Information on EC 1.1.1.4 - (R,R)-butanediol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.4
-
RECOMMENDED NAME
GeneOntology No.
(R,R)-butanediol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH + H+
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R,R)-butanediol biosynthesis
-
-
(R,R)-butanediol degradation
-
-
Butanoate metabolism
-
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acetoin degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(R,R)-butane-2,3-diol:NAD+ oxidoreductase
Also converts diacetyl into acetoin with NADH as reductant.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-09-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
authors suggest systematic name: -glycol:NAD+ oxidoreductase ???
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Ov 421, isolated from ovine milk
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Manually annotated by BRENDA team
strain Ov 421, isolated from ovine milk
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Manually annotated by BRENDA team
strain ET C9, isolated from artisanal goat's milk cheese
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-
Manually annotated by BRENDA team
strain ET C9, isolated from artisanal goat's milk cheese
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Manually annotated by BRENDA team
strain ME-303
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Manually annotated by BRENDA team
strain ME-303
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-
Manually annotated by BRENDA team
2,3-butanediol dehydrogenase 1 and 2; subsp. lactis D10
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
gene mbd1
UniProt
Manually annotated by BRENDA team
gene mbd1
UniProt
Manually annotated by BRENDA team
isolated from soil
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
show the reaction diagram
(2R,3R)-2,3-butanediol + NADP+
(R)-acetoin + NADPH + H+
show the reaction diagram
no detectable activity with (2S,3S)-2,3-butanediol
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
?
show the reaction diagram
69.5% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
show the reaction diagram
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
show the reaction diagram
(2S,3S)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
(3R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
show the reaction diagram
-
-
-
-
?
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
show the reaction diagram
(3R,3S)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
show the reaction diagram
(3S)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
show the reaction diagram
-
-
-
-
?
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
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+
?
show the reaction diagram
32.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
show the reaction diagram
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
show the reaction diagram
(R)-acetoin + NADPH + H+
(2R,3R)-2,3-butanediol + NAD+
show the reaction diagram
-
-
-
-
?
(R)-acetoin + NADPH + H+
(2R,3R)-butane-2,3-diol + NADP+
show the reaction diagram
wild type enzyme does not use NADPH as coenzyme
-
-
?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
(R,S)-3-hydroxy-2-pentanone + NADH
2,3-pentanediol + NAD+
show the reaction diagram
-
-
-
r
(R,S)-4-hydroxy-3-pentanone + NADH
2,3-pentanediol + NAD+
show the reaction diagram
-
-
-
r
1,2-butanediol + NAD+
?
show the reaction diagram
-
-
-
-
?
1,2-hexanediol + NAD+
? + NADH + H+
show the reaction diagram
50% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
?
1,2-pentandiol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
r
1,2-pentanediol + NAD+
? + NADH + H+
show the reaction diagram
74% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
-
-
?
1,2-propandiol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
r
1,2-propanediol + NAD+
?
show the reaction diagram
-
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
show the reaction diagram
1-hydroxy-2-butanone + NADH
?
show the reaction diagram
-
-
-
-
?
1-hydroxy-2-butanone + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
1-hydroxy-2-propanone + NADH + H+
propane-1,2-diol + NAD+
show the reaction diagram
-
-
-
-
r
2,2,2-trifluoroacetophenone + NADH + H+
?
show the reaction diagram
2,3-butanediol + NAD+
acetoin + NADH
show the reaction diagram
2,3-butanediol + NAD+
acetoin + NADH + H+
show the reaction diagram
-
-
-
-
r
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
show the reaction diagram
2-butanone + NADP+
2-butanol + NADPH + H+
show the reaction diagram
-
-
-
-
?
2-hydroxyacetophenone + NADH + H+
?
show the reaction diagram
8.7% activity compared to (R)-acetoin
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?
2-octanone + NADH + H+
?
show the reaction diagram
9.3% activity compared to (R)-acetoin
-
-
?
2-pentanone + NADH
(S)-2-pentanol + NAD+
show the reaction diagram
-
-
-
-
?
2-propanol + NAD+
2-propanone + NADH + H+
show the reaction diagram
3-methyl-2-butenal + NADH + H+
?
show the reaction diagram
16.7% activity compared to (R)-acetoin
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
-
-
-
?
acetoin + 2 NADPH + 2 H+
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + 2 NADP+
show the reaction diagram
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-
r
acetoin + NAD+
diacetyl + NADH
show the reaction diagram
-
18% of the activity with 2,3-butanediol, in the reverse reaction 150% of the activity with acetoin
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r
acetoin + NADH
2,3-butanediol + NAD+
show the reaction diagram
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-
-
-
r
acetoin + NADH + H+
2,3-butanediol + NAD+
show the reaction diagram
acetone + NADPH + H+
propan-2-ol + NADP+
show the reaction diagram
butane-1,2-diol + NAD+
?
show the reaction diagram
butane-1,3-diol + NAD+
?
show the reaction diagram
14.7% activity compared to (2R,3R)-butane-2,3-diol
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-
?
butane-1,4-diol + NAD+
?
show the reaction diagram
butanone + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
butanone + NADPH + H+
butan-2-ol + NADP+
show the reaction diagram
-
-
-
?
cyclohexanone + NADH
?
show the reaction diagram
-
38% of the activity with acetoin
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?
diacetyl + NADH
2,3-butanediol + NAD+
show the reaction diagram
diacetyl + NADH + H+
(2S)-acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
(R)-acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
acetoin + NADH + H+
show the reaction diagram
-
low activity
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?
diacetyl + NADH + H+
acetoin + NADH+
show the reaction diagram
88.2% activity compared to acetoin
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-
?
dicaetyl + NADH + H+
(3S)-acetoin + NAD+
show the reaction diagram
dihydroxyacetone + NADH
?
show the reaction diagram
-
36% of the activity with acetoin
-
-
?
dihydroxyacetone phosphate + NADH
?
show the reaction diagram
-
82% of the activity with acetoin
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-
?
ethyl 4-chloro-3-hydroxybutyrate + NAD+
?
show the reaction diagram
12.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
ethyl pyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
?
show the reaction diagram
glycerol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
r
hexane-2,5-dione + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
hydroxyacetone + NADH
1,2-propanediol
show the reaction diagram
-
-
-
?
isobutanol + NAD+
?
show the reaction diagram
0.4% activity compared to (R,R)-butane-2,3-diol
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
show the reaction diagram
meso-butane-2,3-diol + NAD+
(3S)-acetoin + NADH + H+
show the reaction diagram
meso-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
-
-
-
-
?
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
show the reaction diagram
methyl glyoxal + NADH
?
show the reaction diagram
-
-
-
-
?
methyl pyruvate + NADH
?
show the reaction diagram
-
-
-
-
?
n-butylaldehyde + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
pentane-1,2-diol + NAD+
?
show the reaction diagram
-
very low activity
-
-
?
pentane-2,3-dione + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
pentane-2,4-dione + NADH + H+
?
show the reaction diagram
-
low activity
-
-
?
propane-1,2-diol + NAD+
?
show the reaction diagram
propane-1,3-diol + NAD+
?
show the reaction diagram
1.4% activity compared to (R,R)-butane-2,3-diol
-
-
?
pyruvic aldehyde + NADH
?
show the reaction diagram
-
81% of the activity with acetoin
-
-
?
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
sodium lactate + NAD+
?
show the reaction diagram
10.2% activity compared to (2R,3R)-butane-2,3-diol
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R,3R)-butane-2,3-diol + NAD+
(3R)-acetoin + NADH + H+
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
show the reaction diagram
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
show the reaction diagram
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
show the reaction diagram
(R)-acetoin + NADH + H+
(R,R)-butane-2,3-diol + NAD+
show the reaction diagram
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
dicaetyl + NADH + H+
(3S)-acetoin + NAD+
show the reaction diagram
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
14% of the activity with NAD+
NADPH
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
up to 1.5fold increase of activity at 1 mM
K+
138.9% activity at 1 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylpyrazole
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
acetone
38.3% residual activity at 10% (v/v)
acetonitrile
2.4% residual activity at 10% (v/v)
Ag+
complete inhibition at 1 mM
Al3+
21.6% residual activity at 1 mM
Ba2+
85.8% residual activity at 1 mM
Borate buffer
-
-
-
Ca2+
89.3% residual activity at 1 mM
Co2+
79.5% residual activity at 1 mM
dipicolinate
-
-
DMSO
8.4% residual activity at 40% (v/v)
ethanol
3.7% residual activity at 10% (v/v)
Fe2+
complete inhibition at 1 mM
Fe3+
-
slight inhibition at 1 mM
methanol
14% residual activity at 10% (v/v)
Mn2+
81.1% residual activity at 1 mM
Na+
-
slight inhibition at 1 mM
NADH
-
NADH availability limits the 2,3-butanediol dehydrogenase reaction
o-phenanthroline
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DMSO
the addition of 10% (v/v) dimethyl sulfoxide increases the activity by 161.2%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14 - 65
(2R,3R)-2,3-butanediol
0.58 - 236.4
(2R,3R)-butane-2,3-diol
0.23
(2S)-acetoin
-
at pH 10.5 and 30°C
-
0.052
(2S,3S)-butane-2,3-diol
-
at pH 10.5 and 30°C
0.06 - 4.5
(3R,3S)-acetoin
4.15 - 12.06
(3R,3S)-butane-2,3-diol
-
0.12 - 230
(R)-acetoin
2.01 - 6.01
(R,R)-butane-2,3-diol
38
1,2-propanediol
-
-
14.5
1-hydroxy-2-propanone
-
-
2.6 - 86.8
2,3-Butanediol
6
2,3-pentanediol
-
-
0.8 - 3.6
2-butanone
5.5
acetaldehyde
-
pH 7.5, 25°C
0.4 - 71
acetoin
0.6 - 2
acetone
1.2
Butanone
-
pH 7.5, 25°C
3.3
D-(-)2,3-butanediol
-
-
0.1 - 87
diacetyl
20
ethyl pyruvate
-
-
14.49 - 93.62
glycerol
6.25
meso-2,3-butanediol
-
-
2.73 - 37.39
meso-butane-2,3-diol
75
methyl glyoxal
-
-
18
Methyl pyruvate
-
-
0.16 - 2.3
NAD+
0.045 - 0.7
NADH
0.0017 - 0.087
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
(2R,3R)-2,3-butanediol
Clostridium autoethanogenum
-
pH 7.5, 25°C
3.82 - 5.8
(2R,3R)-butane-2,3-diol
3.68 - 10.38
(3R,3S)-butane-2,3-diol
-
41 - 230
(R)-acetoin
2 - 50
2-butanone
93
acetaldehyde
Clostridium autoethanogenum
-
pH 7.5, 25°C
145
acetoin
Clostridium autoethanogenum
-
pH 7.5, 25°C
3 - 89
acetone
44
Butanone
Clostridium autoethanogenum
-
pH 7.5, 25°C
6.11
diacetyl
Rhodococcus erythropolis
A0A0E4A9D6
at pH 10.0 and 45°C
10.51 - 18.88
glycerol
4.67 - 15.33
meso-butane-2,3-diol
10.27
NAD+
Rhodococcus erythropolis
A0A0E4A9D6
with (2R,3R)-butane-2,3-diol as cosubstrate, at pH 6.5 and 55°C
5.73
NADH
Rhodococcus erythropolis
A0A0E4A9D6
with diacetyl as cosubstrate, at pH 10.0 and 45°C
32 - 68
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
(2R,3R)-2,3-butanediol
Clostridium autoethanogenum
-
pH 7.5, 25°C
16548
0.03 - 7.379
(2R,3R)-butane-2,3-diol
14490
221.2
(2S)-acetoin
Corynebacterium glutamicum
-
at pH 10.5 and 30°C
213971
187.5
(2S,3S)-butane-2,3-diol
Corynebacterium glutamicum
-
at pH 10.5 and 30°C
81773
0.31 - 2.51
(3R,3S)-butane-2,3-diol
213970
0.35 - 2.8
(R)-acetoin
4876
0.9
(R,R)-butane-2,3-diol
Corynebacterium glutamicum
-
at pH 10.5 and 30°C
44987
7.8 - 61
2-butanone
1171
17
acetaldehyde
Clostridium autoethanogenum
-
pH 7.5, 25°C
90
2
acetoin
Clostridium autoethanogenum
-
pH 7.5, 25°C
1274
24 - 86
acetone
333
38
Butanone
Clostridium autoethanogenum
-
pH 7.5, 25°C
3620
61.1
diacetyl
Rhodococcus erythropolis
A0A0E4A9D6
at pH 10.0 and 45°C
746
0.11 - 1.3
glycerol
135
0.13 - 3.11
meso-butane-2,3-diol
42410
9.875
NAD+
Rhodococcus erythropolis
A0A0E4A9D6
with (2R,3R)-butane-2,3-diol as cosubstrate, at pH 6.5 and 55°C
7
71.63
NADH
Rhodococcus erythropolis
A0A0E4A9D6
with diacetyl as cosubstrate, at pH 10.0 and 45°C
8
890 - 39000
NADPH
5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
with (2S,3s)-butane-2,3-diol as substrate, at pH 7.4 and 30°C
0.005
-
with pentane-1,2-diol as substrate, at pH 7.4 and 30°C
0.007
-
with butanone as substrate, at pH 7.4 and 30°C
0.01
-
with pentane-2,3-dione as substrate, at pH 7.4 and 30°C
0.012
-
with hexane-2,5-dione as substrate, at pH 7.4 and 30°C
0.019
-
with pentane-2,4-dione as substrate, at pH 7.4 and 30°C
0.044
-
with n-butyöaödehyde as substrate, at pH 7.4 and 30°C
0.048
-
with butane-1,2-diol as substrate, at pH 7.4 and 30°C
0.084
-
with diacetyl as substrate, at pH 7.4 and 30°C
0.093
-
with propane-1,2-diol as substrate, at pH 7.4 and 30°C
0.1
wild type enzyme, using 1 mM NADPH as cosubstrate
0.257
-
with 1-hydroxy-2-butanone as substrate, at pH 7.4 and 30°C
0.732
-
with 1,3-dihydroxyacetone as substrate, at pH 7.4 and 30°C
1.056
-
with (2R,3R)-butane-2,3-diol as substrate, at pH 7.4 and 30°C
1.193
-
with (R)-acetoin as substrate, at pH 7.4 and 30°C
4.1
mutant enzyme E221S, using 1 mM NADH as cosubstrate
4.65
-
purified native enzyme, pH 7.0, 30°C
4.8
mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate
5.1
-
acetoin, enzyme 1
6.1
mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate
7.55
-
acetoin, enzyme 2
13.7
mutant enzyme E221S, using 1 mM NADPH as cosubstrate
35.55
-
diacetyl, enzyme 2
35.6
-
diacetyl, enzyme 1
54.7
mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate
92
wild type enzyme, using 1 mM NADH as cosubstrate
93.2
mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
for reduction reaction
5.8
-
substrate reduction, enzyme 1
6.5
for acetoin reduction
6.7
-
substrate reduction
7
-
acetoin reduction
7.2
-
substrate oxidation
7.5
assay at, oxidation reaction
8.5
-
substrate oxidation, enzyme 2
8.8
-
oxidation of secondary alcohols
11
oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
for the reduction of acetoin, more than 85% of its maximal activity is in the pH range of 6.5 to 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
45
for (2R,3R)-butane-2,3-diol oxidation
55
for acetoin reduction
60 - 62
100
-
catalytic activity increases up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
2 * 28000, SDS-PAGE
30000
-
gel filtration
32000
-
1 * 32000, SDS-PAGE
35000
-
4 * 35000, SDS-PAGE
41000
-
2 * 41000, SDS-PAGE
44500
-
2 * 44500, SDS-PAGE
61000
-
gel filtration
81800
-
gel filtration
90000
-
gel filtration
100000 - 107000
-
gel filtration
140000
-
gel filtration
170000
-
enzyme 1 and 2, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
-
4 * 35000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 8% (v/v) Tacsimate pH 4.6, 18% (w/v) polyethylene glycol 3350
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
stable, rapid denaturation below pH 5.0
721872
7 - 7.6
-
-
246407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
the enzyme becomes very unstable when the temperature is above 35°C with no activity at 40°C
45
after 6 h incubation at 45°C, the remaining activities for acetoin reduction and butane-2,3-diol oxidation are 49.7% and 43.5%, respectively
50
rapid denaturation of the purified enzyme above 50°C
100
-
half-life: 130 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at -18°C
-
very sensitive to storage, even at -20°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-butanediol dehydrogenase 1 and 2; partially
-
DEAE-Sepharose column chromatography and Phenyl-Sepharose column chromatography
His-Trap column chromatography
HisTrap column chromatography
HisTrap column chromatography and Sephadex G-25 gel filtration
-
native enzyme 35fold to homogeneity by fractional ammonium sulfate precipitation, followed by two different steps of anion exchange chromatography
-
native enzyme by anion exchange and hydrophobic interaction chromatography, followed by ultrafiltration and native PAGE
Ni-affinity column chromatography, and gel filtration
-
Ni-NTA column chromatography
Ni2+-chelating affinity column chromatography and Superdex 200 gel filtration
-
recombinant
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, subcloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21 (DE3)
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Serratia marcescens MG1 slaC mutant strain
-
expression in Escherichia coli
gene mbd1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
open reading frame (ORF) scaffold99_orf00067, DNA and amino acid sequence determination and analysis, phylogenetic analysis
overexpression in Saccharomyces cerevisiae
-
phylogenetic analysis
subcloning of mutant proteins via plasmids in Bacillus subtilis strain WN1038
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced upon glucose depletion
-
the enzyme gene dhaD is highly induced by glycerol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G198D/S199 V/P201E/Y218A
-
mutant displays no detectable activity with NADPH as cofactor, but uses NADH with kcat/Km value of 12 per s and mM
S199A
-
increase in catalytic efficiencies
S199C
-
decrease in catalytic efficiencies, with no significant changes in substrate preference
S199G
-
decrease in catalytic efficiencies, with no significant changes in substrate preference
S199R
-
increase in catalytic efficiencies
S199W
-
decrease in catalytic efficiencies, with no significant changes in substrate preference
E221S the
mutation produces a 170fold decrease in the Vm/Km with NADH because of a simultaneous 16fold increase in the Km value and an 11fold decrease in the Vm value, the mutation provides a positive effect on NADPH coenzyme specificity
E221S/I222R
mutant with preference for NADPH as coenzyme
E221S/I222R/A223S
mutant with preference for NADPH as coenzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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