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Enzyme Nomenclature
Information on EC 1.1.1.76 - (S,S)-butanediol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.76
Word Map on EC 1.1.1.76
- 1.1.1.76
-
brevibacterium
- saccharolyticum
-
klebsiella
-
s-configuration
-
corynebacterium
- pneumoniae
-
chiral
-
chimera
-
short-chain
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.76
-
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RECOMMENDED NAME
GeneOntology No.
(S,S)-butanediol dehydrogenase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 8724, glucose-grown cells contain L-2,3-butanediol dehydrogenase
-
-
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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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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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
M4N626
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+
coenzyme binding motif T11G12XXXG16XG18 is conserved in the N-terminal region
NAD+
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
Mg2+
-
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Mn2+
additional information
Co2+
-
; 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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INHIBITORS
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
-
oxidation of L-butanediol; oxidation of (S,S)-butane-2,3-diol
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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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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
tetramer
tetramer
-
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
tetramer
-
4 * 30000, SDS-PAGE; 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; X-ray analysis
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 40
-
The enzyme is stable up to 37°C but rapidly inactivated over 40°C
37
-
up to, rapidly inactivated over 40°C, 30 min incubation before the enzyme assay
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 enzyme; streptomycin sulfate precipitation, affinity chromatography, gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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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; 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.
-
expression in Escherichia coli JM109/pLBD2-CTC; 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)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.76)
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