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Information on EC 1.1.1.76 - (S,S)-butanediol dehydrogenase
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1.1.1.76 (S,S)-butanediol dehydrogenaseIUBMB Comments
This enzyme catalyses the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol. It can also catalyse the irreversible reduction of diacetyl to (S)-acetoin.
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Word Map
- 1.1.1.76
-
brevibacterium
- saccharolyticum
- synthesis
-
klebsiella
-
s-configuration
-
corynebacterium
- pneumoniae
- chimera
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
(2S, 3S)-BDH, (2S, 3S)-butanediol dehydrogenase, (S,S)-2,3-butanediol dehydrogenase, (S,S)-butanediol dehydrogenase, 2,3-BDH, 2,3-butanediol dehydrogenase, acetoin(diacetyl) reductase, AdR, ADS1, ARA1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S,S)-2,3-butanediol dehydrogenase
(S,S)-butanediol dehydrogenase
2,3-butanediol dehydrogenase
acetoin(diacetyl) reductase
AdR
ADS1
BDH
ButA
L(+)-2,3-butanediol dehydrogenase (L-acetoin forming)
-
-
-
-
L-BDH
L-butanediol dehydrogenase
-
-
-
-
L-BDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-butane-2,3-diol + NAD+ = (S)-acetoin + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(S,S)-butane-2,3-diol:NAD+ oxidoreductase
This enzyme catalyses the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol. It can also catalyse the irreversible reduction of diacetyl to (S)-acetoin.
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CAS REGISTRY NUMBER
COMMENTARY
37250-14-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
-
-
-
?
(2S,3S)-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
-
r
(R,S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
(R,S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NADP+
-
-
Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
-
r
1,2-propanediol + NAD+
?
-
0.57% activity compared to (2S,3S)-butane-2,3-diol
-
-
?
1-phenylpropanol + NAD+
1-phenylpropan-1-one + NADH + H+
-
-
-
?
2,3-hexanedione + NADH + H+
?
-
66% activity compared to diacetyl
-
-
?
3,4-hexanedione + NADH + H+
?
-
10% activity compared to diacetyl
-
-
?
diacetyl + NADH + H+
?
-
35% activity in comparison to L-acetoin
-
-
r
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
-
100% activity
-
-
r
meso-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
-
r
meso-2,3-butanediol + NAD+
acetoin + NADH
poor substrate
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
97% activity compared to diacetyl
-
-
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
-
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
100% activity
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
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
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
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
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
-
low activity with 30 mM
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
-
low activity with 30 mM
-
-
?
2,3-pentanedione + NADH + H+
?
-
69% activity compared to diacetyl
-
-
?
2,3-pentanedione + NADH + H+
?
-
7% activity in comparison to L-acetoin
-
-
r
2,3-pentanedione + NADH + H+
?
-
7% activity in comparison to L-acetoin
-
-
r
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
glyceraldehyde + NADH + H+
?
-
low activity with 30 mM
-
-
?
L-acetoin + NADH
L-2,3-butanediol
-
stereoisomeric specifity for hydroxyl group in L configuration
-
?
L-acetoin + NADH
L-2,3-butanediol
-
reaction dependent of substrate concentration, incubation time, glucose addition, aeration
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
no oxidadion of several alcohols
-
r
L-acetoin + NADH
L-2,3-butanediol
-
exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
-
r
L-acetoin + NADH
L-2,3-butanediol
-
in presence of adequate amounts of NAD+ and hydrazine and in an alkaline condition acetoin formation is much in favour, acetoin concentrations have no appreciable influence on dehydrogenation of L-butanediol
-
r
L-acetoin + NADH
L-2,3-butanediol
-
in presence of adequate amounts of NAD+ and hydrazine and in an alkaline condition acetoin formation is much in favour, acetoin concentrations have no appreciable influence on dehydrogenation of L-butanediol
-
r
L-acetoin + NADH
L-2,3-butanediol
-
reaction dependent of substrate concentration, incubation time, glucose addition, aeration
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
no oxidadion of several alcohols
-
r
L-acetoin + NADH
L-2,3-butanediol
-
stereoisomeric specifity for hydroxyl group in L configuration
-
?
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
-
To confirm the high production of enzyme, the conversion of L-acetoin, in a racemic mixture, to L-2,3-butanediol is studied. 0.37% L-2,3-butanediol is formed from 1% L-acetoin added to the culture.
-
-
?
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
-
To confirm the high production of enzyme, the conversion of L-acetoin, in a racemic mixture, to L-2,3-butanediol is studied. 0.37% L-2,3-butanediol is formed from 1% L-acetoin added to the culture.
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
additional information
?
-
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
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
-
-
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
100% activity
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
NAD+
coenzyme binding motif T11G12XXXG16XG18 is conserved in the N-terminal region
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
additional information
Ba2+
-
Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Ca2+
-
Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Co2+
-
Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Mg2+
-
Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Mn2+
-
Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
additional information
-
not influenced by Ni2+, Ba2+, Li+, Ca2+, and Na+
additional information
-
no significant changes in enzyme activity with 5 mM Ni2+, Zn2+ and Cd2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
competitive. In crystal strucuture, the mercaptoethanol molecule is located in the catalytic cleft formed by residues Ser141, Ileu142, Ala143, Phe148, Tyr154, Pro184, Gly185, Ileu186, Met191, Trp192 and Ile195. These residues may also be involved in substrate recognition and in stereospecific redox reactions
additional information
-
slight inhibition of 10-20% by organic acids at concentrations of 5 mM: lactate, pyruvate, succinate, acetate and formate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
Ba2+, Ca2+, Mn2+, Mg2+ and Co2+ activate enzyme 1.6-1.8 fold at a concentration of 5 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17
-
plasmid containing tac promoter and L-butanediol dehydrogenase ORF
18.6
-
plasmid containing meso-butanediol dehydrogenase promoter region and L-butanediol dehydrogenase ORF
269
purified recombinant enzyme, (2S,3S)-2,3-butanediol oxidation, pH 9.5, 25°C
8519
purified recombinant enzyme, diacetyl reduction, pH 7.0, 30°C
additional information
additional information
-
highest specific activities without glucose addition to culture medium, induction with 0.25 mg/ml isopropyl-beta-thiogalactopyranosid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 8724, glucose-grown cells contain L-2,3-butanediol dehydrogenase
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
-
deletion of BDH1 results in an accumulation of acetoin and a diminution of 2,3-butanediol in two Saccharomyces cerevisiae strains under two different growth conditions
evolution
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
evolution
-
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A518DLI5_9BACT
261
0
28093
TrEMBL
-
A0A292ZI70_SPHSA
Sphingobium fuliginis (strain ATCC 27551)
262
0
27383
TrEMBL
-
A0A1Y0Y6Y7_ACEPA
335
1
35662
TrEMBL
-
A0A1S7NF72_9RHIZ
261
0
27991
TrEMBL
-
A0A1U9Z3A4_9RHIZ
259
0
27665
TrEMBL
-
A0A2N9BJQ2_STRCX
254
0
26233
TrEMBL
-
A0A087AKV3_9BIFI
123
0
13160
TrEMBL
-
A0A2H1L066_9MICO
70
0
7679
TrEMBL
-
A0A1S7P3U0_9RHIZ
261
0
28112
TrEMBL
-
A0A1L3LBY6_9RHIZ
261
0
27407
TrEMBL
-
A0A2H1K0J0_BRELN
261
0
27035
TrEMBL
-
A0A1S7R6G0_9RHIZ
261
0
28141
TrEMBL
-
A0A1S7NX99_9RHIZ
261
0
28070
TrEMBL
-
A0A1S7TDU4_RHIRD
261
0
27991
TrEMBL
-
A0A6J4P605_9ACTN
264
0
28050
TrEMBL
-
A0A1S7NFG4_9RHIZ
261
0
27963
TrEMBL
-
A0A1S7NVJ9_9RHIZ
261
0
27935
TrEMBL
-
A0A087A4R7_9BIFI
275
0
29209
TrEMBL
-
A0A1S7TJQ8_9RHIZ
261
0
28086
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27107
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
30000
30000
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
tetramer
tetramer
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
tetramer
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method with polyethylene glycol 4000 as precipitant
-
hanging drop vapor diffusion method, using 17% (w/v) PEG 4000, 15% (v/v) glycerol and 1% (v/v) beta-mercaptoethanol in 100 mM MES buffer pH 6.4
-
in complex with NAD+ and 2-mercaptoethanol, to 2.0 A resolution. The L-BDH subunit is composed of seven beta-strands, six alpha-helices and two short a helices, aFG1 and aFG2, which form a small lobe on top of the core domain. The conserved active site residues Asn112, Ser141, Tyr154 and Lys158 are located near the NAD+ molecule
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
up to, rapidly inactivated over 40°C, 30 min incubation before the enzyme assay
37 - 40
-
The enzyme is stable up to 37°C but rapidly inactivated over 40°C
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
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
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
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
streptomycin sulfate precipitation, affinity chromatography, gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expressed with glucose dehydrogenase and formate dehydrogenase in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli JM109, stereospecifity of resulting L-butanediol dehydrogenase is reduced. Expressed gene contains tac-promoter and upstream region of the meso-butanediol dehydrogenase gene of Klebsiella pneumoniae IAM1063. A more stable stereospecifity is exhibited
-
L-butanediol gene containing plasmid pLBD2-CTC is expressed in Escherichia coli JM109
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
When the enzyme gene is only expressed in Escherichia coli using the tac promoter, the stereospecificity of resulting enzyme gene is reduced. When the region upstream of the meso-butanediol dehydrogenase gene of Klebsiella pneumoniae is also involved in the expression of gene, the resulting enzyme exhibits more stable stereospecificity.
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
synthesis
the key enzymes in the microbial production of 2,3-butanediol
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
-
synthesis
-
the key enzymes in the microbial production of 2,3-butanediol
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ui, S.; Matsuyama, N.; Masuda, H.; Muraki, H.
Mechanism for the formation of 2,3-butanediol stereoisomers in Klebsiella pneumoniae
J. Ferment. Technol.
62
551-559
1984
Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063
-
brenda
Ui, S.; Masuda, H.; Muraki, H.
Separation and quantitation of 2,3-butanediol isomers ((-), (+), and meso) by a combined use of enzyme and gas chromatography
Agric. Biol. Chem.
48
2837-2838
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
brenda
Ui, S.; Masuda, H.; Muraki, H.
Laboratory-scale production of acetoin isomers (D(-) and L(+)) by bacterial fermentation
J. Ferment. Technol.
62
151-156
1984
Paenibacillus polymyxa, Corynebacterium glutamicum, Saccharomyces cerevisiae, Klebsiella pneumoniae, no activity in Pseudomonas sp., Serratia marcescens, Paenibacillus polymyxa IAM 1189, Corynebacterium glutamicum C-1012, Klebsiella pneumoniae IAM 1063, Saccharomyces cerevisiae OC-2, Serratia marcescens IAM 1022, no activity in Pseudomonas sp. s4
-
brenda
Voloch, M.; Ladisch, M.R.; Rodwell, V.W.; Tsao, G.T.
Reduction of acetoin to 2,3-butanediol in Klebsiella pneumoniae: a new model
Biotechnol. Bioeng.
25
173-183
1983
Klebsiella pneumoniae
brenda
Taylor, M.B.; Juni, E.
Stereoisomeric specificities of 2,3-butanediol dehydrogenase
Biochim. Biophys. Acta
39
448-457
1960
Klebsiella aerogenes, Aeromonas hydrophila, Bacillus subtilis, Paenibacillus polymyxa, Bacillus subtilis Ford
brenda
Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Stereochemical applications of the expression of the L-2,3-butanediol dehydrogenase gene in Escherichia coli
Lett. Appl. Microbiol.
32
93-98
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
brenda
Otagiri, M.; Kurisu, G.; Ui, S.; Ohkuma, M.; Kudo, T.; Kusunoki, M.
Crystallization and preliminary x-ray studies of L-(+)-2,3-butanediol dehydrogenase from Brevibacterium saccharolyticum C-1012
Protein Pept. Lett.
8
57-61
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
brenda
Takusagawa, Y.; Otagiri, M.; Ui, S.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
65
1876-1878
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
brenda
Gonzalez, E.; Fernandez, M.R.; Marco, D.; Calam, E.; Sumoy, L.; Pares, X.; Dequin, S.; Biosca, J.A.
Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol
Appl. Environ. Microbiol.
76
670-679
2010
Saccharomyces cerevisiae
brenda
Otagiri, M.; Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.
Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
FEBS Lett.
584
219-223
2010
Corynebacterium glutamicum (Q9ZNN8)
brenda
Wang, Z.; Song, Q.; Yu, M.; Wang, Y.; Xiong, B.; Zhang, Y.; Zheng, J.; Ying, X.
Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol
Appl. Microbiol. Biotechnol.
98
641-650
2014
Rhodococcus erythropolis (M4N626), Rhodococcus erythropolis, Rhodococcus erythropolis WZ010 (M4N626), Rhodococcus erythropolis WZ010
brenda
Shimegi, T.; Ooyama, T.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.; Ui, S.
Crystallization and preliminary X-ray diffraction analysis of domain-chimeric L-(2S,3S)-butanediol dehydrogenase
Acta Crystallogr. Sect. F
70
461-463
2014
Corynebacterium glutamicum
brenda
Xu, G.C.; Bian, Y.Q.; Han, R.Z.; Dong, J.J.; Ni, Y.
Cloning, expression, and characterization of budC gene encoding meso-2,3-butanediol dehydrogenase from Bacillus licheniformis
Appl. Biochem. Biotechnol.
178
604-617
2016
Bacillus licheniformis
brenda
Jojima, T.; Igari, T.; Moteki, Y.; Suda, M.; Yukawa, H.; Inui, M.
Promiscuous activity of (S,S)-butanediol dehydrogenase is responsible for glycerol production from 1,3-dihydroxyacetone in Corynebacterium glutamicum under oxygen-deprived conditions
Appl. Microbiol. Biotechnol.
99
1427-1433
2015
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
brenda
Takeda, M.; Anamizu, S.; Motomatsu, S.; Chen, X.; Thapa Chhetri, R.
Identification and characterization of a mycobacterial NAD+-dependent alcohol dehydrogenase with superior reduction of diacetyl to (S)-acetoin
Biosci. Biotechnol. Biochem.
78
1879-1886
2014
Mycobacterium sp. (W8VSK8), Mycobacterium sp., Mycobacterium sp. B-009 (W8VSK8)
brenda
Shimegi, T.; Mochizuki, K.; Oyama, T.; Ohtsuki, T.; Kusunoki, M.; Ui, S.
Modification of chimeric (2S, 3S)-butanediol dehydrogenase based on structural information
Protein Pept. Lett.
22
226-233
2015
Corynebacterium glutamicum
brenda
Wang, Y.; Li, L.; Ma, C.; Gao, C.; Tao, F.; Xu, P.
Engineering of cofactor regeneration enhances (2S,3S)-2,3-butanediol production from diacetyl
Sci. Rep.
3
2643
2013
Corynebacterium glutamicum
brenda
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