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Information on EC 1.1.1.4 - (R,R)-butanediol dehydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39714
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1.1.1.4 (R,R)-butanediol dehydrogenaseIUBMB Comments
Also converts diacetyl into acetoin with NADH as reductant.
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Word Map
- 1.1.1.4
-
2r,3r-2,3-butanediol
- acetolactate
-
r-acetoin
- alpha-acetolactate
-
meso-2,3-bd
- polymyxa
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acetoin reductase, 2,3-butanediol dehydrogenase, butanediol dehydrogenase, (2r,3r)-2,3-butanediol dehydrogenase, meso-2,3-butanediol dehydrogenase, meso-bdh, bdh1p, ar/bdh, bdh99::67, (r,r)-butane-2,3-diol dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-diacetyl reductase
-
-
-
-
1-amino-2-propanol dehydrogenase
-
-
-
-
1-amino-2-propanol oxidoreductase
-
-
-
-
2,3-butanediol dehydrogenase
-
-
-
-
aminopropanol oxidoreductase
-
-
-
-
BDH1
butylene glycol dehydrogenase
-
-
-
-
butyleneglycol dehydrogenase
-
-
-
-
D-(-)-butanediol dehydrogenase
-
-
-
-
D-1-amino-2-propanol dehydrogenase
-
-
-
-
D-1-amino-2-propanol:NAD+ oxidoreductase
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-
-
-
D-aminopropanol dehydrogenase
-
-
-
-
dehydrogenase, D-aminopropanol
-
-
-
-
dehydrogenase, D-butanediol
-
-
-
-
diacetyl reductase (acetoin)
-
-
-
-
BDH1
-
essentially responsible for the formation of (2R,3R)-butane-2,3-diol and part of meso-butane-2,3-diol from (3R)-acetoin and (3S)-acetoin, respectively
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
37250-09-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + 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+
(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
acetaldehyde + NADH + H+
ethanol + NAD+
-
-
-
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
-
-
?
furfural + NADH + H+
(furan-2-yl)methanol + NAD+
-
-
-
?
furfural + NADPH + H+
(furan-2-yl)methanol + NADP+
-
-
-
?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
-
-
(3S)-acetoin
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+
-
-
-
r
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-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
-
-
-
-
?
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
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racemate
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r
additional information
?
-
-
3S)-2,3-butanediol, (3R/3S)-acetoin, glycerol, sorbitol or xylitol are no substrates
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-
?
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
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
the enzyme has a catalytic zinc binding domain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
NADH availability limits the 2,3-butanediol dehydrogenase reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
0.67
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
4.49
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
20.18
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
9.38
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
15.52
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
17.91
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
29.42
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.38
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
10.03
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
56.57
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
96.62
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
7.39
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
9.43
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
37.32
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
53.46
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.79
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
12.6
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
14
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
15.43
acetaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
0.32
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
0.41
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B
2.41
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
5.7
glycolaldehyde
recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate
54.7
mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate
6.1
mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate
93.2
mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate
0.24
purified recombinant enzyme, pH 7.0, 30°C, substrates glycolaldehyde and NADPH
0.48
purified recombinant enzyme, pH 7.0, 30°C, substrates formaldehyde and NADPH
0.76
purified recombinant enzyme, pH 7.0, 30°C, substrates formaldehyde and NADPH
0.82
purified recombinant enzyme, pH 7.0, 30°C, substrates furfural and NADPH
1.16
purified recombinant enzyme, pH 7.0, 30°C, substrates hexaldehyde and NADH
1.3
purified recombinant enzyme, pH 7.0, 30°C, substrates formaldehyde and NADH
1.71
purified recombinant enzyme, pH 7.0, 30°C, substrates formaldehyde and NADH
1.94
purified recombinant enzyme, pH 7.0, 30°C, substrates propionaldehyde and NADH
10.2
purified recombinant enzyme, pH 7.0, 30°C, substrates glycolaldehyde and NADH
117.95
purified recombinant enzyme, pH 7.0, 30°C, substrates acetaldehyde and NADH
2.47
purified recombinant enzyme, pH 7.0, 30°C, substrates hexaldehyde and NADH
2.72
purified recombinant enzyme, pH 7.0, 30°C, substrates acetaldehyde and NADPH
2.74
purified recombinant enzyme, pH 7.0, 30°C, substrates furfural and NADH
3.44
purified recombinant enzyme, pH 7.0, 30°C, substrates acetaldehyde and NADPH
4.95
purified recombinant enzyme, pH 7.0, 30°C, substrates furfural and NADH
6.27
purified recombinant enzyme, pH 7.0, 30°C, substrates glycolaldehyde and NADH
78.58
purified recombinant enzyme, pH 7.0, 30°C, substrates acetaldehyde and NADH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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/A223S
mutant with preference for NADPH as coenzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
activities of Bdh1p(Y) and Bdh1p(B) in glucoladehyde reduction gradually drop to approximately 50% at pH 4.5-7.0 after 6 h incubation. Especially, Bdh1p(Y) still retains 80% of its activity at pH 4.5 after incubation for 3 h. At alkaline conditions (pH 8.0-9.0), activities of the two enzymes drop rapidly to 28-45% within the first 3 h, and 3 more hours later, the lowest activity of Bdh1p(Y) is 17% at pH 9.0
760423
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BDH1, cloning from Saccharomyces cerevisiae strains YBA_08 (denoted Y) and BY4742 (denoted B), DNA and amino acid sequence determination and analysis and phylogenetic tree analysis, subcloning in to Escherichia coli strain DH5alpha and functional overexpression in Saccharomyces cerevisiae strain INVSc1, recombinant expression of His-tagged enzymes originnating from both strains
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gonzalez, E.; Fernandez, M.R.; Larroy, C.; Pares, X.; Biosca, J.A.
Characterization and functional role of Saccharomyces cerevisiae 2,3-butanediol dehydrogenase
Chem. Biol. Interact.
130
425-434
2001
Saccharomyces cerevisiae
Heidlas, J.; Tressl, R.
Purification and characterization of a (R)-2,3-butanediol dehydrogenase from Saccharomyces cerevisiae
Arch. Microbiol.
154
267-273
1990
Saccharomyces cerevisiae
Gonzalez, E.; Fernandez, M.R.; Larroy, C.; Sola, L.; Pericas, M.A.; Pares, X.; Biosca, J.A.
Characterization of a (2R,3R)-2,3-butaendiol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product
J. Biol. Chem.
275
35876-35885
2000
Saccharomyces cerevisiae
Ehsani, M.; Fernandez, M.R.; Biosca, J.A.; Julien, A.; Dequin, S.
Engineering of 2,3-butanediol dehydrogenase to reduce acetoin formation by glycerol-overproducing, low-alcohol Saccharomyces cerevisiae
Appl. Environ. Microbiol.
75
3196-3205
2009
Saccharomyces cerevisiae
Ehsani, M.; Fernandez, M.R.; Biosca, J.A.; Dequin, S.
Reversal of coenzyme specificity of 2,3-butanediol dehydrogenase from Saccharomyces cerevisae and in vivo functional analysis
Biotechnol. Bioeng.
104
381-389
2009
Saccharomyces cerevisiae (P39714), Saccharomyces cerevisiae
Gonzalez, E.; Fernandez, M.R.; Marco, D.; Calam, E.; Sumoy, L.; Pares, X.; Dequin, S.; Biosca, J.A.
Role of Saccharomyces cerevisiae oxidoreductases Bdh1p and Ara1p in the metabolism of acetoin and 2,3-butanediol
Appl. Environ. Microbiol.
76
670-679
2010
Saccharomyces cerevisiae
Bae, S.J.; Kim, S.; Hahn, J.S.
Efficient production of acetoin in Saccharomyces cerevisiae by disruption of 2,3-butanediol dehydrogenase and expression of NADH oxidase
Sci. Rep.
6
27667
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Kuang, X.; Ouyang, Y.; Guo, Y.; Li, Q.; Wang, H.; Abrha, G.T.; Ayepa, E.; Gu, Y.; Li, X.; Chen, Q.; Ma, M.
New insights into two yeast BDHs from the PDH subfamily as aldehyde reductases in context of detoxification of lignocellulosic aldehyde inhibitors
Appl. Microbiol. Biotechnol.
104
6679-6692
2020
Saccharomyces cerevisiae (A0A7G4NVP1), Saccharomyces cerevisiae (A0A7G4NVP2), Saccharomyces cerevisiae, Saccharomyces cerevisiae YBA_08 (A0A7G4NVP1), Saccharomyces cerevisiae YBA_08 (A0A7G4NVP2)
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