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show all sequences of 1.1.1.76

Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol

Wang, Z.; Song, Q.; Yu, M.; Wang, Y.; Xiong, B.; Zhang, Y.; Zheng, J.; Ying, X.; Appl. Microbiol. Biotechnol. 98, 641-650 (2014)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
the key enzymes in the microbial production of 2,3-butanediol
Rhodococcus erythropolis
Cloned(Commentary)
Commentary
Organism
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Rhodococcus erythropolis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26864
-
2 * 26864, sequence calculation
Rhodococcus erythropolis
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+
Rhodococcus erythropolis
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
(S)-acetoin + NADH + H+
-
-
r
Organic Solvent Stability
Organic Solvent
Commentary
Organism
DMSO
the enzyme exhibits remarkable tolerance to dimethyl sulfoxide and retains 53.6% of the initial activity after 4 h incubation with 30% v/v DMSO
Rhodococcus erythropolis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodococcus erythropolis
M4N626
-
-
Rhodococcus erythropolis WZ010
M4N626
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Rhodococcus erythropolis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
269
-
purified recombinant enzyme, (2S,3S)-2,3-butanediol oxidation, pH 9.5, 25°C
Rhodococcus erythropolis
8519
-
purified recombinant enzyme, diacetyl reduction, pH 7.0, 30°C
Rhodococcus erythropolis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S,3S)-butane-2,3-diol + NAD+
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
721396
Rhodococcus erythropolis
(S)-acetoin + NADH + H+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Under the optimized conditions, the activity of diacetyl reduction is 11.9fold higher than that of (2S,3S)-2,3-butanediol oxidation
721396
Rhodococcus erythropolis
(S)-acetoin + NADH + H+
-
-
-
r
(S)-1-phenylethanol + NAD+
-
721396
Rhodococcus erythropolis
acetophenone + NADH + H+
-
-
-
r
1,2-propanediol + NAD+
-
721396
Rhodococcus erythropolis
? + NADH + H+
-
-
-
?
1-butanol + NAD+
-
721396
Rhodococcus erythropolis
butanal + NADH + H+
-
-
-
?
1-butanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
butanal + NADH + H+
-
-
-
?
1-phenylpropanol + NAD+
-
721396
Rhodococcus erythropolis
1-phenylpropanal + NADH + H+
-
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
-
721396
Rhodococcus erythropolis
? + NAD+
-
-
-
?
2-butanol + NAD+
-
721396
Rhodococcus erythropolis
2-butanone + NADH + H+
-
-
-
?
2-butanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
2-butanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
-
721396
Rhodococcus erythropolis
2-pentanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
2-pentanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
-
721396
Rhodococcus erythropolis
cyclohexanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
cyclohexanone + NADH + H+
-
-
-
?
ethyl pyruvate + NADH + H+
-
721396
Rhodococcus erythropolis
? + NAD+
-
-
-
?
isopropanol + NAD+
-
721396
Rhodococcus erythropolis
isopropanal + NADH + H+
-
-
-
?
additional information
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
721396
Rhodococcus erythropolis
?
-
-
-
-
additional information
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
721396
Rhodococcus erythropolis WZ010
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homodimer
2 * 26864, sequence calculation
Rhodococcus erythropolis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
(2S,3S)-2,3-butanediol oxidation
Rhodococcus erythropolis
30
-
diacetyl reduction
Rhodococcus erythropolis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
10
50
activity range
Rhodococcus erythropolis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
diacetyl reduction
Rhodococcus erythropolis
9.5
-
(2S,3S)-2,3-butanediol oxidation
Rhodococcus erythropolis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.1
11
activity range
Rhodococcus erythropolis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
coenzyme binding motif T11G12XXXG16XG18 is conserved in the N-terminal region
Rhodococcus erythropolis
Application (protein specific)
Application
Commentary
Organism
synthesis
the key enzymes in the microbial production of 2,3-butanediol
Rhodococcus erythropolis
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Rhodococcus erythropolis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
coenzyme binding motif T11G12XXXG16XG18 is conserved in the N-terminal region
Rhodococcus erythropolis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26864
-
2 * 26864, sequence calculation
Rhodococcus erythropolis
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+
Rhodococcus erythropolis
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
(S)-acetoin + NADH + H+
-
-
r
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
DMSO
the enzyme exhibits remarkable tolerance to dimethyl sulfoxide and retains 53.6% of the initial activity after 4 h incubation with 30% v/v DMSO
Rhodococcus erythropolis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Rhodococcus erythropolis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
269
-
purified recombinant enzyme, (2S,3S)-2,3-butanediol oxidation, pH 9.5, 25°C
Rhodococcus erythropolis
8519
-
purified recombinant enzyme, diacetyl reduction, pH 7.0, 30°C
Rhodococcus erythropolis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S,3S)-butane-2,3-diol + NAD+
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
721396
Rhodococcus erythropolis
(S)-acetoin + NADH + H+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Under the optimized conditions, the activity of diacetyl reduction is 11.9fold higher than that of (2S,3S)-2,3-butanediol oxidation
721396
Rhodococcus erythropolis
(S)-acetoin + NADH + H+
-
-
-
r
(S)-1-phenylethanol + NAD+
-
721396
Rhodococcus erythropolis
acetophenone + NADH + H+
-
-
-
r
1,2-propanediol + NAD+
-
721396
Rhodococcus erythropolis
? + NADH + H+
-
-
-
?
1-butanol + NAD+
-
721396
Rhodococcus erythropolis
butanal + NADH + H+
-
-
-
?
1-butanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
butanal + NADH + H+
-
-
-
?
1-phenylpropanol + NAD+
-
721396
Rhodococcus erythropolis
1-phenylpropanal + NADH + H+
-
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
-
721396
Rhodococcus erythropolis
? + NAD+
-
-
-
?
2-butanol + NAD+
-
721396
Rhodococcus erythropolis
2-butanone + NADH + H+
-
-
-
?
2-butanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
2-butanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
-
721396
Rhodococcus erythropolis
2-pentanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
2-pentanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
-
721396
Rhodococcus erythropolis
cyclohexanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
-
721396
Rhodococcus erythropolis WZ010
cyclohexanone + NADH + H+
-
-
-
?
ethyl pyruvate + NADH + H+
-
721396
Rhodococcus erythropolis
? + NAD+
-
-
-
?
isopropanol + NAD+
-
721396
Rhodococcus erythropolis
isopropanal + NADH + H+
-
-
-
?
additional information
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
721396
Rhodococcus erythropolis
?
-
-
-
-
additional information
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
721396
Rhodococcus erythropolis WZ010
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 26864, sequence calculation
Rhodococcus erythropolis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
(2S,3S)-2,3-butanediol oxidation
Rhodococcus erythropolis
30
-
diacetyl reduction
Rhodococcus erythropolis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
10
50
activity range
Rhodococcus erythropolis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
diacetyl reduction
Rhodococcus erythropolis
9.5
-
(2S,3S)-2,3-butanediol oxidation
Rhodococcus erythropolis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.1
11
activity range
Rhodococcus erythropolis
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
Rhodococcus erythropolis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
Rhodococcus erythropolis
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
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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
-
1
3
2
1
-
2
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1
2
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7
-
3
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3
1
1
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1
-
-
-
-
9
1
1
-
1
3
2
1
-
-
-
-
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3
3
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Promiscuous activity of (S,S)- ...
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1427-1433
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-
-
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-
-
-
-
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4
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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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-
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-
-
-
-
-
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739596
Shimegi
Modification of chimeric (2S, ...
Corynebacterium glutamicum
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226-233
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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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-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
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1
-
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1
1
1
-
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-
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1
1
-
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1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
737865
Takeda
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Mycobacterium sp., Mycobacterium sp. B-009
Biosci. Biotechnol. Biochem.
78
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-
-
-
-
-
-
-
1
-
-
1
-
-
3
-
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4
1
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1
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2
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1
-
-
1
-
-
-
-
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-
-
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-
4
1
-
-
-
1
-
-
-
2
-
-
-
-
1
1
739652
Wang
Engineering of cofactor regene ...
Corynebacterium glutamicum
Sci. Rep.
3
2643
2013
-
-
1
-
-
-
-
-
-
-
-
1
-
1
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-
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1
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3
1
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1
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1
1
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1
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-
1
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710944
Gonzalez
Role of Saccharomyces cerevisi ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
76
670-679
2010
-
-
-
-
-
-
-
-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
1
1
-
-
-
712019
Otagiri
Structural basis for chiral su ...
Corynebacterium glutamicum
FEBS Lett.
584
219-223
2010
-
-
-
1
3
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
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-
-
1
-
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-
-
1
3
-
-
1
1
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-
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-
-
-
-
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-
2
-
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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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.
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57-61
2001
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389580
Takusagawa
Purification and characterizat ...
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Biosci. Biotechnol. Biochem.
65
1876-1878
2001
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389573
Ui
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Mechanism for the formation of ...
Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063
J. Ferment. Technol.
62
551-559
1984
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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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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
J. Ferment. Technol.
62
151-156
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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