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(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
-
-
-
?
meso-2,3-butanediol + NAD+
acetoin + NADH
poor substrate
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
-
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
-
low activity with 30 mM
-
-
?
2,3-pentanedione + NADH + H+
?
-
7% activity in comparison to L-acetoin
-
-
r
diacetyl + NADH
L-acetoin + NAD+
-
also reduction of 2,3-pentanedione
-
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
?
-
35% activity in comparison to L-acetoin
-
-
r
glyceraldehyde + NADH + H+
?
-
low activity with 30 mM
-
-
?
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+
-
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
?
-
-
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
-
-
?
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
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Ui, S.; Masuda, H.; Muraki, H.
Separation and quantitation of 2,3-butanediol isomers ((-), (+), and meso) by a combined use of enzyme and gas chromatography
Agric. Biol. Chem.
48
2837-2838
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
brenda
Ui, S.; Masuda, H.; Muraki, H.
Laboratory-scale production of acetoin isomers (D(-) and L(+)) by bacterial fermentation
J. Ferment. Technol.
62
151-156
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012, Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063, no activity in Pseudomonas sp., no activity in Pseudomonas sp. s4, Paenibacillus polymyxa, Paenibacillus polymyxa IAM 1189, Saccharomyces cerevisiae, Saccharomyces cerevisiae OC-2, Serratia marcescens, Serratia marcescens IAM 1022
-
brenda
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
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
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
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
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