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Information on EC 1.1.1.76 - (S,S)-butanediol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.76
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.76 (S,S)-butanediol dehydrogenase
IUBMB 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.76
- saccharolyticum
-
s-acetoin
-
brevibacterium
- synthesis
-
corynebacterium
-
klebsiella
- pneumoniae
-
s-configuration
- chimera
showSynonyms
l-bdh, 2,3-bdh, (s,s)-butanediol dehydrogenase, acetoin(diacetyl) reductase, s-2,3-butanediol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(2R,3R)-2,3-BDH
(2R,3R)-2,3-butanediol dehydrogenase
(S,S)-2,3-butanediol dehydrogenase
(S,S)-butanediol dehydrogenase
2,3-butanediol dehydrogenase
acetoin(diacetyl) reductase
AdR
BDH
budC
ButA
L(+)-2,3-butanediol dehydrogenase (L-acetoin forming)
-
-
-
-
L-BDH
L-butanediol dehydrogenase
-
-
-
-
S-2,3-butanediol dehydrogenase
additional information
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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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(S,S)-butanediol biosynthesis, (S,S)-butanediol degradation
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
Products: -
?
(2S,3S)-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
Substrates: -
Products: selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
Products: 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+
Substrates: -
Products: -
Products: -
r
(R,S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NADP+
-
Substrates: -
Products: Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
Products: Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
r
1,2-propanediol + NAD+
?
-
Substrates: 0.57% activity compared to (2S,3S)-butane-2,3-diol
Products: -
Products: -
?
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
?
2 diacetyl + 2 NADH + 2 H+
(3S)-acetoin + (2S,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
Products: -
?
2 rac acetoin + 2 NADH + 2 H+
(2S,3S)-butane-2,3-diol + (2R,3S)-butane-2,3-diol + 2 NAD+
-
Substrates: -
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
2,3-hexanedione + NADH + H+
?
-
Substrates: 66% activity compared to diacetyl
Products: -
Products: -
?
2-pentanol + NAD+
2-pentanone + NADH + H+
Substrates: -
Products: -
Products: -
?
3,4-hexanedione + NADH + H+
?
-
Substrates: 10% activity compared to diacetyl
Products: -
Products: -
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
Substrates: -
Products: -
Products: -
?
ethyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
isopropanol + NAD+
isopropanal + NADH + H+
Substrates: -
Products: -
Products: -
?
meso-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
Substrates: -
Products: selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
Products: selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
r
meso-2,3-butanediol + NAD+
acetoin + NADH
Substrates: poor substrate
Products: -
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: preferred substrate
Products: -
Products: -
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
Substrates: 97% activity compared to diacetyl
Products: -
Products: -
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
Products: -
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: stereoselective interconversion
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
Substrates: -
Products: -
Products: -
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
1,2-propanediol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
1,2-propanediol + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
?
1,3-dihydroxyacetone + NADH + H+
?
-
Substrates: low activity with 30 mM
Products: -
Products: -
?
1,3-dihydroxyacetone + NADH + H+
?
-
Substrates: low activity with 30 mM
Products: -
Products: -
?
1-phenylpropanol + NAD+
1-phenylpropan-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
1-phenylpropanol + NAD+
1-phenylpropan-1-one + NADH + H+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADH + H+
?
-
Substrates: 69% activity compared to diacetyl
Products: -
Products: -
?
2,3-pentanedione + NADH + H+
?
-
Substrates: 7% activity in comparison to L-acetoin
Products: -
Products: -
r
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
2-butanol + NAD+
2-butanone + NADH + H+
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
diacetyl + NADH
L-acetoin + NAD+
-
Substrates: also reduction of 2,3-pentanedione
Products: -
Products: -
?
diacetyl + NADH
L-acetoin + NAD+
-
Substrates: also reduction of 2,3-pentanedione
Products: -
Products: -
?
diacetyl + NADH
L-acetoin + NAD+
-
Substrates: -
Products: -
Products: -
ir
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
Substrates: 100% activity
Products: -
Products: -
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
Substrates: -
Products: -
Products: -
?
diacetyl + NADH + H+
?
-
Substrates: 35% activity in comparison to L-acetoin
Products: -
Products: -
r
diacetyl + NADH + H+
?
-
Substrates: 35% activity in comparison to L-acetoin
Products: -
Products: -
r
glyceraldehyde + NADH + H+
?
-
Substrates: low activity with 30 mM
Products: -
Products: -
?
glyceraldehyde + NADH + H+
?
-
Substrates: low activity with 30 mM
Products: -
Products: -
?
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: stereoisomeric specificity for hydroxyl group in L configuration
Products: -
Products: -
?
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: reaction dependent of substrate concentration, incubation time, glucose addition, aeration
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: short chain dehydrogenase reductase family
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: no oxidadion of several alcohols
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: 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
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: 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
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: reaction dependent of substrate concentration, incubation time, glucose addition, aeration
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: short chain dehydrogenase reductase family
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: short chain dehydrogenase reductase family
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: no oxidadion of several alcohols
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: stereoisomeric specificity for hydroxyl group in L configuration
Products: -
Products: -
?
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: -
Products: -
Products: -
r
L-acetoin + NADH
L-2,3-butanediol
-
Substrates: -
Products: -
Products: -
r
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
-
Substrates: 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.
Products: -
Products: -
?
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
-
Substrates: 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.
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propane-1,2-diol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the meso-2,3-butanediol dehydrogenase from Klebsiella pneumoniae is active with meso-2,3-butanediol, but also with (2S,3S)-butane-2,3-diol converting them to (3R)-acetoin and (3S)-acetoin, respectively. Additionally the enzyme also has diacetyl reductase [(S)-acetoin forming] activity (EC 1.1.1.304)
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: although the gene encoding (S,S)-2,3-butanediol dehydrogenase is found in the genome of Paenibacillus brasilensis strain PB24, only R,R-2,3-butanediol ((R,R)-2,3-butanediol dehydrogenase, EC 1.1.1.4) and meso-2,3-butanediol are detected by gas chromatography under the growth conditions (modified YEPD medium, pH 6.3, 32°C, up to 72 h)
Products: -
Products: -
?
additional information
?
-
-
Substrates: although the gene encoding (S,S)-2,3-butanediol dehydrogenase is found in the genome of Paenibacillus brasilensis strain PB24, only R,R-2,3-butanediol ((R,R)-2,3-butanediol dehydrogenase, EC 1.1.1.4) and meso-2,3-butanediol are detected by gas chromatography under the growth conditions (modified YEPD medium, pH 6.3, 32°C, up to 72 h)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with (2R,3R)-butane-2,3-diol and (2R,3S)-butane-2,3-diol, and no activity with 1,3-butanediol, 1,2-pentanediol, 1,3-propanediol, and glycerol in the oxidation reaction. No activity with 2,4-pentanedione, butanone, 2,5-hexanedione, and 1,3-dihydroxypropanone in the reduction reaction. Substrate specificity, overview. (2S,3S)-2,3-BDH reduces diacetyl into (3S)-acetoin and (2S,3S)-2,3-BD, while racemic acetoin is reduced to form (2S,3S)-2,3-BD and meso-2,3-BD
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: meso-2,3-BDH from Serratia sp. T241 exhibits higher catalytic efficiency compared with the meso-2,3-BDHs from Klebsiella pneumoniae strain XJ-Li and Serratia marcescens strain H30. No activity is detected for (2R,3R)-2,3-BD as substrate by meso-2,3-BDH, but meso-2,3-BDH from Serratia sp. T241 can efficiently convert (2S,3S)-2,3-BD and meso-2,3-BD into (3S)-acetoin and (3R)-acetoin, respectively
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
Products: -
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: 100% activity
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: 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
Products: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 structure, 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
6.26
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant wild-type enzyme
7.45
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212Y
10.2
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212W
10.86
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant N146Q
23.95
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212S
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.56
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212W
0.56
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212S
0.81
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant N146Q
3.51
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant wild-type enzyme
11.06
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212Y
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212S
0.055
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212W
0.075
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant N146Q
0.56
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant wild-type enzyme
1.49
(2S,3S)-butane-2,3-diol
pH 8.0, 25°C, recombinant mutant F212Y
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
identification of the the active tunnel of meso-2,3-BDH. The two short alpha-helices positioned away from the alpha4-helix possibly expose the hydrophobic ligand-binding cavity, gating the exit of product and cofactor from the activity pocket. AC binds in the active pocket including Ser139, Gln140, Ala141, Leu149, Tyr152, Gly183, Ile184, and Trp190. Residues Phe212 and Asn146 function as the key product-release sites. Three catalytic residues are Ser139, Tyr152, and Lys156. Docking study using the structure of meso-2,3-BDH (PDB ID 1GEG), molecular dynamics simulation
evolution
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
evolution
the enzyme belongs to the short-chain dehydrogenases/reductases
evolution
-
the enzyme belongs to the family of the short-chain dehydrogenase/reductases
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of (2S,3S)-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The disruption of locus pa4148, encoding (2S,3S)-2,3-BDH, partially impairs the growth of this strain in (2S,3S)-2,3-BD but does not affect its growth in (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4148 mutant strain with its gene successfully restores the growth ability. The DELTApa4148 PAO1 strain can grow in racemic acetoin, indicating that (2S,3S)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
metabolism
-
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
2,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
metabolism
-
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
-
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
physiological function
-
besides encoding diacetyl reductase, the butA gene is also responsible for the expression of S-2,3-butanediol dehydrogenase, which may direct the pathway for production of S,S-2,3-BDO and meso-2,3-BDO
physiological function
the meso-2,3-butanediol dehydrogenase (meso-2,3-BDH) catalyzes NAD+-dependent conversion of meso-2,3-butanediol to acetoin (AC), a crucial external energy storage molecule in fermentive bacteria. The interconversion between (3R)-AC and meso-2,3-BD or (3S)-AC and (2S,3S)-2,3-BD is catalyzed by meso-2,3-butanediol dehydrogenase (meso-2,3-BDH)
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
2,3-butanediol (2,3-BD) is a primary microbial metabolite that enhances the virulence of Pseudomonas aeruginosa and alters the lung microbiome. 2,3-BD exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD
-
physiological function
-
besides encoding diacetyl reductase, the butA gene is also responsible for the expression of S-2,3-butanediol dehydrogenase, which may direct the pathway for production of S,S-2,3-BDO and meso-2,3-BDO
-
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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). M4N626_RHOER
259
0
26864
TrEMBL
other Location (Reliability: 2)
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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
F212S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
F212W
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
F212Y
site-directed mutagenesis, the kcat of the mutant is enhanced 4-8fold compared to wild-type
N146Q
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
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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
recombinant SUMO-His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21-Gold by affinity chromatography, desalting gel filtration, and protease-mediated tag cleavage
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, stereospecificity 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 stereospecificity is exhibited
-
gene budC, recombinant expression of SUMO-His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold from plasmid pET28a-SUMO-KpBDH
gene mbdh, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
-
genetic structure of the 2,3-BD utilization operon in Pseudomonas aeruginosa strain PAO1 and comparisons, overview
-
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
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
-
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
Aeromonas hydrophila, Bacillus subtilis, Bacillus subtilis Ford, Klebsiella aerogenes, Paenibacillus polymyxa
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.
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
Guo, Z.; Zhao, X.; He, Y.; Yang, T.; Gao, H.; Li, G.; Chen, F.; Sun, M.; Lee, J.K.; Zhang, L.
Efficient (3R)-acetoin production from meso-2,3-butanediol using a new whole-cell biocatalyst with co-expression of meso-2,3-butanediol dehydrogenase, NADH oxidase and Vitreoscilla hemoglobin
J. Microbiol. Biotechnol.
27
92-100
2016
Serratia sp. T241
brenda
Liu, Q.; Liu, Y.; Kang, Z.; Xiao, D.; Gao, C.; Xu, P.; Ma, C.
2,3-Butanediol catabolism in Pseudomonas aeruginosa PAO1
Environ. Microbiol.
20
3927-3940
2018
Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692, Pseudomonas aeruginosa DSM 22644, Pseudomonas aeruginosa CIP 104116, Pseudomonas aeruginosa JCM 14847, Pseudomonas aeruginosa LMG 12228, Pseudomonas aeruginosa 1C, Pseudomonas aeruginosa PRS 101
brenda
Dias, B.D.C.; Lima, M.E.D.N.V.; Vollu, R.E.; da Mota, F.F.; da Silva, A.J.R.; de Castro, A.M.; Freire, D.M.G.; Seldin, L.
2,3-Butanediol production by the non-pathogenic bacterium Paenibacillus brasilensis
Appl. Microbiol. Biotechnol.
102
8773-8782
2018
Paenibacillus brasilensis, Paenibacillus brasilensis PB24
brenda
Pu, Z.; Ji, F.; Wang, J.; Zhang, Y.; Sun, W.; Bao, Y.
Rational design of meso-2,3-butanediol dehydrogenase by molecular dynamics simulation and experimental evaluations
FEBS Lett.
591
3402-3413
2017
Klebsiella pneumoniae (Q48436)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.76)
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