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(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
(2R,3R)-2,3-butanediol + NADP+
(R)-acetoin + NADPH + H+
no detectable activity with (2S,3S)-2,3-butanediol
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
?
69.5% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
(3R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
-
-
-
-
?
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
(3R,3S)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
(3S)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
-
-
-
?
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
73% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction, very low activity with the (S)-enantiomer
-
-
?
(R)-1-phenyl-1,2-ethanediol + NAD+
?
32.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADPH + H+
(2R,3R)-2,3-butanediol + NAD+
-
-
-
?
(R)-acetoin + NADPH + H+
(2R,3R)-butane-2,3-diol + NADP+
wild type enzyme does not use NADPH as coenzyme
-
-
?
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
(R,S)-3-hydroxy-2-pentanone + NADH
2,3-pentanediol + NAD+
-
-
-
r
(R,S)-4-hydroxy-3-pentanone + NADH
2,3-pentanediol + NAD+
-
-
-
r
1,2-butanediol + NAD+
?
-
-
-
-
?
1,2-hexanediol + NAD+
? + NADH + H+
50% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
?
1,2-pentandiol + NAD+
? + NADH + H+
-
-
-
r
1,2-pentanediol + NAD+
? + NADH + H+
74% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
?
1,2-propandiol + NAD+
? + NADH + H+
-
-
-
r
1,3-dihydroxyacetone + NADH + H+
?
-
low activity
-
-
?
1-hydroxy-2-butanone + NADH
?
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
?
-
low activity
-
-
?
1-hydroxy-2-butanone + NADH + H+
? + NAD+
-
-
-
?
1-hydroxy-2-propanone + NADH + H+
propane-1,2-diol + NAD+
-
-
-
-
r
2,2,2-trifluoroacetophenone + NADH + H+
?
2,3-butanediol + NAD+
acetoin + NADH
2,3-butanediol + NAD+
acetoin + NADH + H+
-
-
-
-
r
2,3-hexanedione + NADH + H+
(3R)-3-hydroxy-2-hexanone + NAD+
2,3-pentandione + NADH + H+
? + NAD+
-
-
-
?
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
2,3-pentanediol + NAD+
?
-
-
-
-
r
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
2-butanone + NADP+
2-butanol + NADPH + H+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(R)-1-phenyl-1,2-ethanediol + NAD+
2-hydroxyacetophenone + NADH + H+
?
8.7% activity compared to (R)-acetoin
-
-
?
2-octanone + NADH + H+
?
9.3% activity compared to (R)-acetoin
-
-
?
2-pentanone + NADH + H+
(S)-2-pentanol + NAD+
-
-
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
3,4-hexanedione + 2 NADH + 2 H+
(3R,4R)-3,4-hexanediol + 2 NAD+
-
-
-
r
3-methyl-2-butenal + NADH + H+
?
16.7% activity compared to (R)-acetoin
-
-
?
5-methyl-2,3-hexanedione + NADH + H+
(3R)-5-methyl-3-hydroxy-2-hexanone + NAD+
acetaldehyde + NADH + H+
ethanol + NAD+
acetaldehyde + NADPH + H+
ethanol + NADP+
acetoin + 2 NADPH + 2 H+
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + 2 NADP+
-
-
-
r
acetoin + NAD+
diacetyl + NADH
-
18% of the activity with 2,3-butanediol, in the reverse reaction 150% of the activity with acetoin
-
-
r
acetoin + NADH
2,3-butanediol + NAD+
-
-
-
-
r
acetoin + NADH + H+
(R,R)-butanediol + NAD+
acetoin + NADH + H+
2,3-butanediol + NAD+
acetoin + NADPH + H+
(R,R)-butanediol + NADP+
acetone + NADPH + H+
propan-2-ol + NADP+
-
-
-
?
butane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
butane-1,3-diol + NAD+
?
14.7% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
butane-1,4-diol + NAD+
?
2.9% activity compared to (R,R)-butane-2,3-diol
-
-
?
butanone + NADH + H+
?
-
low activity
-
-
?
butanone + NADPH + H+
butan-2-ol + NADP+
-
-
-
?
cyclohexanone + NADH
?
-
38% of the activity with acetoin
-
-
?
diacetyl + 2 NADH + 2 H+
(2R,3R)-butane-2,3-diol + 2 NAD+
-
-
-
r
diacetyl + NADH
2,3-butanediol + NAD+
diacetyl + NADH + H+
(2S)-acetoin + NAD+
diacetyl + NADH + H+
(3R)-acetoin + NAD+
-
-
-
r
diacetyl + NADH + H+
(3S)-acetoin + NAD+
diacetyl + NADH + H+
(R)-acetoin + NAD+
diacetyl + NADH + H+
acetoin + NAD+
dihydroxyacetone + NADH
?
-
36% of the activity with acetoin
-
-
?
dihydroxyacetone phosphate + NADH
?
-
82% of the activity with acetoin
-
-
?
ethyl 4-chloro-3-hydroxybutyrate + NAD+
?
12.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
ethyl pyruvate + NADH
?
-
-
-
-
?
formaldehyde + NADH + H+
? + NAD+
-
-
-
?
formaldehyde + NADPH + H+
? + NADP+
-
-
-
?
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
furfural + NADPH + H+
(furan-2-yl)methanol + NADP+
-
-
-
?
glycerol + NAD+
? + NADH + H+
-
-
-
r
glycolaldehyde + NADH + H+
? + NAD+
-
-
-
?
hexaldehyde + NADH + H+
? + NAD+
-
-
-
?
hexane-2,5-dione + NADH + H+
?
-
low activity
-
-
?
hydroxyacetone + NADH
1,2-propanediol
-
-
-
?
isobutanol + NAD+
?
0.4% activity compared to (R,R)-butane-2,3-diol
-
-
?
meso-2,3-butanediol + NAD+
?
-
-
-
-
r
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
meso-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
meso-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
?
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
methyl glyoxal + NADH
?
-
-
-
-
?
methyl pyruvate + NADH
?
-
-
-
-
?
n-butylaldehyde + NADH + H+
?
-
low activity
-
-
?
pentane-1,2-diol + NAD+
?
-
very low activity
-
-
?
pentane-2,3-dione + NADH + H+
?
-
low activity
-
-
?
pentane-2,4-dione + NADH + H+
?
-
low activity
-
-
?
propane-1,2-diol + NAD+
?
propane-1,2-diol + NAD+
? + NADH + H+
-
-
-
?
propane-1,3-diol + NAD+
?
1.4% activity compared to (R,R)-butane-2,3-diol
-
-
?
propionaldehyde + NADH + H+
? + NAD+
-
-
-
?
pyruvic aldehyde + NADH
?
-
81% of the activity with acetoin
-
-
?
rac acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
-
-
-
?
rac acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
-
-
-
?
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
sodium lactate + NAD+
?
10.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
additional information
?
-
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
-
r
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
-
r
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
-
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
-
?
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
-
?
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
preferred substrate
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
preferred substrate, very low activity with the (S)-enantiomer
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
-
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
preferred substrate in the reduction reaction
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
preferred substrate in the reduction reaction
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
-
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
slightly preferred substrate
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
slightly preferred substrate
-
-
r
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
-
-
-
?
(2R,3S)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
the enzyme is not absolutely specific for (S)-acetoin, though this is the preferred substrate
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
-
the enzyme is not absolutely specific for (S)-acetoin, though this is the preferred substrate
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
very low activity
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
very low activity
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
-
-
-
-
?
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
-
-
r
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
-
-
r
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
-
the enzyme shows lower Km value and higher catalytic efficiency for (3S/3R)-acetoin in comparison to those for (2R,3R)-2,3-butanediol and meso-2,3-butanediol, the reduction reaction is preferred, low activity with (2R,3R)-2,3-butanediol
-
-
r
(3R,3S)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
-
-
-
-
?
(3R,3S)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
-
-
-
-
?
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
the activity of (R)-acetoin reduction is 7.7times higher than that of (2R,3R)-butane-2,3-diol oxidation at pH 7.0
-
-
r
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
the activity of (R)-acetoin reduction is 7.7times higher than that of (2R,3R)-butane-2,3-diol oxidation at pH 7.0
-
-
r
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
-
-
-
?
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
low activity
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
low activity
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
high level production of (R,R)-butane-2,3-diol
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
high level production of (R,R)-butane-2,3-diol
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
stereoselective interconversion
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
preferred substrate, 100% activity
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
preferred substrate, 100% activity
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
effects of growth substrate on enzyme activity in vivo, overview
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
effects of growth substrate on enzyme activity in vivo, overview
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
effects of growth substrate on enzyme activity in vivo, overview
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
effects of growth substrate on enzyme activity in vivo, overview
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
r
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
-
?
1,2-propanediol + NAD+
?
-
-
-
-
r
1,2-propanediol + NAD+
?
-
-
-
-
?
1,4-butanediol + NAD+
?
-
low activity
-
-
r
1,4-butanediol + NAD+
?
-
low activity
-
-
r
2,2,2-trifluoroacetophenone + NADH + H+
?
28% activity compared to (R)-acetoin
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
?
28% activity compared to (R)-acetoin
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
-
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
-
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
2,3-butanediol without specification of stereochemistry
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
D(-)-2,3-butandiol
-
-
?
2,3-butanediol + NAD+
acetoin + NADH
-
2,3-butanediol without specification of stereochemistry
-
r
2,3-butanediol + NAD+
acetoin + NADH
-
oxidation occurs selectively at the (R)-center of 2,3-butanediol
-
r
2,3-hexanedione + NADH + H+
(3R)-3-hydroxy-2-hexanone + NAD+
small amounts of (2R)-2-hydroxy-3-hexanone are produced as by-product
-
-
r
2,3-hexanedione + NADH + H+
(3R)-3-hydroxy-2-hexanone + NAD+
small amounts of (2R)-2-hydroxy-3-hexanone are produced as by-product
-
-
r
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
-
-
-
-
?
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
-
racemate
-
r
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
small amounts of 2,3-pentanediol are produced as by-product
-
-
r
2,3-pentanedione + NADH + H+
3-hydroxy-2-pentanone + NAD+
small amounts of 2,3-pentanediol are produced as by-product
-
-
r
2-hydroxyacetophenone + NADH + H+
(R)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(R)-1-phenyl-1,2-ethanediol + NAD+
over 99% enantiomeric excess
-
-
?
2-hydroxyacetophenone + NADH + H+
(R)-1-phenyl-1,2-ethanediol + NAD+
-
-
-
?
2-hydroxyacetophenone + NADH + H+
(R)-1-phenyl-1,2-ethanediol + NAD+
over 99% enantiomeric excess
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
-
-
-
r
2-propanol + NAD+
2-propanone + NADH + H+
-
-
-
r
5-methyl-2,3-hexanedione + NADH + H+
(3R)-5-methyl-3-hydroxy-2-hexanone + NAD+
small amounts of 5-methyl-2-hydroxy-3-hexanone and traces of (3S)-5-methyl-3-hydroxy-2-hexanone are produced as by-products
-
-
r
5-methyl-2,3-hexanedione + NADH + H+
(3R)-5-methyl-3-hydroxy-2-hexanone + NAD+
small amounts of 5-methyl-2-hydroxy-3-hexanone and traces of (3S)-5-methyl-3-hydroxy-2-hexanone are produced as by-products
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
acetoin + NADH + H+
(R,R)-butanediol + NAD+
-
-
-
-
?
acetoin + NADH + H+
(R,R)-butanediol + NAD+
-
-
-
-
?
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
enzyme 1, only meso-2,3-butanediol is formed, enzyme 2 gives mixture of meso- and optical isomers
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
-
-
-
-
r
acetoin + NADPH + H+
(R,R)-butanediol + NADP+
-
-
-
-
?
acetoin + NADPH + H+
(R,R)-butanediol + NADP+
-
-
-
-
?
butane-1,2-diol + NAD+
?
-
low activity
-
-
?
butane-1,2-diol + NAD+
?
76.6% activity compared to (R,R)-butane-2,3-diol
-
-
?
butane-1,2-diol + NAD+
?
76.6% activity compared to (R,R)-butane-2,3-diol
-
-
?
diacetyl + NADH
2,3-butanediol + NAD+
-
-
-
-
?
diacetyl + NADH
2,3-butanediol + NAD+
-
-
enzyme 1, only meso-2,3-butanediol is formed, enzyme 2 gives mixture of meso- and optical isomers
r
diacetyl + NADH
2,3-butanediol + NAD+
-
-
-
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
-
-
-
-
?
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
ir
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
ir
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(3S)-acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
(R)-acetoin + NAD+
69.3% activity compared to (R)-acetoin
-
-
r
diacetyl + NADH + H+
(R)-acetoin + NAD+
69.3% activity compared to (R)-acetoin
-
-
r
diacetyl + NADH + H+
acetoin + NAD+
-
low activity
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
-
low activity
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
88.2% activity compared to acetoin
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
88.2% activity compared to acetoin
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
-
-
-
-
r
diacetyl + NADH + H+
acetoin + NAD+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
-
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
-
-
?
diacetyl + NADH + H+
acetoin + NAD+
-
diacetyl can be converted into 2,3-butanediol via acetoin by the enzyme
-
-
?
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
-
-
-
?
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
-
-
-
?
glycerol + NAD+
?
-
-
-
-
?
glycerol + NAD+
?
-
-
-
-
?
glycerol + NAD+
?
16.3% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
glycerol + NAD+
?
16.3% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
isopropanol + NAD+
?
-
low activity
-
-
r
isopropanol + NAD+
?
-
low activity
-
-
r
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
(3S)-acetoin
r
meso-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
-
-
-
?
meso-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
-
-
-
-
?
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
93.6% activity compared to (R,R)-butane-2,3-diol
-
-
?
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
93.6% activity compared to (R,R)-butane-2,3-diol
-
-
?
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
61% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
r
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
-
-
-
r
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
72% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
r
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
-
-
-
-
r
propane-1,2-diol + NAD+
?
-
low activity
-
-
?
propane-1,2-diol + NAD+
?
58.6% activity compared to (R,R)-butane-2,3-diol
-
-
?
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
-
-
-
?
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
68% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
?
additional information
?
-
substrate specificity analysis, overview. Enzyme BcBDH catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione, and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. The biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated. Stereoselectivity and conversion is analyzed by carrying out the reduction reaction of selected diketones and alpha-hydroxyketones
-
-
-
additional information
?
-
substrate specificity analysis, overview. Enzyme BcBDH catalyzes the selective asymmetric reduction of prochiral 1,2-diketones to the corresponding HK and, in some cases, the reduction of the same to the corresponding 1,2-diols. Aliphatic diketones, like 2,3-pentanedione, 2,3-hexanedione, 5-methyl-2,3-hexanedione, 3,4-hexanedione, and 2,3-heptanedione are well transformed. In addition, surprisingly alkyl phenyl dicarbonyls, like 2-hydroxy-1-phenylpropan-1-one and phenylglyoxal are accepted, whereas their derivatives with two phenyl groups are not substrates. The biocatalytic reduction of 5-methyl-2,3-hexanedione to mainly 5-methyl-3-hydroxy-2-hexanone with only small amounts of 5-methyl-2-hydroxy-3-hexanone within an enzyme membrane reactor is demonstrated. Stereoselectivity and conversion is analyzed by carrying out the reduction reaction of selected diketones and alpha-hydroxyketones
-
-
-
additional information
?
-
-
no activity with meso-butane-2,3-diol, glycerol, glycerol-3-phosphate, 1,3-dihydroxyacetone, dihydroxyacetonephosphate, glyceraldehyde-3-phosphate, 2-butanol, and 1,3-butanediol
-
-
?
additional information
?
-
-
no activity with meso-butane-2,3-diol, glycerol, glycerol-3-phosphate, 1,3-dihydroxyacetone, dihydroxyacetonephosphate, glyceraldehyde-3-phosphate, 2-butanol, and 1,3-butanediol
-
-
?
additional information
?
-
no activity with (S,S)-butane-2,3-diol
-
-
?
additional information
?
-
no activity with (S,S)-butane-2,3-diol
-
-
?
additional information
?
-
an enantiocomplementary carbonyl reductase, 2,3-butanediol dehydrogenase (BDHA) from Bacillus subtilis is discovered to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) with excellent stereochemical selectivity. No activity with NADPH
-
-
-
additional information
?
-
an enantiocomplementary carbonyl reductase, 2,3-butanediol dehydrogenase (BDHA) from Bacillus subtilis is discovered to convert 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) with excellent stereochemical selectivity. No activity with NADPH
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
enzyme is a strictly NADPH-dependent primary-secondary alcohol dehydrogenase able to reduce acetoin to 2,3-butanediol. The enzyme accepts a range of 2-, 3-, and 4-carbon substrates, including the nonphysiological ketones acetone and butanone
-
-
?
additional information
?
-
-
enzyme is a strictly NADPH-dependent primary-secondary alcohol dehydrogenase able to reduce acetoin to 2,3-butanediol. The enzyme accepts a range of 2-, 3-, and 4-carbon substrates, including the nonphysiological ketones acetone and butanone
-
-
?
additional information
?
-
-
no activity with (2S,3S)-butane-2,3-diol or diacetyl
-
-
?
additional information
?
-
-
no activity with (2S,3S)-butane-2,3-diol or diacetyl
-
-
?
additional information
?
-
substrate specificity, overview. No or poor activity with ethanol, ethylene glycol, diethylene glycol, 1-propanol, 2-propanol, 1,3-propanediol, glycerol, dipropylene glycol, 1-butanol, 1,4-butanediol, 1,2,4-butanetriol, (2S,3S)-butane-2,3-diol, 1,5-pentanediol, 2,4-pentanediol, 3-methyl-1,5-pentandiol, and 1,2,6-hexantriol
-
-
?
additional information
?
-
production of 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
-
-
-
additional information
?
-
production of 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
-
-
-
additional information
?
-
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
-
-
?
additional information
?
-
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
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-
?
additional information
?
-
-
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
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-
?
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with (2S,3S)-2,3-butane-2,3-diol, but the (2R,3R)-2,3-butanediol dehydrogenase is also active with meso-2,3-butanediol. 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
-
-
-
additional information
?
-
no activity with acetoin plus NAD+ or (2S,3S)-butane-2,3-diol witrh NAD+, or (S)-1-phenyl-1,2-ethanediol plus NAD+. 5% or less activity with 2-butanol, ethyl lactate, isopropanol, 1-butanol, cyclohexanol, 2-pentanol, 2-octanol, acetophenone, and 4-hydroxy-2-butanone
-
-
?
additional information
?
-
no activity with acetoin plus NAD+ or (2S,3S)-butane-2,3-diol witrh NAD+, or (S)-1-phenyl-1,2-ethanediol plus NAD+. 5% or less activity with 2-butanol, ethyl lactate, isopropanol, 1-butanol, cyclohexanol, 2-pentanol, 2-octanol, acetophenone, and 4-hydroxy-2-butanone
-
-
?
additional information
?
-
-
no activity with acetoin plus NAD+ or (2S,3S)-butane-2,3-diol witrh NAD+, or (S)-1-phenyl-1,2-ethanediol plus NAD+. 5% or less activity with 2-butanol, ethyl lactate, isopropanol, 1-butanol, cyclohexanol, 2-pentanol, 2-octanol, acetophenone, and 4-hydroxy-2-butanone
-
-
?
additional information
?
-
-
3S)-2,3-butanediol, (3R/3S)-acetoin, glycerol, sorbitol or xylitol are no substrates
-
-
?
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh1p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for glycolaldehyde or hexaldehyde with NADPH. Propionaldehyde is a poor substrate, no activity with glutaraldehyde
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh1p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for glycolaldehyde or hexaldehyde with NADPH. Propionaldehyde is a poor substrate, no activity with glutaraldehyde
-
-
-
additional information
?
-
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh1p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for glycolaldehyde or hexaldehyde with NADPH. Propionaldehyde is a poor substrate, no activity with glutaraldehyde
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh2p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for furfural, propionaldehyde, or hexaldehyde with NADPH. Glutaraldehyde is a poor substrate
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh2p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for furfural, propionaldehyde, or hexaldehyde with NADPH. Glutaraldehyde is a poor substrate
-
-
-
additional information
?
-
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh2p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for furfural, propionaldehyde, or hexaldehyde with NADPH. Glutaraldehyde is a poor substrate
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh1p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for glycolaldehyde or hexaldehyde with NADPH. Propionaldehyde is a poor substrate, no activity with glutaraldehyde
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh1p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for glycolaldehyde or hexaldehyde with NADPH. Propionaldehyde is a poor substrate, no activity with glutaraldehyde
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh2p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for furfural, propionaldehyde, or hexaldehyde with NADPH. Glutaraldehyde is a poor substrate
-
-
-
additional information
?
-
enzyme Bdh1p exhibits (2R,3R)-2,3-butanediol dehydrogenase activity, but Bdh2p also exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. No activity for furfural, propionaldehyde, or hexaldehyde with NADPH. Glutaraldehyde is a poor substrate
-
-
-
additional information
?
-
-
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
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-
?
additional information
?
-
-
the purified enzyme glycerol dehydrogenase, GDH EC 1.1.1.6, also catalyzes the interconversion of (3S)-acetoin/meso-2,3-butanediol and (3R)-acetoin/(2R,3R)-2,3-butanediol. (2S,3S)-2,3-Butanediol is not a substrate for the GDH at all. Also no activity with 1-propanol, 1-butanol, isopentanol, ethylene glycol, ethanol, and (3S/3R)-acetoin in the oxidation reaction, and poor activity with formaldehyde in the reduction reaction
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-
?
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evolution
the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
the enzyme has homology to the medium-chain dehydrogenases/reductases with preference for secondary alcohols, phylogenetic analysis
evolution
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the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
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 R-selective 2,3-butanediol dehydrogenase from Bacillus clausii strain DSM 8716 (BcBDH) belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR)
evolution
two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of Saccharomyces cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), are members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural
evolution
-
the Serratia marcescens enzyme belongs to the type III Fe-ADH superfamily, three consecutive glycine residues belong to a 14-amino acid residue motif (GDK motif) as the coenzyme NAD(H) binding site, and three conserved histidine residues belong to a 16-residue segment that is homologous to the 15-residue stretch as the binding site of metal
-
evolution
-
two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of Saccharomyces cerevisiae, Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), are members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibit reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural
-
evolution
-
the R-selective 2,3-butanediol dehydrogenase from Bacillus clausii strain DSM 8716 (BcBDH) belongs to the metal-dependent medium chain dehydrogenases/reductases family (MDR)
-
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 (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
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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 (2R,3R)-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 (2R,3R)-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 (2R,3R)-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 (2R,3R)-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 (2R,3R)-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 (2R,3R)-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 (2R,3R)-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 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 (2R,3R)-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
-
metabolism
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BDH2 is a gene adjacent to BDH1, and these genes are regulated reciprocally. BDH2 is only responsible for converting diacetyl into acetoin, but not for the metabolic pathway of acetoin to 2,3-butanediol in Saccharomyces uvarum
metabolism
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overview of 2,3-BDL biosynthesis pathway and byproducts in microaerobic conditions of Paenibacillus polymyxa strain DSM 365 starting from sucrose as a substrate
metabolism
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
metabolism
-
overview of 2,3-BDL biosynthesis pathway and byproducts in microaerobic conditions of Paenibacillus polymyxa strain DSM 365 starting from sucrose as a substrate
-
metabolism
-
BDH2 is a gene adjacent to BDH1, and these genes are regulated reciprocally. BDH2 is only responsible for converting diacetyl into acetoin, but not for the metabolic pathway of acetoin to 2,3-butanediol in Saccharomyces uvarum
-
metabolism
-
the proposed pathway from glucose to 2,3-butanediol in Paenibacillus brasilensis involves the enzyme, overview
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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
-
glycerol/1,2-propanediol dehydrogenase GldA is the major enzyme responsible for the acetoin reducing activity observed in Escherichia coli
physiological function
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
physiological function
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
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 multifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
physiological function
-
the enzyme is involved in formation of diacetyl in wine
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
the enzyme is involved in formation of diacetyl in wine
-
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
glycerol/1,2-propanediol dehydrogenase GldA is the major enzyme responsible for the acetoin reducing activity observed in Escherichia coli
-
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
22,3-butanediol (2,3-BD) exists in three stereoisomeric forms: (2R,3R)-2,3-BD, meso-2,3-BD and (2S,3S)-2,3-BD. All three stereoisomers are transformed into acetoin by (2R,3R)-2,3-butanediol dehydrogenase (BDH) or (2S,3S)-2,3-BDH. Acetoin is cleaved to form acetyl-CoA and acetaldehyde by acetoin dehydrogenase enzyme system (AoDH ES). Genes encoding (2R,3R)-2,3-BDH, (2S,3S)-2,3-BDH and the E1 and E2 components of AoDH ES are identified as part of a 2,3-BD utilization operon. In addition, the regulatory protein AcoR promotes the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector. Proposed model for 2,3-BD utilization in Pseudomonas aeruginosa strain PAO1 in downstream catabolic pathways, overview. Genes pa4148, pa4149, pa4150, pa4151, pa4152 and pa4153 comprise an operon responsible for 2,3-BD utilization, mutational analysis. Acetaldehyde is the direct inducer of the 2,3-BD utilization operon
-
physiological function
-
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 multifunctional as R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase
-
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
-
22,3-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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Cloning, expression and characterization of a novel (2R,3R) -2,3-butanediol dehydrogenase from Bacillus thuringiensis
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22
10137
2019
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-
brenda
Yamada, R.; Wakita, K.; Mitsui, R.; Nishikawa, R.; Ogino, H.
Efficient production of 2,3-butanediol by recombinant Saccharomyces cerevisiae through modulation of gene expression by cocktail delta-integration
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245
1558-1566
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Bacillus amyloliquefaciens (S6FPW0), Bacillus amyloliquefaciens UCMB5033 (S6FPW0)
brenda
Subramanian, V.; Lunin, V.V.; Farmer, S.J.; Alahuhta, M.; Moore, K.T.; Ho, A.; Chaudhari, Y.B.; Zhang, M.; Himmel, M.E.; Decker, S.R.
Phylogenetics-based identification and characterization of a superior 2,3-butanediol dehydrogenase for Zymomonas mobilis expression
Biotechnol. Biofuels
13
186
2020
no activity in Serratia marcescens
brenda
Cui, Z.; Zhang, J.; Fan, X.; Zheng, G.; Chang, H.; Wei, W.
Highly efficient bioreduction of 2-hydroxyacetophenone to (S)- and (R)-1-phenyl-1,2-ethanediol by two substrate tolerance carbonyl reductases with cofactor regeneration
J. Biotechnol.
243
1-9
2017
Bacillus subtilis subsp. subtilis (O34788), Bacillus subtilis subsp. subtilis 168 (O34788)
brenda
Li, P.; Guo, X.; Shi, T.; Hu, Z.; Chen, Y.; Du, L.; Xiao, D.
Reducing diacetyl production of wine by overexpressing BDH1 and BDH2 in Saccharomyces uvarum
J. Ind. Microbiol. Biotechnol.
44
1541-1550
2017
Saccharomyces uvarum, Saccharomyces uvarum WY1
brenda
Schilling, C.; Ciccone, R.; Sieber, V.; Schmid, J.
Engineering of the 2,3-butanediol pathway of Paenibacillus polymyxa DSM 365
Metab. Eng.
61
381-388
2020
Paenibacillus polymyxa, Paenibacillus polymyxa DSM 365
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Zhang, X.; Han, R.; Bao, T.; Zhao, X.; Li, X.; Zhu, M.; Yang, T.; Xu, M.; Shao, M.; Zhao, Y.; Rao, Z.
Synthetic engineering of Corynebacterium crenatum to selectively produce acetoin or 2,3-butanediol by one step bioconversion method
Microb. Cell Fact.
18
128
2019
Bacillus subtilis subsp. subtilis (O34788), Bacillus subtilis subsp. subtilis 168 (O34788)
brenda
Zhang, J.; Zhao, X.; Zhang, J.; Zhao, C.; Liu, J.; Tian, Y.; Yang, L.
Effect of deletion of 2,3-butanediol dehydrogenase gene (bdhA) on acetoin production of Bacillus subtilis
Prep. Biochem. Biotechnol.
47
761-767
2017
Bacillus subtilis (O34788), Bacillus subtilis, Bacillus subtilis BS168D (O34788)
brenda
Muschallik, L.; Molinnus, D.; Jablonski, M.; Kipp, C.; Bongaerts, J.; Pohl, M.; Wagner, T.; Schoening, M.; Selmer, T.; Siegert, P.
Synthesis of alpha-hydroxy ketones and vicinal (R,R)-diols by Bacillus clausii DSM 8716T butanediol dehydrogenase
RSC Adv.
10
12206-12216
2020
Alkalihalobacillus clausii (A0A223LRZ7), Alkalihalobacillus clausii DSM 8716T (A0A223LRZ7)
-
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