Information on EC 1.1.1.B20 - meso-2,3-butandiol dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.B20
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
meso-2,3-butandiol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R,3S)-butane-2,3-diol + NAD+ = acetoin + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-butane-2,3-diol:NAD+ oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
gene budC
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Manually annotated by BRENDA team
gene budC
UniProt
Manually annotated by BRENDA team
gene budC
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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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
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH
show the reaction diagram
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(2S,3S)-2,3-butanediol is a poor substrate
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-
?
(2S,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
show the reaction diagram
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
show the reaction diagram
(3S)-acetoin + NADH + H+
(2S,3S)-2,3-butanediol + NAD+
show the reaction diagram
1,2-pentanediol + NADH + H+
?
show the reaction diagram
1,2-propandiol + NADH + H+
?
show the reaction diagram
low activity
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-
?
2 (R,S)-acetoin + 2 NADPH + 2 H+
(2S,3S)-2,3-butanediol + meso-2,3-butanediol + NADP+
show the reaction diagram
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Ara1p is selective toward the acetoin carbonyl group, leading to an S-alcohol
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r
4-methyl-2-pentanone + NADH + H+
4-methyl-2-pentanol + NAD+
show the reaction diagram
diacetyl + NADH + H+
(3S)-acetoin + NAD+
show the reaction diagram
-
-
-
?
glycerol + NADH + H+
?
show the reaction diagram
low activity
-
-
?
L-acetoin + NADH
L-2,3-butanediol + NAD+
show the reaction diagram
-
-
-
?
meso-2,3-butanediol + NAD+
(3R)-acetoin + NADH + H+
show the reaction diagram
-
-
-
r
meso-2,3-butanediol + NAD+
acetoin + NADH
show the reaction diagram
-
-
-
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?
meso-2,3-butanediol + NAD+
acetoin + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
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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
(3R)-acetoin + NADH + H+
meso-2,3-butanediol + NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
enhances for oxidation and reduction reactions
Mg2+
enhances diacetyl and (3S/3R)-acetoin reduction
Mn2+
enhances diacetyl and (3S/3R)-acetoin reduction
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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competitive
Fe3+
inhibits diacetyl and (3S/3R)-acetoin reduction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31.2
(2S,3S)-2,3-butanediol
pH 5.0, 40°C
0.65 - 0.97
(3R)-acetoin
6
4-methyl-2-pentanone
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pH 8.0-9.0, 35°C, recombinant enzyme
3.3
diacetyl
pH 8.0, 40°C
2 - 13
meso-2,3-butanediol
0.66
NAD+
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pH 8.0-9.0, 35°C, recombinant enzyme
0.05
NADH
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pH 8.0-9.0, 35°C, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02
(2S,3S)-2,3-butanediol
Serratia marcescens
H9XP47
pH 5.0, 40°C
19.7
(3R)-acetoin
Serratia marcescens
H9XP47
pH 8.0, 40°C
11.5
diacetyl
Serratia marcescens
H9XP47
pH 8.0, 40°C
6.2
meso-2,3-butanediol
Serratia marcescens
H9XP47
pH 5.0, 40°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
2-mercaptoethanol
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pH 8.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1
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mutant N146F, substrate (2S,3S)-2,3-butanediol, pH 8.0, 37°C
2.9
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mutant Q140I/N146F/W190H, substrate (2S,3S)-2,3-butanediol, pH 8.0, 37°C
3.1
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mutant Q140I/N146F, substrate (2,3S)-2,3-butanediol, pH 8.0, 37°C
4.5
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mutant Q140I/N146F, substrate meso-2,3-butanediol, pH 8.0, 37°C
5.5
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wild-type, substrate (2S,3S)-2,3-butanediol, pH 8.0, 37°C
19.4
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mutant N146F, substrate meso-2,3-butanediol, pH 8.0, 37°C
21
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purified reconstituted, recombinant enzyme, reduction of 4-methyl-2-pentanone, pH 8.0, 35°C
66
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purified reconstituted, recombinant enzyme, oxidation of meso-2,3-butanediol, pH 8.0, 35°C
177
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wild-type, substrate meso-2,3-butanediol, pH 8.0, 37°C
218
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purified reconstituted, recombinant enzyme, reduction of acetoin, pH 8.0, 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
maximal activity of (3S/3R)-acetoin reduction
8
maximal activity of diacetyl reduction and meso-2,3-butanediol oxidation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
optimum for oxidation and reduction reactions
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with substrate meso-2,3-butanediol and inhibitor 2-mercaptoethanol, to 1.7 A resolution. The overall strucuture is similar to that of other short chain dehydrogenase/reductase enzymes, the NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. 2-Mercaptoethanol forms hydrogens bonds with residues Gln 140 and Gly 183 close to the active site, which are important but not sufficient for distiguishing stereoisomerism of a chiral substrate
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene bdh1, phylogenetic analysis, expression in Escherichia coi strain YYC202(DE3) ldhA-/- ilvC? expressing ilvBN from Escherichia coli and aldB from Lactobacillus lactis, encoding acetolactate synthase and acetolactate decarboxylase activities, respectively, disruption of the lactate biosynthesis pathway in the strain increases pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-butanediol is the most important consequence of ldhA deletion
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gene budC, expression in Escherichia coli strain BL21(DE3) pLys
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gene budC, sequence comparisons, expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
phylogenetic analysis, enzyme expression in Escherichia coli strains MG1655(DE3) and YYC202(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N146F
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11% of wild-type specific activity
Q140I
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trace activity below 0.1 U/mg
Q140I/N146F
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poor activity
Q140I/N146F/W190H
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trace activity below 0.1 U/mg with substrate meso-butanediol, 2.9 U/mg with substrate (2S,3S)-2,3-butanediol
Q140I
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mutation mimicking the corresponding residue in (S,S)-butanediol dehydrogenase. No activity with substrates meso-butanediol or (S,S)-butanediol
Q140I/N146F
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mutation mimicking the corresponding residues in (S,S)-butanediol dehydrogenase. Poor activity with substrates meso-butanediol or (S,S)-butanediol
additional information
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expression of gene bdh1 from Saccharomyces cervisiae in Escherichia coi strain YYC202(DE3) ldhA-/- ilvC-/- expressing ilvBN from Escherichia coli and aldB from Lactobacillus lactis, encoding acetolactate synthase and acetolactate decarboxylase activities, respectively. Disruption of the lactate biosynthesis pathway in the strain increases pyruvate precursor availability to this strain, increased availability of NADH for acetoin reduction to meso-2,3-butanediol is the most important consequence of ldhA deletion. Optimization of 2,3-butanediol production in Escherichia coli, overview