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(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH
-
Substrates: (2S,3S)-2,3-butanediol is a poor substrate
Products: -
?
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
(R)-acetoin + NADPH + H+
meso-2,3-butanediol + NADP+
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: stereoselective interconversion
Products: -
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(S)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
1,2-cyclohexanedione + NADH + H+
(S,S)-1,2-cyclohexanediol + NAD+
1,2-pentanediol + NADH + H+
?
1,2-propandiol + NADH + H+
?
Substrates: low activity
Products: -
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
Substrates: -
Products: -
?
1-phenyl-1,2-propanedione + NADH + H+
(S)-2-hydroxy-1-phenylpropan-1-one + NAD+
2 (R,S)-acetoin + 2 NADPH + 2 H+
(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
r
2 acetoin + 2 NADH + 2 H+
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + 2 NAD+
-
Substrates: racemic mixture of (3S/3R)-acetoin
Products: -
r
2,3-heptanedione + NADH + H+
3-hydroxy-2-heptanone + NAD+
Substrates: -
Products: -
?
2,3-hexanedione + NADH + H+
(S)-3-hydroxy-2-hexanone + NAD+
Substrates: -
Products: -
?
2,3-pentandione + NADH + H+
? + NAD+
Substrates: -
Products: -
?
2,3-pentanedione + NADH + H+
(3S)-3-hydroxy-2-pentanone + NAD+
Substrates: -
Products: -
?
3,4-hexanedione + NADH + H+
(3S,4S)-3,4-hexanediol + NAD+
Substrates: -
Products: -
?
4-methyl-2-pentanone + NADH + H+
4-methyl-2-pentanol + NAD+
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
butane-1,2-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
diacetyl + 2 NADH + 2 H+
(2R,3R)-butane-2,3-diol + 2 NAD+
Substrates: -
Products: -
r
diacetyl + NADH + H+
(3R)-acetoin + NAD+
Substrates: -
Products: -
r
diacetyl + NADH + H+
(3S)-acetoin + NAD+
Substrates: -
Products: -
?
glycerol + NADH + H+
?
Substrates: low activity
Products: -
?
L-acetoin + NADH
L-2,3-butanediol + NAD+
-
Substrates: -
Products: -
?
meso-2,3-butanediol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
acetoin + NADH
-
Substrates: -
Products: -
?
meso-2,3-butanediol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
?
meso-2,3-butanediol + NADP+
(R)-acetoin + NADPH + H+
Substrates: very low activity
Products: -
r
propane-1,2-diol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
rac acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
Substrates: -
Products: -
?
rac acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
Substrates: -
Products: -
?
additional information
?
-
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: slightly preferred substrate
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: preferred substrate
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: meso-butane-2,3-diol
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: stereoselective interconversion
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
AEF50077
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
Substrates: -
Products: -
?
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
Substrates: low activity
Products: -
r
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
Substrates: low activity
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: low activity in vivo
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
Substrates: at pH 9.0
Products: -
r
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
Substrates: at pH 9.0
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: preferred reaction direction
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: preferred reaction direction
Products: -
r
(R)-acetoin + NADPH + H+
meso-2,3-butanediol + NADP+
Substrates: very low activity
Products: -
r
(R)-acetoin + NADPH + H+
meso-2,3-butanediol + NADP+
Substrates: very low activity
Products: -
r
1,2-cyclohexanedione + NADH + H+
(S,S)-1,2-cyclohexanediol + NAD+
Substrates: -
Products: -
?
1,2-cyclohexanedione + NADH + H+
(S,S)-1,2-cyclohexanediol + NAD+
Substrates: -
Products: -
?
1,2-pentanediol + NADH + H+
?
Substrates: low activity
Products: -
?
1,2-pentanediol + NADH + H+
?
Substrates: low activity
Products: -
?
1-phenyl-1,2-propanedione + NADH + H+
(S)-2-hydroxy-1-phenylpropan-1-one + NAD+
Substrates: -
Products: -
?
1-phenyl-1,2-propanedione + NADH + H+
(S)-2-hydroxy-1-phenylpropan-1-one + NAD+
Substrates: -
Products: -
?
4-methyl-2-pentanone + NADH + H+
4-methyl-2-pentanol + NAD+
-
Substrates: low activity
Products: -
r
4-methyl-2-pentanone + NADH + H+
4-methyl-2-pentanol + NAD+
-
Substrates: low activity
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: racemic mixture of (3S/3R)-acetoin
Products: -
r
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: racemic mixture of (3S/3R)-acetoin
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
-
Substrates: the (S)-specific ADH-9 produces (R)-acetoin by an oxidative route starting from meso-2,3-butanediol
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
-
Substrates: enantioselective enzymatic synthesis of the alpha-hydroxy ketone(R)-acetoin from meso-2,3-butanediol
Products: -
r
additional information
?
-
Substrates: stereoisomeric composition analysis of 2,3-butanediol produced by strain 10-1-A using gas chromatography. Strain 10-1-A produces a mixture of (2R,3R)-2,3-butanediol and meso-2,3-butanediol with a ratio of nearly 1:1. As (3R)-acetoin is the major source of (2R,3R)-2,3-butanediol and meso-2,3-butanediol, a meso-butanediol dehydrogenase and a (2R,3R)-2,3-butanediol dehydrogenase are co-present in strain 10-1-A
Products: -
?
additional information
?
-
-
Substrates: most of the Bacillus strains produce 2,3-butanediol but not acetoin as their major product
Products: -
-
additional information
?
-
Substrates: stereoisomeric composition analysis of 2,3-butanediol produced by strain 10-1-A using gas chromatography. Strain 10-1-A produces a mixture of (2R,3R)-2,3-butanediol and meso-2,3-butanediol with a ratio of nearly 1:1. As (3R)-acetoin is the major source of (2R,3R)-2,3-butanediol and meso-2,3-butanediol, a meso-butanediol dehydrogenase and a (2R,3R)-2,3-butanediol dehydrogenase are co-present in strain 10-1-A
Products: -
?
additional information
?
-
-
Substrates: most of the Bacillus strains produce 2,3-butanediol but not acetoin as their major product
Products: -
-
additional information
?
-
-
Substrates: meso-2,3-butanediol dehydrogenase (BDH) catalyzes the redox reaction between (R)-acetoin and meso-2,3-butanediol
Products: -
?
additional information
?
-
Substrates: enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl
Products: -
-
additional information
?
-
Substrates: enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl
Products: -
-
additional information
?
-
-
Substrates: NMR identification and quantification of reaction products. Meso-2,3-butanediol is the major form (over 95% of the 2,3-butanediol pool, depending on oxygen availability) produced in fermentations using a strain that overexpresses ALS/ALDC of Lactobacillus lactis and BDH of Corynebacterium glutamicum, i.e., strain DELTAaceEDELTApqoDELTAldhA(pEKEx2als,aldB,butACg)
Products: -
?
additional information
?
-
Substrates: the enzyme is also active with diacetyl and NADH
Products: -
?
additional information
?
-
Substrates: the enzyme is also active with diacetyl and NADH
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly stereospecific, and shows no significant activities towards 2R,3R-2,3-butanediol, 1,4-butanediol, and 2S,3S-2,3-butanediol
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 (EC 1.1.1.76) 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: -
-
additional information
?
-
-
Substrates: the enzyme is highly stereospecific, and shows no significant activities towards 2R,3R-2,3-butanediol, 1,4-butanediol, and 2S,3S-2,3-butanediol
Products: -
?
additional information
?
-
Substrates: production of S,S- and/or R,R- and meso-2,3-BDO by Paenibacillus brasilensis strain PB24 grown in the modified YEPD medium, pH 6.3, 32°C, up to 72 h
Products: -
-
additional information
?
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Substrates: production of S,S- and/or R,R- and meso-2,3-BDO by Paenibacillus brasilensis strain PB24 grown in the modified YEPD medium, pH 6.3, 32°C, up to 72 h
Products: -
-
additional information
?
-
Substrates: the (2R,3R)-2,3-butanediol dehydrogenase is active with (R,R)-butane-2,3-diol, but also with meso-butane-2,3-diol, but not with with (2S,3S)-2,3-butane-2,3-diol. No activity with 2-butanol, 1,3-butanediol, 1,2-pentanediol, 1,3-propanediol, and glycerol in the oxidation reaction. And no activity with 2,4-pentanedione, butanone, 2,5-hexanedione, n-butanal and 1,3-dihydroxypropanone in the reduction reaction. Substrate specificity, overview. (2R,3R)-2,3-BDH reduces diacetyl into (3R)-acetoin and (2R,3R)-2,3-BD, while racemic acetoin is reduced into (2R,3R)-2,3-BD and meso-2,3-BD
Products: -
-
additional information
?
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Substrates: (2R,3R)-2,3-butanediol is no substrate for the enzyme
Products: -
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additional information
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Substrates: (2R,3R)-2,3-butanediol is no substrate for the enzyme
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additional information
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Substrates: 2,3-butanediol dehydrogenase (BudC) catalyses the selective asymmetric reductions of prochiral alpha-diketones to the corresponding alpha-hydroxy ketones and diols. BudC is highly active towards structurally diverse diketones in combination with nicotinamide cofactor regeneration systems. Aliphatic diketones, cyclic diketones, and alkyl phenyl diketones are well accepted, whereas their derivatives possessing two bulky groups are not converted. In the reverse reaction vicinal diols are preferred over other substrates with hydroxy/keto groups in non-vicinal positions. Substrate specificity and stereoselectivity, overview. In the reductive reaction diacetyl is the preferred substrate of BudC over acetoin, while only meso-2,3-butanediol oxidation is catalysed by the enzyme under the conditions assessed. No activity with (2S,3S)-butane-2,3-diol and (2R,3R)-butane-2,3-diol. BudC is S-selective for the reduction of diacetyl yielding (S,S)-2,3-butanediol ((S,S)-2,3-BDO), rac-acetoin is reduced to both meso-2,3-BDO and (S,S)-2,3-BDO. Here (R)-acetoin is the preferred substrate and 15% (S)-acetoin remains unconverted after 24 h. Thus, BudC shows a stereo-preference consistent with meso-2,3-butanediol dehydrogenases with respect to acetoin. No activity with R-benzoin, rac-benzoin, benzil, acetone, 2,4-pentanediol, 1,3-butanediol, ethanol, and 2-propanol
Products: -
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additional information
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Substrates: substrate promiscuity of the SmBdh enzyme, SmBdh has been reported to be able to reduce both (3R)- and (3S)-acetoin to 2,3-BDO, although (3R)-acetoin is more readily converted than (3S)-acetoin. On the other hand, SmBdh is able to oxidize meso-2,3-BDO and (2S,3S)-BDO, while oxidation of (2R,3R)-BDO is not detectable. Moreover, its activity towards (2S,3S)-BDO is only 11% of that towards meso-2,3-BDO. The enzyme is classified as an S-acting Bdh based on production of meso-2,3-BDO and (2S,3S)-BDO from a racemic mixture of acetoin
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additional information
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Substrates: substrate promiscuity of the SmBdh enzyme, SmBdh has been reported to be able to reduce both (3R)- and (3S)-acetoin to 2,3-BDO, although (3R)-acetoin is more readily converted than (3S)-acetoin. On the other hand, SmBdh is able to oxidize meso-2,3-BDO and (2S,3S)-BDO, while oxidation of (2R,3R)-BDO is not detectable. Moreover, its activity towards (2S,3S)-BDO is only 11% of that towards meso-2,3-BDO. The enzyme is classified as an S-acting Bdh based on production of meso-2,3-BDO and (2S,3S)-BDO from a racemic mixture of acetoin
Products: -
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additional information
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Substrates: substrate promiscuity of the SmBdh enzyme, SmBdh has been reported to be able to reduce both (3R)- and (3S)-acetoin to 2,3-BDO, although (3R)-acetoin is more readily converted than (3S)-acetoin. On the other hand, SmBdh is able to oxidize meso-2,3-BDO and (2S,3S)-BDO, while oxidation of (2R,3R)-BDO is not detectable. Moreover, its activity towards (2S,3S)-BDO is only 11% of that towards meso-2,3-BDO. The enzyme is classified as an S-acting Bdh based on production of meso-2,3-BDO and (2S,3S)-BDO from a racemic mixture of acetoin
Products: -
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additional information
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Substrates: 2,3-butanediol dehydrogenase (BudC) catalyses the selective asymmetric reductions of prochiral alpha-diketones to the corresponding alpha-hydroxy ketones and diols. BudC is highly active towards structurally diverse diketones in combination with nicotinamide cofactor regeneration systems. Aliphatic diketones, cyclic diketones, and alkyl phenyl diketones are well accepted, whereas their derivatives possessing two bulky groups are not converted. In the reverse reaction vicinal diols are preferred over other substrates with hydroxy/keto groups in non-vicinal positions. Substrate specificity and stereoselectivity, overview. In the reductive reaction diacetyl is the preferred substrate of BudC over acetoin, while only meso-2,3-butanediol oxidation is catalysed by the enzyme under the conditions assessed. No activity with (2S,3S)-butane-2,3-diol and (2R,3R)-butane-2,3-diol. BudC is S-selective for the reduction of diacetyl yielding (S,S)-2,3-butanediol ((S,S)-2,3-BDO), rac-acetoin is reduced to both meso-2,3-BDO and (S,S)-2,3-BDO. Here (R)-acetoin is the preferred substrate and 15% (S)-acetoin remains unconverted after 24 h. Thus, BudC shows a stereo-preference consistent with meso-2,3-butanediol dehydrogenases with respect to acetoin. No activity with R-benzoin, rac-benzoin, benzil, acetone, 2,4-pentanediol, 1,3-butanediol, ethanol, and 2-propanol
Products: -
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additional information
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Substrates: (2R,3R)-2,3-butanediol is no substrate for the enzyme
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additional information
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Substrates: (2R,3R)-2,3-butanediol is no substrate for the enzyme
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additional information
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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, cf. EC 1.1.1.76
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additional information
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Substrates: reaction component identification and quantification by GC-MS. No or very poor activity with isopropanol 2-methyl-1-butanol, 2-methyl-2-butanol, 2,5-hexanediol, 1,4-butanediol
Products: -
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
additional information
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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: meso-butane-2,3-diol
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(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
AEF50077
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
Substrates: -
Products: -
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(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2R,3S)-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
Substrates: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: low activity in vivo
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
-
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
(R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
Substrates: -
Products: -
r
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: racemic mixture of (3S/3R)-acetoin
Products: -
r
acetoin + NADH + H+
meso-2,3-butanediol + NAD+
Substrates: racemic mixture of (3S/3R)-acetoin
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
-
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
Substrates: -
Products: -
r
meso-2,3-butanediol + NAD+
(R)-acetoin + NADH + H+
-
Substrates: the (S)-specific ADH-9 produces (R)-acetoin by an oxidative route starting from meso-2,3-butanediol
Products: -
r
additional information
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Substrates: stereoisomeric composition analysis of 2,3-butanediol produced by strain 10-1-A using gas chromatography. Strain 10-1-A produces a mixture of (2R,3R)-2,3-butanediol and meso-2,3-butanediol with a ratio of nearly 1:1. As (3R)-acetoin is the major source of (2R,3R)-2,3-butanediol and meso-2,3-butanediol, a meso-butanediol dehydrogenase and a (2R,3R)-2,3-butanediol dehydrogenase are co-present in strain 10-1-A
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additional information
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Substrates: most of the Bacillus strains produce 2,3-butanediol but not acetoin as their major product
Products: -
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additional information
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Substrates: stereoisomeric composition analysis of 2,3-butanediol produced by strain 10-1-A using gas chromatography. Strain 10-1-A produces a mixture of (2R,3R)-2,3-butanediol and meso-2,3-butanediol with a ratio of nearly 1:1. As (3R)-acetoin is the major source of (2R,3R)-2,3-butanediol and meso-2,3-butanediol, a meso-butanediol dehydrogenase and a (2R,3R)-2,3-butanediol dehydrogenase are co-present in strain 10-1-A
Products: -
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additional information
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Substrates: most of the Bacillus strains produce 2,3-butanediol but not acetoin as their major product
Products: -
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evolution
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phylogenetic analysis
evolution
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phylogenetic analysis
evolution
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the enzyme belongs to the short chain dehydrogenase/reductase family
evolution
the enzyme belongs to the shortchain dehydrogenase/reductase superfamily
evolution
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enzyme BDH belongs to the SDR family, of enzymes
evolution
Bdh enzymes can be classified into R-acting or S-acting depending on the chirality of the chiral center introduced by the enzyme at the acetoin C2 atom. Whereas the preference for (3R)-acetoin or (3S)-acetoin is imprinted in the geometry of the substrate-binding pocket, R-acting and S-acting Bdh enzymes belong to different protein families and possess different architectures
evolution
enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family
evolution
the enzyme belongs to the NADH-dependent metal-independent short-chain dehydrogenases/reductase (SDR) family of oxidoreductases
evolution
the enzyme belongs to the short-chain dehydrogenases/reductases
evolution
-
the enzyme belongs to the shortchain dehydrogenase/reductase superfamily
-
evolution
-
the enzyme belongs to the NADH-dependent metal-independent short-chain dehydrogenases/reductase (SDR) family of oxidoreductases
-
evolution
-
the enzyme belongs to the short chain dehydrogenase/reductase family
-
evolution
-
Bdh enzymes can be classified into R-acting or S-acting depending on the chirality of the chiral center introduced by the enzyme at the acetoin C2 atom. Whereas the preference for (3R)-acetoin or (3S)-acetoin is imprinted in the geometry of the substrate-binding pocket, R-acting and S-acting Bdh enzymes belong to different protein families and possess different architectures
-
evolution
-
enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family
-
malfunction
-
the budC knockout strain produces only the D-2,3-butanediol isomer with high yield and productivity. Deletion of budC gene causes a slight decrease (about 5-10%) in cell growth
malfunction
deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation
malfunction
deletion of budC causes redox imbalance towards NADH
malfunction
extending the alpha6 helix of SmBdh to mimic the lower activity Enterobacter cloacae enzyme EcBdh results in reduction of SmBdh function to nearly 3% of the total activity. In great contrast, reduction of the corresponding alpha6 helix of the EcBdh to mimic the SmBdh structure results in about 70% increase in its activity
malfunction
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
malfunction
-
the growth of Bacillus licheniformis mutant strain MW3 (DELTAbudCDELTAgdh) is slightly lower than that of Bacillus licheniformis wild-type strain MW3, but the mutant strain can produce acetoin instead of 2,3-butanediol as its major product
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the growth of Bacillus licheniformis mutant strain MW3 (DELTAbudCDELTAgdh) is slightly lower than that of Bacillus licheniformis wild-type strain MW3, but the mutant strain can produce acetoin instead of 2,3-butanediol as its major product
-
malfunction
-
the budC knockout strain produces only the D-2,3-butanediol isomer with high yield and productivity. Deletion of budC gene causes a slight decrease (about 5-10%) in cell growth
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
deletion of budC causes redox imbalance towards NADH
-
malfunction
-
deletion of bdhA gene successfully blocks the reversible transformation between acetoin and 2,3-butanediol and eliminates the effect of dissolved oxygen on the transformation
-
malfunction
-
the amount of meso-2,3-BD is highly reduced in a DELTAacoR mutant lacking the regulatory protein AcoR. The loss of locus pa4153, encoding (2R,3R)-2,3-BDH, has no effect on the ability of this strain to grow in (2S,3S)-2,3-BD but completely impairs its ability to utilize (2R,3R)-2,3-BD and meso-2,3-BD. The complementation of the pa4153 mutant strain with its gene successfully restores the growth ability. The DELTApa4153 PAO1 strain can grow in racemic acetoin, indicating that (2R,3R)-2,3-BDH contributes to 2,3-BD utilization by converting 2,3-BD into acetoin
-
malfunction
-
extending the alpha6 helix of SmBdh to mimic the lower activity Enterobacter cloacae enzyme EcBdh results in reduction of SmBdh function to nearly 3% of the total activity. In great contrast, reduction of the corresponding alpha6 helix of the EcBdh to mimic the SmBdh structure results in about 70% increase in its activity
-
metabolism
-
pathways for the synthesis of 2,3-butanediol in bacteria, 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
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
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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 dehydrogenase (BDH) catalyzes the interconversion between acetoin and 2,3-butanediol and is a key enzyme for 2,3-butanediol production
physiological function
-
budC encodes the major meso-2,3-butanediol dehydrogenase catalyzing the reversible reaction from acetoin to meso-2,3-butanediol in Bacillus licheniformis
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
acetoin and 2,3-butanediol can be transformed into each other by 2,3-butanediol dehydrogenase (BDH) using NADH/NAD+ as coenzyme. The main 2,3-butanediol production of strain BS168D is meso-2,3-butanediol and the bdhA gene is only responsible for (2R,3R)-2,3-butanediol synthesis. Oxygen supply in the culture of Bacillus subtilis has an important impact on the product yield, productivity and 2,3-butanediol formation in acetoin fermentation. In general, high oxygen supply favours acetoin formation and decrease 2,3-butanediol final yield
physiological function
acetoin can be converted to 2,3-butanediol by 2,3-butanediol dehydrogenase (budC) with consumption of NADH
physiological function
-
D-(-)-acetoin with an optical purity of 25.9% is produced by PT-BDH
physiological function
D-(-)-acetoin with an optical purity of 57% is produced by BS-BDH
physiological function
L-(+)-acetoin with an optical purity of 92% is produced by BS-BDH
physiological function
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO). And although the gene encoding (S,S)-2,3-butanediol dehydrogenase (EC 1.1.1.76) 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 tested. The enzyme is bifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
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
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physiological function
-
budC encodes the major meso-2,3-butanediol dehydrogenase catalyzing the reversible reaction from acetoin to meso-2,3-butanediol in Bacillus licheniformis
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physiological function
-
D-(-)-acetoin with an optical purity of 57% is produced by BS-BDH
-
physiological function
-
D-(-)-acetoin with an optical purity of 57% is produced by BS-BDH
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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
-
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO). And although the gene encoding (S,S)-2,3-butanediol dehydrogenase (EC 1.1.1.76) 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 tested. The enzyme is bifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
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physiological function
-
2,3-butanediol dehydrogenase (BDH) catalyzes the interconversion between acetoin and 2,3-butanediol and is a key enzyme for 2,3-butanediol production
-
physiological function
-
acetoin can be converted to 2,3-butanediol by 2,3-butanediol dehydrogenase (budC) with consumption of NADH
-
physiological function
-
D-(-)-acetoin with an optical purity of 57% is produced by BS-BDH
-
physiological function
-
acetoin and 2,3-butanediol can be transformed into each other by 2,3-butanediol dehydrogenase (BDH) using NADH/NAD+ as coenzyme. The main 2,3-butanediol production of strain BS168D is meso-2,3-butanediol and the bdhA gene is only responsible for (2R,3R)-2,3-butanediol synthesis. Oxygen supply in the culture of Bacillus subtilis has an important impact on the product yield, productivity and 2,3-butanediol formation in acetoin fermentation. In general, high oxygen supply favours acetoin formation and decrease 2,3-butanediol final yield
-
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
-
D-(-)-acetoin with an optical purity of 25.9% is produced by PT-BDH
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additional information
the enzyme possesses two conserved sequences including the coenzyme binding motif (GxxxGxG) and the active-site motif (YxxxK)
additional information
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the enzyme possesses two conserved sequences including the coenzyme binding motif (GxxxGxG) and the active-site motif (YxxxK)
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
additional information
Serratia marcescens is a very efficient producer of meso-2,3-butanediol (meso-2,3-BTD)from glucose
additional information
SmBdh shows a more extensive supporting hydrogen-bond network in comparison to the other well-studied Bdh enzymes, which enables improved substrate positioning and substrate specificity. The substrate-binding pocket is formed by two protein molecules, not a single peptide as found in all other reported Bdh enzymes. The C-terminus of molecule A protrudes into the groove between alpha7 helix and the alpha-turn alphat1 capping substrate-binding pocket of molecule Asymm and vice versa. The SmBdh active site is populated by a Gln247 residue contributed by the diagonally opposite subunit. The enzyme protein also contains a short alpha6 helix, which provides more efficient entry and exit of molecules from the active site, thereby contributing to enhanced substrate turnover. While coordinated active site formation is a unique structural characteristic of this tetrameric complex, the smaller alpha6 helix and extended hydrogen network contribute towards improved activity and substrate promiscuity of the enzyme. Gln247 plays a crucial role in SmBdh catalysis
additional information
-
SmBdh shows a more extensive supporting hydrogen-bond network in comparison to the other well-studied Bdh enzymes, which enables improved substrate positioning and substrate specificity. The substrate-binding pocket is formed by two protein molecules, not a single peptide as found in all other reported Bdh enzymes. The C-terminus of molecule A protrudes into the groove between alpha7 helix and the alpha-turn alphat1 capping substrate-binding pocket of molecule Asymm and vice versa. The SmBdh active site is populated by a Gln247 residue contributed by the diagonally opposite subunit. The enzyme protein also contains a short alpha6 helix, which provides more efficient entry and exit of molecules from the active site, thereby contributing to enhanced substrate turnover. While coordinated active site formation is a unique structural characteristic of this tetrameric complex, the smaller alpha6 helix and extended hydrogen network contribute towards improved activity and substrate promiscuity of the enzyme. Gln247 plays a crucial role in SmBdh catalysis
additional information
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the enzyme possesses two conserved sequences including the coenzyme binding motif (GxxxGxG) and the active-site motif (YxxxK)
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additional information
-
Serratia marcescens is a very efficient producer of meso-2,3-butanediol (meso-2,3-BTD)from glucose
-
additional information
-
SmBdh shows a more extensive supporting hydrogen-bond network in comparison to the other well-studied Bdh enzymes, which enables improved substrate positioning and substrate specificity. The substrate-binding pocket is formed by two protein molecules, not a single peptide as found in all other reported Bdh enzymes. The C-terminus of molecule A protrudes into the groove between alpha7 helix and the alpha-turn alphat1 capping substrate-binding pocket of molecule Asymm and vice versa. The SmBdh active site is populated by a Gln247 residue contributed by the diagonally opposite subunit. The enzyme protein also contains a short alpha6 helix, which provides more efficient entry and exit of molecules from the active site, thereby contributing to enhanced substrate turnover. While coordinated active site formation is a unique structural characteristic of this tetrameric complex, the smaller alpha6 helix and extended hydrogen network contribute towards improved activity and substrate promiscuity of the enzyme. Gln247 plays a crucial role in SmBdh catalysis
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D194G
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site-directed mutagenesis, the mutant binds the substrate but is catalytically almost inactive. The mutant is inactive with (2S,3S)-butanediol, meso-butanediol and (2R,3R)-butanediol. D194G enzyme mutant shows a similar secondary structure compared to Enterobacter aerogenes BDH. While the mutant is highly susceptible to protease digestion compared to the wild-type enzyme. Homology modeling of the mutant enzyme, with meso-2,3-butanediol dehydrogenase from Klebsiella pneumoniae, PDB ID 1GEG, as a template, reveals that Gly194 seems to lose the hydrogen bond interactions with the surrounding residues (Gly206, Gly207 and Thr209), resulting in a putative conformational changes of mutant D194G which might be responsible for the loss of activity
moe
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construction and engineering of Corynebacterium glutamicum strain DELTAaceEDELTApqoDELTAldhA(pEKEx2-als,aldB,butACg). Chromosomal inactivation of the putative BDH gene butACg (cg2958) in strain DELTAaceEDELTApqoDELTAldhA. BDH activity is nearly abolished upon inactivation of butACg indicating that Corynebacterium glutamicum expresses a single BDH under the experimental conditions examined. BDH activity increases 3fold in strain DELTAaceEDELTApqoDELTAldhA(pEKEx2-als,aldB,butACg) compared to the respective control. The inactivation of butACg gene decreases the BDH activity 75fold for the DELTAaceEDELTApqoDELTAldhADELTAbutACg(pEKEx2) strain compared to strain DELTAaceEDELTApqoDELTAldhA(pEKEx2). The major form of 2,3-butanediol is meso-2,3-butandediol, and the ratio meso-2,3-BD/optically active 2,3-BD is 95:5, the main side products are glycerol, ethanol, and acetoin
N146F
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11% of wild-type specific activity
Q140I
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trace activity below 0.1 U/mg
Q140I/N146F
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poor activity
Q140I/N146F/W190H
-
trace activity below 0.1 U/mg with substrate meso-butanediol, 2.9 U/mg with substrate (2S,3S)-2,3-butanediol
F212S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
F212W
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
F212Y
site-directed mutagenesis, the kcat of the mutant is enhanced 4-8fold compared to wild-type
N146A
site-directed mutagenesis, inactive mutant
N146Q
site-directed mutagenesis, the mutant shows unaltered activity compared to wild-type
Q140I
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mutation mimicking the corresponding residue in (S,S)-butanediol dehydrogenase. No activity with substrates meso-butanediol or (S,S)-butanediol
Q140I/N146F
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mutation mimicking the corresponding residues in (S,S)-butanediol dehydrogenase. Poor activity with substrates meso-butanediol or (S,S)-butanediol
Q274A
site-directed mutagenesis, the substrate binding site is occupied by a glycerol molecule in the Q247A mutant, the mutation disrupts the active site of the protein, the Q247A mutant shows a 90% loss in activity compare to wild-type
Q274A/V139Q
site-directed mutagenesis, the substrate binding site is occupied by an ethylene glycol molecule in the Q274A/V139Q mutant, the mutation disrupts the active site of the protein, the double mutant Q247A/V139Q showa 300% improvement in activity in comparison to the Q247A mutant. Although the double mutant does not completely restore the loss of Gln247 activity, significant function is regained by introducing the V139Q mutation in this protein, to about 50% activity compared to wild-type
Q274A
-
site-directed mutagenesis, the substrate binding site is occupied by a glycerol molecule in the Q247A mutant, the mutation disrupts the active site of the protein, the Q247A mutant shows a 90% loss in activity compare to wild-type
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Q274A/V139Q
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site-directed mutagenesis, the substrate binding site is occupied by an ethylene glycol molecule in the Q274A/V139Q mutant, the mutation disrupts the active site of the protein, the double mutant Q247A/V139Q showa 300% improvement in activity in comparison to the Q247A mutant. Although the double mutant does not completely restore the loss of Gln247 activity, significant function is regained by introducing the V139Q mutation in this protein, to about 50% activity compared to wild-type
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additional information
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generation of a mutant strain WX-02 DELTAbudC of Bacillus licheniformis with depleted budC gene that produces high yields of the D-2,3-butanediol isomer with high optimal purity
additional information
-
construction of a knockout Bacillus licheniformis mutant DELTAbudCDELTAgdh deleting two 2,3-butanediol dehydrogenases, i.e. meso-2,3-butanediol dehydrogenases BudC and GDH, through gene disruption. Escherichia coli strain S17-1 lpir is used as donor strain to allow the conjugal transfer of plasmids pKVM1-1budC and pKVM1-1gdh into Bacillus licheniformis strain MW3. Although the growth of strain MW3 (DELTAbudCDELTAgdh) is slightly lower than that of wild-type strain MW3, it can produce acetoin instead of 2,3-butanediol as its major product. Using fedbatch fermentation of Bacillus licheniformis MW3 (DELTAbudCDELTAgdh), 64.2 g/l acetoin is produced at a productivity of 2.378 g/l/h and a yield of 0.412 g/g from 156 g/l glucose in 27 h
additional information
-
construction of a knockout Bacillus licheniformis mutant DELTAbudCDELTAgdh deleting two 2,3-butanediol dehydrogenases, i.e. meso-2,3-butanediol dehydrogenases BudC and GDH, through gene disruption. Escherichia coli strain S17-1 lpir is used as donor strain to allow the conjugal transfer of plasmids pKVM1-1budC and pKVM1-1gdh into Bacillus licheniformis strain MW3. Although the growth of strain MW3 (DELTAbudCDELTAgdh) is slightly lower than that of wild-type strain MW3, it can produce acetoin instead of 2,3-butanediol as its major product. Using fedbatch fermentation of Bacillus licheniformis MW3 (DELTAbudCDELTAgdh), 64.2 g/l acetoin is produced at a productivity of 2.378 g/l/h and a yield of 0.412 g/g from 156 g/l glucose in 27 h
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additional information
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generation of a mutant strain WX-02 DELTAbudC of Bacillus licheniformis with depleted budC gene that produces high yields of the D-2,3-butanediol isomer with high optimal purity
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additional information
a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
additional information
construction of an engineered Bacillus subtilis strain 168 in which the bdhA gene is knocked out by the cre/lox system using the lox71-zeo-lox66 resistance marker cassette. The effects of bdhA gene deletion on production of acetoin and 2,3-butanediol are evaluated. By increasing the glucose concentration, the acetoin yield is improved from 6.61 g/l to 24.6 g/l. Deletion of the gene bdhA efficiently blocks the transformation of acetoin and 2,3-butanediol during the fermentation of strain BS168D, overview
additional information
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construction of an engineered Bacillus subtilis strain 168 in which the bdhA gene is knocked out by the cre/lox system using the lox71-zeo-lox66 resistance marker cassette. The effects of bdhA gene deletion on production of acetoin and 2,3-butanediol are evaluated. By increasing the glucose concentration, the acetoin yield is improved from 6.61 g/l to 24.6 g/l. Deletion of the gene bdhA efficiently blocks the transformation of acetoin and 2,3-butanediol during the fermentation of strain BS168D, overview
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additional information
a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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expression of gene bdh1 from Saccharomyces cervisiae in Escherichia coi strain YYC202(DE3) ldhA-/- ilvC-/- expressing ilvBN from Escherichia coli and aldB from Lactobacillus lactis, encoding acetolactate synthase and acetolactate decarboxylase activities, respectively. Disruption of the lactate biosynthesis pathway in the strain increases pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-butanediol is the most important consequence of ldhA deletion. Optimization of 2,3-butanediol production in Escherichia coli, overview
additional information
Enterobacter aerogenes is metabolically engineered for acetoin production. To remove the pathway enzymes that catalyze the formation of by-products, the three genes encoding a lactate dehydrogenase (ldhA) and two 2,3-butanediol dehydrogenases (budC, and dhaD), respectively, are deleted from the genome. The acetoin production is higher under highly aerobic conditions. An extracellular glucose oxidative pathway in Enterobacter aerogenes is activated under the aerobic conditions, resulting in the accumulation of 2-ketogluconate. To decrease the accumulation of this by-product, the gene encoding a glucose dehydrogenase (gcd) is also deleted. The resulting strain does not produce 2-ketogluconate but produces significant amounts of acetoin, with concentration reaching 71.7 g/l with 2.87 g/l/h productivity in fed-batch fermentation. The resulting strains are EMY-01 (DELTAldhA), EJW-0 (DELTAldhA-DELTAbudC), EJW-02 (DELTAldhA-DELTAbudC-DELTAdhaD), and EJW-03 (DELTAldhA-DELTAbudC-DELTAdhaD-DELTAgcd), evaluation for acetoin production, overview
additional information
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Enterobacter aerogenes is metabolically engineered for acetoin production. To remove the pathway enzymes that catalyze the formation of by-products, the three genes encoding a lactate dehydrogenase (ldhA) and two 2,3-butanediol dehydrogenases (budC, and dhaD), respectively, are deleted from the genome. The acetoin production is higher under highly aerobic conditions. An extracellular glucose oxidative pathway in Enterobacter aerogenes is activated under the aerobic conditions, resulting in the accumulation of 2-ketogluconate. To decrease the accumulation of this by-product, the gene encoding a glucose dehydrogenase (gcd) is also deleted. The resulting strain does not produce 2-ketogluconate but produces significant amounts of acetoin, with concentration reaching 71.7 g/l with 2.87 g/l/h productivity in fed-batch fermentation. The resulting strains are EMY-01 (DELTAldhA), EJW-0 (DELTAldhA-DELTAbudC), EJW-02 (DELTAldhA-DELTAbudC-DELTAdhaD), and EJW-03 (DELTAldhA-DELTAbudC-DELTAdhaD-DELTAgcd), evaluation for acetoin production, overview
additional information
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Enterobacter aerogenes is metabolically engineered for acetoin production. To remove the pathway enzymes that catalyze the formation of by-products, the three genes encoding a lactate dehydrogenase (ldhA) and two 2,3-butanediol dehydrogenases (budC, and dhaD), respectively, are deleted from the genome. The acetoin production is higher under highly aerobic conditions. An extracellular glucose oxidative pathway in Enterobacter aerogenes is activated under the aerobic conditions, resulting in the accumulation of 2-ketogluconate. To decrease the accumulation of this by-product, the gene encoding a glucose dehydrogenase (gcd) is also deleted. The resulting strain does not produce 2-ketogluconate but produces significant amounts of acetoin, with concentration reaching 71.7 g/l with 2.87 g/l/h productivity in fed-batch fermentation. The resulting strains are EMY-01 (DELTAldhA), EJW-0 (DELTAldhA-DELTAbudC), EJW-02 (DELTAldhA-DELTAbudC-DELTAdhaD), and EJW-03 (DELTAldhA-DELTAbudC-DELTAdhaD-DELTAgcd), evaluation for acetoin production, overview
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additional information
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Bacillus subtilis is engineered to produce chiral pure meso-2,3-BD. D-2,3-butanediol production is abolished by deleting D-2,3-butanediol dehydrogenase (EC 1.1.1.4) coding gene bdhA, and acoA gene is knocked out to prevent the degradation of acetoin, the immediate precursor of 2,3-butanediol. Next, both pta and ldh gene are deleted to decrease the accumulation of the byproducts, acetate and L-lactate. The meso-2,3-butanediol dehydrogenase coding gene from Klebsiella pneumoniae CICC10011 is introduced, as well as alsSD overexpressed in the tetra mutant (DELTAacoADELTAbdhADELTAptaDELTAldh) to achieve the efficient production of chiral meso-2,3-butanediol. Finally, the pool of NADH availability is further increased to facilitate the conversion of meso-2,3-butanediol from acetoin by overexpressing the udhA gene (coding a soluble transhydrogenase) and low dissolved oxygen control during the cultivation. Under microaerobic oxygen conditions, the best strain BSF9 produced 103.7 g/L meso-2,3-butanediol with a yield of 0.487 g/g glucose in the 5-L batch fermenter, and the titer of the main byproduct acetoin is no more than 1.1 g/L. Method optimization. The titer of meso-2,3-butanediol is almost unchanged at 37°C, 42°C, and 46°C, while the meso-2,3-butanediol productivity increases when the cultivation temperature is increased from 37°C to 46°C. The titer and productivity at 50°C decreases by 28.6% and 36.3% compared to those at 37°C
additional information
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Bacillus subtilis is engineered to produce chiral pure meso-2,3-BD. D-2,3-butanediol production is abolished by deleting D-2,3-butanediol dehydrogenase (EC 1.1.1.4) coding gene bdhA, and acoA gene is knocked out to prevent the degradation of acetoin, the immediate precursor of 2,3-butanediol. Next, both pta and ldh gene are deleted to decrease the accumulation of the byproducts, acetate and L-lactate. The meso-2,3-butanediol dehydrogenase coding gene from Klebsiella pneumoniae CICC10011 is introduced, as well as alsSD overexpressed in the tetra mutant (DELTAacoADELTAbdhADELTAptaDELTAldh) to achieve the efficient production of chiral meso-2,3-butanediol. Finally, the pool of NADH availability is further increased to facilitate the conversion of meso-2,3-butanediol from acetoin by overexpressing the udhA gene (coding a soluble transhydrogenase) and low dissolved oxygen control during the cultivation. Under microaerobic oxygen conditions, the best strain BSF9 produced 103.7 g/L meso-2,3-butanediol with a yield of 0.487 g/g glucose in the 5-L batch fermenter, and the titer of the main byproduct acetoin is no more than 1.1 g/L. Method optimization. The titer of meso-2,3-butanediol is almost unchanged at 37°C, 42°C, and 46°C, while the meso-2,3-butanediol productivity increases when the cultivation temperature is increased from 37°C to 46°C. The titer and productivity at 50°C decreases by 28.6% and 36.3% compared to those at 37°C
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
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a two-enzyme system composed of meso-2,3-butanediol dehydrogenase (BDH) and xylose reductase (CT-XR) from Candida tenuis is constructed to co-produce acetoin and xylitol with NAD+ regeneration. Four BDHs from four candidate organisms (Bacillus subtilis, Corynebacterium glutamicum, Parageobacillus thermoglucosidans, and Pyrococcus furiosus), as well as xylose reductase from Candida tenuis are purified and analyzed The best BDH is then selected according to titers and chiral purities of acetoin. After optimization of reaction conditions, and the ratios of meso-2,3-butanediol to xylose and BDH to xylose reductase, 28.5 g/l D-(-)-acetoin with an optical purity of 95.2% is produced in 6 h. The yield and productivity of acetoin is 0.97 g/g and 4.75 g/l/h. The titer of co-product xylitol is 40.29 g/l, and the yield and productivity of xylitol reaches 0.98 g/g and 6.72 g/l/h. Method development, evaluation, and optimization for production of optically pure D-(-)-acetoin, overview. Enzyme CT-XR acts most effectively with BDH from Corynebacterium glutamicum (CG-BDH)
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additional information
enzyme SmBdh is superior to other Bdhs for expression in Zymomonas mobilis for 2,3-BDO production. Structurally guided changes of recombinantly SmBdh expressed in Zymomonas mobilis can explain its superiority over lower activity Bdh enzymes from the same family of proteins. Development of two mutants of SmBdh: (1) Q247A where the Gln247 side chain is removed, leaving alanine at position 247 and (2) the double mutant Q247A/V139Q, where the missing glutamine side chain is reinstated at the position 139 that is present in KpBdh. Whereas Q247A will disrupt the active site of the protein, Q247A/V139Q is expected to restore the active site via a compensatory mechanism resulting in the active site being established by a single protein chain without contribution from a symmetry-related molecule (i.e. from the C-terminus of the opposite molecule in the tetramer)
additional information
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enzyme SmBdh is superior to other Bdhs for expression in Zymomonas mobilis for 2,3-BDO production. Structurally guided changes of recombinantly SmBdh expressed in Zymomonas mobilis can explain its superiority over lower activity Bdh enzymes from the same family of proteins. Development of two mutants of SmBdh: (1) Q247A where the Gln247 side chain is removed, leaving alanine at position 247 and (2) the double mutant Q247A/V139Q, where the missing glutamine side chain is reinstated at the position 139 that is present in KpBdh. Whereas Q247A will disrupt the active site of the protein, Q247A/V139Q is expected to restore the active site via a compensatory mechanism resulting in the active site being established by a single protein chain without contribution from a symmetry-related molecule (i.e. from the C-terminus of the opposite molecule in the tetramer)
additional information
the enzyme from Serratia marcescens is overexpressed in Lactobacillus diolivorans to produce meso-2,3-butanediol (meso-2,3-BTD). A two-step cultivation process with Serratia marcescens is developed for production of 2-butanol in Lactobacillus diolivorans via vitamin B12-dependent diol dehydratase (PduCDE) and alcohol dehydrogenase (pduQ). In the first step of the process, Serratia marcescens is used to produce stereospecifically meso-2,3-BTD from glucose followed by heat inactivation of Serratia marcescens. The accumulated meso-2,3-BTD is then converted during anaerobic fermentation with glucose into 2-butanol by Lactobacillus diolivorans. The process yields a butanol concentration of 10 g/l relying on wild-type bacterial strains. A further improvement of the maximum butanol titer is achieved using an engineered Lactobacillus diolivorans strain overexpressing the endogenous alcohol dehydrogenase pduQ. The two-step cultivation process based on this engineered strain leads to a maximum 2-butanol titer of 13.4 g/l, which means an increase of 34%
additional information
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enzyme SmBdh is superior to other Bdhs for expression in Zymomonas mobilis for 2,3-BDO production. Structurally guided changes of recombinantly SmBdh expressed in Zymomonas mobilis can explain its superiority over lower activity Bdh enzymes from the same family of proteins. Development of two mutants of SmBdh: (1) Q247A where the Gln247 side chain is removed, leaving alanine at position 247 and (2) the double mutant Q247A/V139Q, where the missing glutamine side chain is reinstated at the position 139 that is present in KpBdh. Whereas Q247A will disrupt the active site of the protein, Q247A/V139Q is expected to restore the active site via a compensatory mechanism resulting in the active site being established by a single protein chain without contribution from a symmetry-related molecule (i.e. from the C-terminus of the opposite molecule in the tetramer)
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additional information
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the enzyme from Serratia marcescens is overexpressed in Lactobacillus diolivorans to produce meso-2,3-butanediol (meso-2,3-BTD). A two-step cultivation process with Serratia marcescens is developed for production of 2-butanol in Lactobacillus diolivorans via vitamin B12-dependent diol dehydratase (PduCDE) and alcohol dehydrogenase (pduQ). In the first step of the process, Serratia marcescens is used to produce stereospecifically meso-2,3-BTD from glucose followed by heat inactivation of Serratia marcescens. The accumulated meso-2,3-BTD is then converted during anaerobic fermentation with glucose into 2-butanol by Lactobacillus diolivorans. The process yields a butanol concentration of 10 g/l relying on wild-type bacterial strains. A further improvement of the maximum butanol titer is achieved using an engineered Lactobacillus diolivorans strain overexpressing the endogenous alcohol dehydrogenase pduQ. The two-step cultivation process based on this engineered strain leads to a maximum 2-butanol titer of 13.4 g/l, which means an increase of 34%
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additional information
AEF50077
efficient (3R)-acetoin production from meso-2,3-butanediol using a whole-cell biocatalyst with coexpression of Serratia sp. meso-2,3-butanediol dehydrogenase, Lactobacillus brevis NADH oxidase and Vitreoscilla sp. hemoglobin
additional information
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chiral (3R)-AC production from meso-2,3-butanediol (meso-2,3-BD) is obtained using recombinant Escherichia coli cells co-expressing meso-2,3-butanediol dehydrogenase (meso-2,3-BDH), NADH oxidase (NOX), and hemoglobin protein (VHB) from Serratia sp. T241, Lactobacillus brevis, and Vitreoscilla, respectively. The biocatalysis system of Escherichia coli/pET-mbdh-nox-vgb is developed and the bioconversion conditions are optimized. Under the optimal conditions, 86.74 g/l of (3R)-acetoin with the productivity of 3.61 g/l/h and the stereoisomeric purity of 97.89% is achieved from 93.73 g/l meso-2,3-BD using the whole-cell biocatalysis system, pH 7.0 at 30°C for 12 h. The results show the industrial potential for (3R)-acetoin production via whole-cell biocatalysis. Escherichia coli/pET-mbdh cannot produce acetoin from (2R,3R)-2,3-BD as substrate. To obtain high (3R)-acetoin productivity, a cofactor regeneration system involved in co-expression of meso-2,3-BDH and NOX enzymes from Serratia sp. T241 Lactobacillus brevis is developed in Escherichia coli. The NOX enzyme efficiently oxidizes NADH, which is formed by meso-2,3-BDH, and regenerate NAD+ for the biocatalytic process. The feasibility of (3R)-AC production from the substrate of meso-2,3-BD by whole-cell biocatalysis is conducted, method optimization, overview. A small amount of (3S)-acetoin (1.86 g/l) can also be produced from (2S,3S)-2,3-BD in the substrate 2,3-BD (2.23% of (2S,3S)-2,3-BD) by the biocatalyst
additional information
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the regeneration of oxidised nicotinamide adenine dinucleotide is a key point in preparative application of dehydrogenases for the oxidative route. An electrochemical regeneration system is successfully combined with the BDH catalysed reaction. Up to 48 mM (R)-acetoin is produced in the reaction system while productivities up to 2 mM/h are reached. Possibility to apply an electrochemical system in a semi-preparative synthesis. Lyophilised recombinant ADH-9 from Escherichia coli BL21(DE3) cells is immobilized onto Amberlite FPA54 to 0.01 U per mg carrier leading to increased productivity compared to the immobilised form, method optimization
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