BRENDA - Enzyme Database
show all sequences of 1.1.1.4

Cloning, expression and characterization of glycerol dehydrogenase involved in 2,3-butanediol formation in Serratia marcescens H30

Zhang, L.; Xu, Q.; Peng, X.; Xu, B.; Wu, Y.; Yang, Y.; Sun, S.; Hu, K.; Shen, Y.; J. Ind. Microbiol. Biotechnol. 41, 1319-1327 (2014) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene gldA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)
Serratia marcescens
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
inhibits (3S/3R)-acetoin reduction
Serratia marcescens
Fe2+
strongly inhibits (3S/3R)-acetoin reduction by over 85%
Serratia marcescens
Fe3+
strongly inhibits (3S/3R)-acetoin reduction by over 85%
Serratia marcescens
Zn2+
inhibits (3S/3R)-acetoin reduction
Serratia marcescens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
GDH activity is significantly enhanced to 784% for meso-2,3-butanediol oxidation in the presence of Fe2+
Serratia marcescens
Mg2+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
Mn2+
GDH activity is significantly enhanced for (3S/3R)-acetoin reduction in the presence of Mn2+
Serratia marcescens
Na+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
NH4+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39000
-
x * 39000, recombinant enzyme, SDS-PAGE
Serratia marcescens
Organism
Organism
UniProt
Commentary
Textmining
Serratia marcescens
-
-
-
Serratia marcescens H30
-
-
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
10.48
-
crude enzyme, with substrate (3S/3R)-acetoin and NADH at room temperature, pH 8.0, 22°C
Serratia marcescens
20.75
-
purified enzyme, with substrate (3S/3R)-acetoin and NADH at room temperature, pH 8.0, 22°C
Serratia marcescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(3R,3S)-acetoin + NADH
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
740827
Serratia marcescens
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
(3R,3S)-acetoin + NADH
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
740827
Serratia marcescens H30
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
1,4-butanediol + NAD+
low activity
740827
Serratia marcescens
?
-
-
-
r
1,4-butanediol + NAD+
low activity
740827
Serratia marcescens H30
?
-
-
-
r
diacetyl + NADH + H+
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
740827
Serratia marcescens
acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
740827
Serratia marcescens H30
acetoin + NAD+
-
-
-
?
isopropanol + NAD+
low activity
740827
Serratia marcescens
?
-
-
-
r
isopropanol + NAD+
low activity
740827
Serratia marcescens H30
?
-
-
-
r
additional information
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
740827
Serratia marcescens
?
-
-
-
?
additional information
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
740827
Serratia marcescens H30
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 39000, recombinant enzyme, SDS-PAGE
Serratia marcescens
Synonyms
Synonyms
Commentary
Organism
2,3-butanediol dehydrogenase
-
Serratia marcescens
acetoin/diacetyl reductase
-
Serratia marcescens
BDH
-
Serratia marcescens
More
cf. EC 1.1.1.6, glycerol dehydrogenase
Serratia marcescens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
-
Serratia marcescens
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
temperature profile, overview
Serratia marcescens
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
over 60% of maximal activity is retained
Serratia marcescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
diacetyl reduction
Serratia marcescens
8
-
reduction of (3S/3R)-acetoin and oxidations of meso-2,3-butanediol and glycerol
Serratia marcescens
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
9
temperature profile, overview
Serratia marcescens
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Serratia marcescens
NADH
-
Serratia marcescens
Cloned(Commentary) (protein specific)
Commentary
Organism
gene gldA, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3)
Serratia marcescens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Serratia marcescens
NADH
-
Serratia marcescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
inhibits (3S/3R)-acetoin reduction
Serratia marcescens
Fe2+
strongly inhibits (3S/3R)-acetoin reduction by over 85%
Serratia marcescens
Fe3+
strongly inhibits (3S/3R)-acetoin reduction by over 85%
Serratia marcescens
Zn2+
inhibits (3S/3R)-acetoin reduction
Serratia marcescens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
GDH activity is significantly enhanced to 784% for meso-2,3-butanediol oxidation in the presence of Fe2+
Serratia marcescens
Mg2+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
Mn2+
GDH activity is significantly enhanced for (3S/3R)-acetoin reduction in the presence of Mn2+
Serratia marcescens
Na+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
NH4+
enhances (3S/3R)-acetoin reduction
Serratia marcescens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39000
-
x * 39000, recombinant enzyme, SDS-PAGE
Serratia marcescens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
10.48
-
crude enzyme, with substrate (3S/3R)-acetoin and NADH at room temperature, pH 8.0, 22°C
Serratia marcescens
20.75
-
purified enzyme, with substrate (3S/3R)-acetoin and NADH at room temperature, pH 8.0, 22°C
Serratia marcescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(3R,3S)-acetoin + NADH
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
740827
Serratia marcescens
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
(3R,3S)-acetoin + NADH
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
740827
Serratia marcescens H30
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
1,4-butanediol + NAD+
low activity
740827
Serratia marcescens
?
-
-
-
r
1,4-butanediol + NAD+
low activity
740827
Serratia marcescens H30
?
-
-
-
r
diacetyl + NADH + H+
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
740827
Serratia marcescens
acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
740827
Serratia marcescens H30
acetoin + NAD+
-
-
-
?
isopropanol + NAD+
low activity
740827
Serratia marcescens
?
-
-
-
r
isopropanol + NAD+
low activity
740827
Serratia marcescens H30
?
-
-
-
r
additional information
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
740827
Serratia marcescens
?
-
-
-
?
additional information
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
740827
Serratia marcescens H30
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 39000, recombinant enzyme, SDS-PAGE
Serratia marcescens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
-
Serratia marcescens
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
70
temperature profile, overview
Serratia marcescens
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
70
-
over 60% of maximal activity is retained
Serratia marcescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
diacetyl reduction
Serratia marcescens
8
-
reduction of (3S/3R)-acetoin and oxidations of meso-2,3-butanediol and glycerol
Serratia marcescens
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
9
temperature profile, overview
Serratia marcescens
General Information
General Information
Commentary
Organism
evolution
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
Serratia marcescens
General Information (protein specific)
General Information
Commentary
Organism
evolution
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
Serratia marcescens
Other publictions for EC 1.1.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Protein Variants
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
Synonyms
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)
760423
Kuang
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8
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2
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4
-
6
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-
2
-
-
-
17
-
31
-
8
2
-
-
8
2
-
2
6
-
-
-
-
-
2
6
-
-
-
-
-
-
8
-
2
-
4
-
-
-
2
-
-
17
-
31
-
2
-
-
8
2
-
2
-
-
2
2
-
8
8
760761
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Phylogenetics-based identific ...
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-
-
-
-
-
-
-
-
-
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-
-
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-
-
-
-
-
-
-
-
-
-
-
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-
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-
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Engineering of the 2,3-butane ...
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-
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-
-
-
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-
2
-
4
-
-
-
-
-
-
-
-
4
-
2
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
762382
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-
1
-
1
-
-
-
-
1
-
2
-
2
-
-
1
-
-
-
-
-
8
-
5
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
2
-
-
-
1
-
-
-
-
8
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
760463
Gong
-
Cloning, expression and chara ...
Bacillus thuringiensis serovar kurstaki, Bacillus thuringiensis serovar kurstaki ACCC 10066
Biocatal. Agricult. Biotechnol.
22
10137
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1
-
1
-
-
-
2
2
-
1
-
4
-
2
-
-
1
-
-
-
-
1
8
1
3
2
-
1
-
2
-
1
2
-
1
-
1
-
1
2
-
-
-
-
2
-
2
-
1
-
4
-
-
-
1
-
-
-
1
8
1
2
-
1
-
2
-
1
1
-
1
1
-
-
-
761834
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-
-
1
-
1
-
-
-
-
-
-
2
-
5
-
-
-
-
-
-
-
-
2
-
2
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
756608
Liu
2,3-Butanediol catabolism in ...
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Environ. Microbiol.
20
3927-3940
2018
-
-
1
-
-
-
-
1
-
1
-
16
-
11
-
-
-
-
-
-
8
-
48
-
5
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
1
-
16
-
-
-
-
-
-
8
-
48
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
760411
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Paenibacillus brasilensis, Paenibacillus brasilensis PB24
Appl. Microbiol. Biotechnol.
102
8773-8782
2018
-
1
1
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
740952
Liang
Selection of an endogenous 2,3 ...
Escherichia coli, Escherichia coli BW25113
Metab. Eng.
39
181-191
2017
-
-
-
-
-
-
-
2
-
-
-
-
-
32
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
2
-
-
-
-
-
1
1
-
2
2
760716
Yamada
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Bacillus amyloliquefaciens, Bacillus amyloliquefaciens UCMB5033
Biores. Technol.
245
1558-1566
2017
-
-
1
-
1
-
-
-
-
-
-
2
-
3
-
-
-
-
-
1
-
-
2
-
4
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
2
-
-
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-
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-
-
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-
-
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Highly efficient bioreduction ...
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2017
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6
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1
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1
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Li
Reducing diacetyl production ...
Saccharomyces uvarum, Saccharomyces uvarum WY1
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2017
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2
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1
2
2
1
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762259
Zhang
Effect of deletion of 2,3-but ...
Bacillus subtilis, Bacillus subtilis BS168D
Prep. Biochem. Biotechnol.
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2017
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2
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2
2
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737512
Rados
Stereospecificity of Corynebac ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Appl. Microbiol. Biotechnol.
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2016
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10
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1
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4
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1
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10
-
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-
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-
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-
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4
4
737519
de Oliveira
Synthetic operon for (R,R)-2,3 ...
Bacillus subtilis, Bacillus subtilis WN1038
Appl. Microbiol. Biotechnol.
100
719-728
2016
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2
2
1
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2
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2
2
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738345
Ge
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Contracted but effective: Prod ...
Bacillus licheniformis, Bacillus licheniformis MW3
Green Chem.
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4693-4703
2016
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1
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4
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3
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14
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20
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3
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1
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1
1
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4
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1
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14
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20
-
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-
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739694
Bae
Efficient production of acetoi ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Sci. Rep.
6
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2016
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-
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737847
Kang
Enhanced production of 2,3-but ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) BRC1
Bioprocess Biosyst. Eng.
38
299-305
2015
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14
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2
1
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2
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1
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1
1
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4
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1
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2
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1
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-
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14
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1
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-
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2
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-
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738800
Bai
Engineered Serratia marcescens ...
Bacillus subtilis, Serratia marcescens, Bacillus subtilis 168, Serratia marcescens MG1
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12
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4
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4
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2
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12
2
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Zhao
Identification and characteriz ...
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Lett. Appl. Microbiol.
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2015
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1
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2
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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4
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5
1
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1
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1
1
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1
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2
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739127
Yu
Characterization of a (2R,3R)- ...
Rhodococcus erythropolis, Rhodococcus erythropolis WZ010
Molecules
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2015
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1
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4
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3
2
3
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10
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19
2
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2
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2
1
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1
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15
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4
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3
2
3
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19
2
2
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1
4
2
1
-
-
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4
4
739571
Maddock
Substitutions at the cofactor ...
Clostridium autoethanogenum
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7
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2
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7
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21
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3
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21
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21
737501
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Reconstruction of an acetogeni ...
Clostridium autoethanogenum
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5
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6
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738472
Cui
Utilization of excess NADH in ...
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2
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Wang
Glycerol dehydrogenase plays a ...
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1
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8
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1
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1
1
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8
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1
2
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1
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10
1
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8
-
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1
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8
8
738878
Kochius
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Enantioselective enzymatic syn ...
Haloarcula marismortui
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1
1
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1
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738880
Hao
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Biochemical characterization o ...
Bacillus subtilis, Bacillus subtilis 168
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2014
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1
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Zhang
Cloning, expression and charac ...
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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
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2
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1
1
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2
1
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722559
Gao
A 2,3-butanediol dehydrogenase ...
Paenibacillus polymyxa, Paenibacillus polymyxa ZJ-9
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Crystallization and preliminar ...
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721345
Yu
Novel (2R,3R)-2,3-butanediol d ...
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721872
Takeda
Identification and characteriz ...
Mycolicibacterium smegmatis, Mycolicibacterium vanbaalenii, Mycolicibacterium gilvum, Mycobacterium sp., Mycobacterium sp. B-009
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Gonzalez
Role of Saccharomyces cerevisi ...
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Ehsani
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