicum
FEBS Lett.
584
219-223
2010
-
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-
1
3
-
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
3
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1
1
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2
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2
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389578
Ui
Stereochemical applications of ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Lett. Appl. Microbiol.
32
93-98
2001
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1
-
-
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-
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9
-
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4
-
6
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2
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1
2
-
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4
-
6
-
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-
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-
389579
Otagiri
-
Crystallization and preliminar ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Protein Pept. Lett.
8
57-61
2001
-
-
1
1
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
2
-
-
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1
-
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1
1
1
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2
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-
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-
-
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-
389580
Takusagawa
Purification and characterizat ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Biosci. Biotechnol. Biochem.
65
1876-1878
2001
1
1
1
-
-
-
9
5
-
6
3
-
-
8
-
-
1
-
-
-
2
-
12
1
-
-
2
-
2
-
1
2
1
1
-
1
1
1
2
-
-
-
-
9
1
5
-
6
3
-
-
-
-
1
-
-
2
-
12
1
-
-
2
-
2
-
1
1
-
-
-
-
-
-
389573
Ui
-
Mechanism for the formation of ...
Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063
J. Ferment. Technol.
62
551-559
1984
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3
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4
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1
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2
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2
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4
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1
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389574
Ui
Separation and qunatitation of ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Agric. Biol. Chem.
48
2837-2838
1984
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1
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6
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1
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1
1
2
-
2
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1
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2
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2
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1
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-
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1
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1
1
2
-
2
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1
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-
389575
Ui
-
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
J. Ferment. Technol.
62
151-156
1984
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-
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1
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18
-
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2
-
4
-
1
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2
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4
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4
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1
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2
-
4
-
1
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2
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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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1
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1
1
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2
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2
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1
1
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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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5
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2
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