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(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
-
-
?
(2S,3S)-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
?
-
-
-
?
(R,S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
r
(R,S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NADP+
-
-
Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
1,2-propanediol + NAD+
?
-
0.57% activity compared to (2S,3S)-butane-2,3-diol
-
?
1,2-propanediol + NAD+
? + NADH + H+
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
1-butanol + NAD+
butanal + NADH + H+
1-phenylpropanol + NAD+
1-phenylpropan-1-one + NADH + H+
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
? + NAD+
-
-
?
2,3-hexanedione + NADH + H+
?
-
66% activity compared to diacetyl
-
?
2,3-pentanedione + NADH + H+
?
2-butanol + NAD+
2-butanone + NADH + H+
2-pentanol + NAD+
2-pentanone + NADH + H+
3,4-hexanedione + NADH + H+
?
-
10% activity compared to diacetyl
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
diacetyl + NADH
L-acetoin + NAD+
diacetyl + NADH + H+
(2S)-acetoin + NAD+
diacetyl + NADH + H+
?
-
35% activity in comparison to L-acetoin
-
r
ethyl pyruvate + NADH + H+
? + NAD+
-
-
?
glyceraldehyde + NADH + H+
?
isopropanol + NAD+
isopropanal + NADH + H+
-
-
?
L-acetoin + NADH
L-2,3-butanediol
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
-
100% activity
-
r
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
meso-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
r
meso-2,3-butanediol + NAD+
acetoin + NADH
poor substrate
-
?
additional information
?
-
(2S)-acetoin + NADH + H+

(2S,3S)-butane-2,3-diol + NAD+
-
97% activity compared to diacetyl
-
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
r
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+

(2S)-acetoin + NADH + H+
-
100% activity
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+

(S)-acetoin + NADH + H+
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
-
r
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
the enzyme displays absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Under the optimized conditions, the activity of diacetyl reduction is 11.9fold higher than that of (2S,3S)-2,3-butanediol oxidation
-
r
(S,S)-butane-2,3-diol + NAD+

L-acetoin + NADH + H+
-
-
-
?
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
-
-
?
1,3-dihydroxyacetone + NADH + H+

?
-
low activity with 30 mM
-
?
1,3-dihydroxyacetone + NADH + H+
?
-
low activity with 30 mM
-
?
1-butanol + NAD+

butanal + NADH + H+
-
-
?
1-butanol + NAD+
butanal + NADH + H+
-
-
?
2,3-pentanedione + NADH + H+

?
-
69% activity compared to diacetyl
-
?
2,3-pentanedione + NADH + H+
?
-
7% activity in comparison to L-acetoin
-
r
2,3-pentanedione + NADH + H+
?
-
7% activity in comparison to L-acetoin
-
r
2-butanol + NAD+

2-butanone + NADH + H+
-
-
?
2-butanol + NAD+
2-butanone + NADH + H+
-
-
?
2-pentanol + NAD+

2-pentanone + NADH + H+
-
-
?
2-pentanol + NAD+
2-pentanone + NADH + H+
-
-
?
cyclohexanol + NAD+

cyclohexanone + NADH + H+
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
-
-
?
diacetyl + NADH

L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH
L-acetoin + NAD+
-
-
-
ir
diacetyl + NADH
L-acetoin + NAD+
-
-
-
ir
diacetyl + NADH + H+

(2S)-acetoin + NAD+
-
100% activity
-
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
-
-
?
glyceraldehyde + NADH + H+

?
-
low activity with 30 mM
-
?
glyceraldehyde + NADH + H+
?
-
low activity with 30 mM
-
?
L-acetoin + NADH

L-2,3-butanediol
-
stereoisomeric specifity for hydroxyl group in L configuration
-
?
L-acetoin + NADH
L-2,3-butanediol
-
reaction dependent of substrate concentration, incubation time, glucose addition, aeration
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
no oxidadion of several alcohols
-
r
L-acetoin + NADH
L-2,3-butanediol
-
exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
-
r
L-acetoin + NADH
L-2,3-butanediol
-
in presence of adequate amounts of NAD+ and hydrazine and in an alkaline condition acetoin formation is much in favour, acetoin concentrations have no appreciable influence on dehydrogenation of L-butanediol
-
r
L-acetoin + NADH
L-2,3-butanediol
-
in presence of adequate amounts of NAD+ and hydrazine and in an alkaline condition acetoin formation is much in favour, acetoin concentrations have no appreciable influence on dehydrogenation of L-butanediol
-
r
L-acetoin + NADH
L-2,3-butanediol
-
reaction dependent of substrate concentration, incubation time, glucose addition, aeration
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
exhibits marked sequence similarity and common functionally conserved sequence with meso-enzyme
-
r
L-acetoin + NADH
L-2,3-butanediol
-
short chain dehydrogenase reductase family
-
r
L-acetoin + NADH
L-2,3-butanediol
-
no oxidadion of several alcohols
-
r
L-acetoin + NADH
L-2,3-butanediol
-
stereoisomeric specifity for hydroxyl group in L configuration
-
?
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH
L-2,3-butanediol
-
-
-
r
L-acetoin + NADH + H+

(S,S)-butanediol + NAD+
-
To confirm the high production of enzyme, the conversion of L-acetoin, in a racemic mixture, to L-2,3-butanediol is studied. 0.37% L-2,3-butanediol is formed from 1% L-acetoin added to the culture.
-
?
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
-
To confirm the high production of enzyme, the conversion of L-acetoin, in a racemic mixture, to L-2,3-butanediol is studied. 0.37% L-2,3-butanediol is formed from 1% L-acetoin added to the culture.
-
?
additional information

?
-
-
the enzyme shows no activity toward racemic acetoin in the presence of NAD+ as well as no activity with NADPH, 1,4-butanediol, 2,5-hexanedione, 2,4-pentanedione, 2-butanone, methanol, mannitol, and glycerol
-
?
additional information
?
-
-
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
-
?
additional information
?
-
-
not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
-
?
additional information
?
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
?
additional information
?
-
-
enzyme shows activity as a reductase specific for (S)-acetoin, EC 1.1.1.76, and both diacetyl reductase (EC 1.1.1.304) and NAD+-dependent alcohol dehydrogenase (EC 1.1.1.1) activities
-
?
additional information
?
-
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
-
?
additional information
?
-
-
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
-
?
additional information
?
-
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
-
?
additional information
?
-
-
the enzyme accepts a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones, overview. No activity with 4-chloroacetophenone, (R)-1-phenylethanol, and (2R,3R)-2,3-butanediol, poor activity with 3-methyl-2-acetophenone, 4-bromoacetophenone, 2-bromoacetophenone, benzaldehyde, and isophorone
-
?
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Ui, S.; Matsuyama, N.; Masuda, H.; Muraki, H.
Mechanism for the formation of 2,3-butanediol stereoisomers in Klebsiella pneumoniae
J. Ferment. Technol.
62
551-559
1984
Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063
-
brenda
Ui, S.; Masuda, H.; Muraki, H.
Separation and quantitation of 2,3-butanediol isomers ((-), (+), and meso) by a combined use of enzyme and gas chromatography
Agric. Biol. Chem.
48
2837-2838
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
brenda
Ui, S.; Masuda, H.; Muraki, H.
Laboratory-scale production of acetoin isomers (D(-) and L(+)) by bacterial fermentation
J. Ferment. Technol.
62
151-156
1984
Paenibacillus polymyxa, Corynebacterium glutamicum, Saccharomyces cerevisiae, Klebsiella pneumoniae, no activity in Pseudomonas sp., Serratia marcescens, Paenibacillus polymyxa IAM 1189, Corynebacterium glutamicum C-1012, Klebsiella pneumoniae IAM 1063, Saccharomyces cerevisiae OC-2, Serratia marcescens IAM 1022, no activity in Pseudomonas sp. s4
-
brenda
Voloch, M.; Ladisch, M.R.; Rodwell, V.W.; Tsao, G.T.
Reduction of acetoin to 2,3-butanediol in Klebsiella pneumoniae: a new model
Biotechnol. Bioeng.
25
173-183
1983
Klebsiella pneumoniae
brenda
Taylor, M.B.; Juni, E.
Stereoisomeric specificities of 2,3-butanediol dehydrogenase
Biochim. Biophys. Acta
39
448-457
1960
Klebsiella aerogenes, Aeromonas hydrophila, Bacillus subtilis, Paenibacillus polymyxa, Bacillus subtilis Ford
brenda
Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Stereochemical applications of the expression of the L-2,3-butanediol dehydrogenase gene in Escherichia coli
Lett. Appl. Microbiol.
32
93-98
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
brenda
Otagiri, M.; Kurisu, G.; Ui, S.; Ohkuma, M.; Kudo, T.; Kusunoki, M.
Crystallization and preliminary x-ray studies of L-(+)-2,3-butanediol dehydrogenase from Brevibacterium saccharolyticum C-1012
Protein Pept. Lett.
8
57-61
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
brenda
Takusagawa, Y.; Otagiri, M.; Ui, S.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
65
1876-1878
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
brenda
Gonzalez, E.; Fernandez, M.R.; Marco, D.; Calam, E.; Sumoy, L.; Pares, X.; Dequin, S.; Biosca, J.A.
Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol
Appl. Environ. Microbiol.
76
670-679
2010
Saccharomyces cerevisiae
brenda
Otagiri, M.; Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.
Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
FEBS Lett.
584
219-223
2010
Corynebacterium glutamicum (Q9ZNN8)
brenda
Wang, Z.; Song, Q.; Yu, M.; Wang, Y.; Xiong, B.; Zhang, Y.; Zheng, J.; Ying, X.
Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol
Appl. Microbiol. Biotechnol.
98
641-650
2014
Rhodococcus erythropolis (M4N626), Rhodococcus erythropolis, Rhodococcus erythropolis WZ010 (M4N626), Rhodococcus erythropolis WZ010
brenda
Shimegi, T.; Ooyama, T.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.; Ui, S.
Crystallization and preliminary X-ray diffraction analysis of domain-chimeric L-(2S,3S)-butanediol dehydrogenase
Acta Crystallogr. Sect. F
70
461-463
2014
Corynebacterium glutamicum
brenda
Xu, G.C.; Bian, Y.Q.; Han, R.Z.; Dong, J.J.; Ni, Y.
Cloning, expression, and characterization of budC gene encoding meso-2,3-butanediol dehydrogenase from Bacillus licheniformis
Appl. Biochem. Biotechnol.
178
604-617
2016
Bacillus licheniformis
brenda
Jojima, T.; Igari, T.; Moteki, Y.; Suda, M.; Yukawa, H.; Inui, M.
Promiscuous activity of (S,S)-butanediol dehydrogenase is responsible for glycerol production from 1,3-dihydroxyacetone in Corynebacterium glutamicum under oxygen-deprived conditions
Appl. Microbiol. Biotechnol.
99
1427-1433
2015
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
brenda
Takeda, M.; Anamizu, S.; Motomatsu, S.; Chen, X.; Thapa Chhetri, R.
Identification and characterization of a mycobacterial NAD+-dependent alcohol dehydrogenase with superior reduction of diacetyl to (S)-acetoin
Biosci. Biotechnol. Biochem.
78
1879-1886
2014
Mycobacterium sp. (W8VSK8), Mycobacterium sp., Mycobacterium sp. B-009 (W8VSK8)
brenda
Shimegi, T.; Mochizuki, K.; Oyama, T.; Ohtsuki, T.; Kusunoki, M.; Ui, S.
Modification of chimeric (2S, 3S)-butanediol dehydrogenase based on structural information
Protein Pept. Lett.
22
226-233
2015
Corynebacterium glutamicum
brenda
Wang, Y.; Li, L.; Ma, C.; Gao, C.; Tao, F.; Xu, P.
Engineering of cofactor regeneration enhances (2S,3S)-2,3-butanediol production from diacetyl
Sci. Rep.
3
2643
2013
Corynebacterium glutamicum
brenda