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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(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
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
?
-
-
-
-
?
(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
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
1,2-propanediol + NAD+
?
-
0.57% activity compared to (2S,3S)-butane-2,3-diol
-
-
?
1,2-propanediol + NAD+
? + NADH + H+
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
1-butanol + NAD+
butanal + NADH + H+
1-hydroxy-2-butanone + NADH + H+
? + NAD+
1-phenylpropanol + NAD+
1-phenylpropan-1-one + NADH + H+
-
-
-
?
2 diacetyl + 2 NADH + 2 H+
(3S)-acetoin + (2S,3S)-butane-2,3-diol + NAD+
-
-
-
-
?
2 rac acetoin + 2 NADH + 2 H+
(2S,3S)-butane-2,3-diol + (2R,3S)-butane-2,3-diol + 2 NAD+
-
-
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
? + NAD+
-
-
-
?
2,3-hexanedione + NADH + H+
?
-
66% activity compared to diacetyl
-
-
?
2,3-pentandione + NADH + H+
? + NAD+
-
-
-
-
?
2,3-pentanedione + NADH + H+
?
2-butanol + NAD+
2-butanone + NADH + H+
2-pentanol + NAD+
2-pentanone + NADH + H+
3,4-hexanedione + NADH + H+
?
-
10% activity compared to diacetyl
-
-
?
butane-1,2-diol + NAD+
? + NADH + H+
-
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
diacetyl + NADH
L-acetoin + NAD+
diacetyl + NADH + H+
(2S)-acetoin + NAD+
diacetyl + NADH + H+
?
-
35% activity in comparison to L-acetoin
-
-
r
ethyl pyruvate + NADH + H+
? + NAD+
-
-
-
?
glyceraldehyde + NADH + H+
?
isopropanol + NAD+
isopropanal + NADH + H+
-
-
-
?
L-acetoin + NADH
L-2,3-butanediol
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
-
100% activity
-
-
r
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
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
-
-
?
n-butanal + NADH + H+
? + NAD+
-
-
-
-
?
propane-1,2-diol + NAD+
? + NADH + H+
-
-
-
-
?
additional information
?
-
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
preferred substrate
-
-
r
(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+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
stereoselective interconversion
-
-
?
(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
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
-
-
-
-
?
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
-
-
-
?
(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
-
-
?
1-butanol + NAD+
butanal + NADH + H+
-
-
-
?
1-butanol + NAD+
butanal + NADH + H+
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
-
?
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
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
-
ir
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
?
2-butanol + NAD+
2-butanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
-
-
?
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH
L-acetoin + NAD+
-
-
-
ir
diacetyl + NADH
L-acetoin + NAD+
-
-
-
ir
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
100% activity
-
-
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
-
-
-
?
glyceraldehyde + NADH + H+
?
-
low activity with 30 mM
-
-
?
glyceraldehyde + NADH + H+
?
-
low activity with 30 mM
-
-
?
L-acetoin + NADH
L-2,3-butanediol
-
stereoisomeric specificity 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 specificity for hydroxyl group in L configuration
-
?
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
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
?
-
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)
-
-
-
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
?
-
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
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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?
additional information
?
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-
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
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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
-
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
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
-
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
-
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
-
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
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
-
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
-
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
-
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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
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2016
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