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Information on EC 1.1.1.76 - (S,S)-butanediol dehydrogenase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q9ZNN8

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IUBMB Comments
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.
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This record set is specific for:
Corynebacterium glutamicum
UNIPROT: Q9ZNN8
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The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
l-bdh, 2,3-bdh, (s,s)-butanediol dehydrogenase, acetoin(diacetyl) reductase, s-2,3-butanediol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(2S, 3S)-butanediol dehydrogenase
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(S,S)-2,3-butanediol dehydrogenase
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(S,S)-butanediol dehydrogenase
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L(+)-2,3-butanediol dehydrogenase (L-acetoin forming)
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-
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L-(2S,3S)-butanediol dehydrogenase
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L-BDH
L-butanediol dehydrogenase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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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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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 + H+
show the reaction diagram
-
-
-
?
meso-2,3-butanediol + NAD+
acetoin + NADH
show the reaction diagram
poor substrate
-
-
?
(2S)-acetoin + NADH + H+
(2S,3S)-butane-2,3-diol + NAD+
show the reaction diagram
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
show the reaction diagram
-
-
-
-
r
(S,S)-butane-2,3-diol + NAD+
L-acetoin + NADH + H+
show the reaction diagram
-
-
-
-
?
1,3-dihydroxyacetone + NADH + H+
?
show the reaction diagram
-
low activity with 30 mM
-
-
?
2,3-pentanedione + NADH + H+
?
show the reaction diagram
-
7% activity in comparison to L-acetoin
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-
r
diacetyl + NADH
L-acetoin + NAD+
show the reaction diagram
-
also reduction of 2,3-pentanedione
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?
diacetyl + NADH + H+
(2S)-acetoin + NAD+
show the reaction diagram
-
-
-
-
?
diacetyl + NADH + H+
?
show the reaction diagram
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35% activity in comparison to L-acetoin
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-
r
glyceraldehyde + NADH + H+
?
show the reaction diagram
-
low activity with 30 mM
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-
?
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
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-
r
L-acetoin + NADH + H+
(S,S)-butanediol + NAD+
show the reaction diagram
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To confirm the high production of enzyme, the conversion of L-acetoin, in a racemic mixture, to L-2,3-butanediol is studied. 0.37% L-2,3-butanediol is formed from 1% L-acetoin added to the culture.
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-
?
additional information
?
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not: meso-butanediol, D-butanediol, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, n-propanol, D-acetoin, acetol, dihydroxyacetone, 2,4-pentanedione
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-
?
NATURAL SUBSTRATE
NATURAL 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
-
-
-
-
r
(2S,3S)-butane-2,3-diol + NAD+
(2S)-acetoin + NADH + H+
show the reaction diagram
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-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
increased acetoin production
additional information
-
no significant changes in enzyme activity with 5 mM Ni2+, Zn2+ and Cd2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
competitive. In crystal structure, the mercaptoethanol molecule is located in the catalytic cleft formed by residues Ser141, Ileu142, Ala143, Phe148, Tyr154, Pro184, Gly185, Ileu186, Met191, Trp192 and Ile195. These residues may also be involved in substrate recognition and in stereospecific redox reactions
2-mercaptoethanol
acetate
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slight inhibition at 5 mM
formate
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slight inhibition at 5 mM
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
additional information
-
slight inhibition of 10-20% by organic acids at concentrations of 5 mM: lactate, pyruvate, succinate, acetate and formate
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
(S,S)-butane-2,3-diol
0.44
L-acetoin
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pH 6.0
0.07
NAD+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
2-mercaptoethanol
pH 8.0, 37°C
4.28
2-mercaptoethanol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
substrate meso-2,3-butanediol, pH 8.0, 37°C
4.3
substrate (2S,3S)-2,3-butanediol, pH 8.0, 37°C
0.44
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3% 2,3-butanediol as carbon source
0.79
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1% glucose as carbon source
1.51
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plasmid containing L-butanediol dehydrogenase gene
17
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plasmid containing tac promoter and L-butanediol dehydrogenase ORF
18.6
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plasmid containing meso-butanediol dehydrogenase promoter region and L-butanediol dehydrogenase ORF
39
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at pH 7.4 and 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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reduction of L-acetoin
6.2
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assay at, reduction of acetoin
8
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assay at, oxidation of 2,3-butanediol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
isoelectric focussing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BUDC_CORGT
258
0
27108
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
103000
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gel filtration
110000
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gel filtration
26000
-
4 * 26000, SDS-PAGE
26800
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x * 26800, SDS-PAGE
27107
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4 * 30000, SDS-PAGE, 4 * 27107, estimation from gene sequence
30000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 26800, SDS-PAGE
homotetramer
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4 * 26000, SDS-PAGE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapor diffusion method with polyethylene glycol 4000 as precipitant
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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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PROTEIN VARIANTS
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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up to, rapidly inactivated over 40°C, 30 min incubation before the enzyme assay
37 - 40
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The enzyme is stable up to 37°C but rapidly inactivated over 40°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable to repeated freezing and thawing during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-17°C, pH 8.0, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Q column chromatography and Superdex 200 gel filtration
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protamine sufate precipitation
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recombinant enzyme
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streptomycin sulfate precipitation, affinity chromatography, gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expressed with glucose dehydrogenase and formate dehydrogenase in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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expression in Escherichia coli JM109, stereospecificity 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 stereospecificity is exhibited
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expression in Escherichia coli JM109/pLBD2-CTC
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L-butanediol gene containing plasmid pLBD2-CTC is expressed in Escherichia coli JM109
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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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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preparation of chiral acetoinic compounds, enzymic identification for chiral acetoinic compounds or as model enzyme for studying the interrelation between enzymic stereospecificity and structure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ui, S.; Masuda, H.; Muraki, H.
Separation and quantitation of 2,3-butanediol isomers ((-), (+), and meso) by a combined use of enzyme and gas chromatography
Agric. Biol. Chem.
48
2837-2838
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
Manually annotated by BRENDA team
Ui, S.; Masuda, H.; Muraki, H.
Laboratory-scale production of acetoin isomers (D(-) and L(+)) by bacterial fermentation
J. Ferment. Technol.
62
151-156
1984
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012, Klebsiella pneumoniae, Klebsiella pneumoniae IAM 1063, no activity in Pseudomonas sp., no activity in Pseudomonas sp. s4, Paenibacillus polymyxa, Paenibacillus polymyxa IAM 1189, Saccharomyces cerevisiae, Saccharomyces cerevisiae OC-2, Serratia marcescens, Serratia marcescens IAM 1022
-
Manually annotated by BRENDA team
Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Stereochemical applications of the expression of the L-2,3-butanediol dehydrogenase gene in Escherichia coli
Lett. Appl. Microbiol.
32
93-98
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Manually annotated by BRENDA team
Otagiri, M.; Kurisu, G.; Ui, S.; Ohkuma, M.; Kudo, T.; Kusunoki, M.
Crystallization and preliminary x-ray studies of L-(+)-2,3-butanediol dehydrogenase from Brevibacterium saccharolyticum C-1012
Protein Pept. Lett.
8
57-61
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
-
Manually annotated by BRENDA team
Takusagawa, Y.; Otagiri, M.; Ui, S.; Ohtsuki, T.; Mimura, A.; Ohkuma, M.; Kudo, T.
Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
65
1876-1878
2001
Corynebacterium glutamicum, Corynebacterium glutamicum C-1012
Manually annotated by BRENDA team
Otagiri, M.; Ui, S.; Takusagawa, Y.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.
Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
FEBS Lett.
584
219-223
2010
Corynebacterium glutamicum (Q9ZNN8)
Manually annotated by BRENDA team
Shimegi, T.; Ooyama, T.; Ohtsuki, T.; Kurisu, G.; Kusunoki, M.; Ui, S.
Crystallization and preliminary X-ray diffraction analysis of domain-chimeric L-(2S,3S)-butanediol dehydrogenase
Acta Crystallogr. Sect. F
70
461-463
2014
Corynebacterium glutamicum
Manually annotated by BRENDA team
Jojima, T.; Igari, T.; Moteki, Y.; Suda, M.; Yukawa, H.; Inui, M.
Promiscuous activity of (S,S)-butanediol dehydrogenase is responsible for glycerol production from 1,3-dihydroxyacetone in Corynebacterium glutamicum under oxygen-deprived conditions
Appl. Microbiol. Biotechnol.
99
1427-1433
2015
Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229
Manually annotated by BRENDA team
Shimegi, T.; Mochizuki, K.; Oyama, T.; Ohtsuki, T.; Kusunoki, M.; Ui, S.
Modification of chimeric (2S, 3S)-butanediol dehydrogenase based on structural information
Protein Pept. Lett.
22
226-233
2015
Corynebacterium glutamicum
Manually annotated by BRENDA team
Wang, Y.; Li, L.; Ma, C.; Gao, C.; Tao, F.; Xu, P.
Engineering of cofactor regeneration enhances (2S,3S)-2,3-butanediol production from diacetyl
Sci. Rep.
3
2643
2013
Corynebacterium glutamicum
Manually annotated by BRENDA team