Information on EC 1.1.1.76 - (S,S)-butanediol dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.76
-
RECOMMENDED NAME
GeneOntology No.
(S,S)-butanediol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S,3S)-butane-2,3-diol + NAD+ = (S)-acetoin + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S,S)-butanediol biosynthesis
-
-
(S,S)-butanediol degradation
-
-
Butanoate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
(S,S)-butane-2,3-diol:NAD+ oxidoreductase
This enzyme catalyses the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol. It can also catalyse the irreversible reduction of diacetyl to (S)-acetoin.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-14-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 11439
-
-
Manually annotated by BRENDA team
Ford strain
-
-
Manually annotated by BRENDA team
Ford strain
-
-
Manually annotated by BRENDA team
ATCC 8724, glucose-grown cells contain L-2,3-butanediol dehydrogenase
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in Pseudomonas sp.
lacks 2,3-butanediol dehydrogenase
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas sp. s4
lacks 2,3-butanediol dehydrogenase
-
-
Manually annotated by BRENDA team
IAM 1022
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-
Manually annotated by BRENDA team
IAM 1022
-
-
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
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
show the reaction diagram
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
show the reaction diagram
-
-
-
?
(2S,3S)-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
show the reaction diagram
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
show the reaction diagram
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
show the reaction diagram
(R,R)-butane-2,3-diol + NAD+
?
show the reaction diagram
-
-
-
-
?
(R,S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NAD+
show the reaction diagram
-
-
-
r
(R,S)-acetoin + NADPH
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NADP+
show the reaction diagram
-
-
Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
-
r
(S)-1-phenylethanol + NAD+
acetophenone + NADH + H+
show the reaction diagram
-
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
show the reaction diagram
1,2-propanediol + NAD+
?
show the reaction diagram
-
0.57% activity compared to (2S,3S)-butane-2,3-diol
-
-
?
1,2-propanediol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
show the reaction diagram
1-butanol + NAD+
butanal + NADH + H+
show the reaction diagram
1-phenylpropanol + NAD+
1-phenylpropanal + NADH + H+
show the reaction diagram
-
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
2,3-hexanedione + NADH + H+
?
show the reaction diagram
-
66% activity compared to diacetyl
-
-
?
2,3-pentanedione + NADH + H+
?
show the reaction diagram
2-butanol + NAD+
2-butanone + NADH + H+
show the reaction diagram
2-pentanol + NAD+
2-pentanone + NADH + H+
show the reaction diagram
3,4-hexanedione + NADH + H+
?
show the reaction diagram
-
10% activity compared to diacetyl
-
-
?
cyclohexanol + NAD+
cyclohexanone + NADH + H+
show the reaction diagram
diacetyl + NADH
L-acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
(2S)-acetoin + NAD+
show the reaction diagram
diacetyl + NADH + H+
?
show the reaction diagram
-
35% activity in comparison to L-acetoin
-
-
r
ethyl pyruvate + NADH + H+
? + NAD+
show the reaction diagram
-
-
-
?
glyceraldehyde + NADH + H+
?
show the reaction diagram
isopropanol + NAD+
isopropanal + NADH + H+
show the reaction diagram
-
-
-
?
L-acetoin + NADH
L-2,3-butanediol
show the reaction diagram
L-acetoin + NADH + H+
(S,S)-butane-2,3-diol + NAD+
show the reaction diagram
-
100% activity
-
-
r
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
show the reaction diagram
meso-2,3-butanediol + NAD+
(R,S)-acetoin + NADH + H+
show the reaction diagram
-
selective catalysis of S,S- and meso-butanediol, but not R,R-butanediol
-
r
meso-2,3-butanediol + NAD+
acetoin + NADH
show the reaction diagram
poor substrate
-
-
?
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
(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+
(S)-acetoin + NADH + H+
show the reaction diagram
M4N626
the enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. Physiological role in favor of (2S,3S)-2,3-butanediol formation
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Ca2+
-
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
Fe2+
-
increased acetoin production
Mg2+
-
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
acetate
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slight inhibition at 5 mM
Ag+
-
strong inhibition
Al3+
-
strong inhibition
Fe3+
-
strong inhibition
formate
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slight inhibition at 5 mM
Hg2+
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100% inhibition at 5 mM; 5 mM, 100% inhibition
K+
-
slight inhibition
Lactate
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slight inhibition at 5 mM
pyruvate
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slight inhibition at 5 mM
succinate
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slight inhibition at 5 mM
Zn2+
-
slight inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
Ba2+, Ca2+, Mn2+, Mg2+ and Co2+ activate enzyme 1.6-1.8 fold at a concentration of 5 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.47
(2S)-acetoin
-
at pH 10.0 and 30C
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7.25
(R,R)-butane-2,3-diol
-
at pH 10.0 and 30C
42.2
(R,S)-acetoin
pH 7.0, 30C
-
0.22
(S,S)-butane-2,3-diol
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pH 6.0
72.4
diacetyl
-
at pH 5.0 and 30C
0.44
L-acetoin
-
pH 6.0
0.22
L-butanediol
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pH 10.5
-
0.07
NAD+
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pH 10.5; pH 6.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
202
(2S)-acetoin
Bacillus licheniformis
-
at pH 10.0 and 30C
-
591
(R,R)-butane-2,3-diol
Bacillus licheniformis
-
at pH 10.0 and 30C
6
(R,S)-acetoin
Mycobacterium sp.
W8VSK8
pH 7.0, 30C
-
1222
diacetyl
Bacillus licheniformis
-
at pH 5.0 and 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
432
(2S)-acetoin
Bacillus licheniformis
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at pH 10.0 and 30C
213971
81.5
(R,R)-butane-2,3-diol
Bacillus licheniformis
-
at pH 10.0 and 30C
44987
0.1
(R,S)-acetoin
Mycobacterium sp.
W8VSK8
pH 7.0, 30C
84132
16.9
diacetyl
Bacillus licheniformis
-
at pH 5.0 and 30C
746
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.28 - 4.3
2-mercaptoethanol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
substrate meso-2,3-butanediol, pH 8.0, 37C
0.44
-
3% 2,3-butanediol as carbon source
0.79
-
1% glucose as carbon source
1.51
-
plasmid containing L-butanediol dehydrogenase gene
4.3
substrate (2S,3S)-2,3-butanediol, pH 8.0, 37C
17
-
plasmid containing tac promoter and L-butanediol dehydrogenase ORF
18.6
-
plasmid containing meso-butanediol dehydrogenase promoter region and L-butanediol dehydrogenase ORF
39
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at pH 7.4 and 30C
269
purified recombinant enzyme, (2S,3S)-2,3-butanediol oxidation, pH 9.5, 25C
8519
purified recombinant enzyme, diacetyl reduction, pH 7.0, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
for diacetyl reduction
6
-
reduction of L-acetoin
6.2
-
assay at, reduction of acetoin
7
diacetyl reduction
8
-
assay at, oxidation of 2,3-butanediol
9.5
(2S,3S)-2,3-butanediol oxidation
10
-
for 2,3-butanediol oxidation
10.5
-
oxidation of L-butanediol; oxidation of (S,S)-butane-2,3-diol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
the enzyme shows a relatively high activity over a wide pH range from 5.0 to 8.0 for racemic acetoin reduction and more than 60% of activity is retained between pH 4.5 and 10.0
6.1 - 11
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
activity range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
isoelectric focusing
4.9
-
isoelectric focussing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26864
2 * 26864, sequence calculation
27107
-
4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
30000
-
4 * 30000, SDS-PAGE; 4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
103000
-
gel filtration
110000
-
gel filtration
125000
-
gel filtration
150000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 26800, SDS-PAGE
homodimer
homotetramer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method with polyethylene glycol 4000 as precipitant; X-ray analysis
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hanging drop vapor diffusion method, using 17% (w/v) PEG 4000, 15% (v/v) glycerol and 1% (v/v) beta-mercaptoethanol in 100 mM MES buffer pH 6.4
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in complex with NAD+ and 2-mercaptoethanol, to 2.0 A resolution. The L-BDH subunit is composed of seven beta-strands, six alpha-helices and two short a helices, aFG1 and aFG2, which form a small lobe on top of the core domain. The conserved active site residues Asn112, Ser141, Tyr154 and Lys158 are located near the NAD+ molecule
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
; stable
389580
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
-
The enzyme is stable up to 37C but rapidly inactivated over 40C
37
-
up to, rapidly inactivated over 40C, 30 min incubation before the enzyme assay
50
-
at 50C, the enzymatic activity drops rapidly to half of its initial activity within 40 min, then further decreases to 20% after 330 min
additional information
-
thermolabile
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to repeated freezing and thawing during storage
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-17C, pH 8.0, stable
-
-20C, 4 months, activity preserved
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
-
HiTrap Q column chromatography and Superdex 200 gel filtration
-
protamine sufate precipitation
-
recombinant enzyme; streptomycin sulfate precipitation, affinity chromatography, gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-expressed with glucose dehydrogenase and formate dehydrogenase in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli JM109, stereospecifity of resulting L-butanediol dehydrogenase is reduced. Expressed gene contains tac-promoter and upstream region of the meso-butanediol dehydrogenase gene of Klebsiella pneumoniae IAM1063. A more stable stereospecifity is exhibited; When the enzyme gene is only expressed in Escherichia coli using the tac promoter, the stereospecificity of resulting enzyme gene is reduced. When the region upstream of the meso-butanediol dehydrogenase gene of Klebsiella pneumoniae is also involved in the expression of gene, the resulting enzyme exhibits more stable stereospecificity.
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expression in Escherichia coli JM109/pLBD2-CTC; L-butanediol gene containing plasmid pLBD2-CTC is expressed in Escherichia coli JM109
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F148N
trace activity below 0.1 U/mg
I142Q
trace activity below 0.1 U/mg
I142Q/F148N
trace activity below 0.1 U/mg
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis