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

Word Map on EC 1.1.1.76
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(S,S)-butanediol biosynthesis
-
-
(S,S)-butanediol degradation
-
-
Butanoate metabolism
-
-
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
-
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
-
-
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
-
-
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,3S)-2,3-butanediol + NAD+
(3S)-acetoin + NADH + H+
show the reaction diagram
-
-
-
?
(2S,3S)-butane-2,3-diol + NAD+
(S)-acetoin + NADH + H+
show the reaction diagram
(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+
? + 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-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
cyclohexanol + NAD+
cyclohexanone + NADH + H+
show the reaction diagram
diacetyl + NADH
L-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
-
-
-
?
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+
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,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
Co2+
-
; 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
Mn2+
-
; Ba2+, Ca2+, Mn2+, Mg2+, and Co2+ activate the enzyme 1.6-1.8fold at a concentration of 5 mM
additional information
-
no significant changes in enzyme activity with 5 mM Ni2+, Zn2+ and Cd2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
acetate
-
slight inhibition at 5 mM
Cu2+
-
5 mM, 89% inhibition; 89% inhibition at 5 mM
formate
-
slight inhibition at 5 mM
Hg2+
-
100% inhibition at 5 mM; 5 mM, 100% inhibition
Lactate
-
slight inhibition at 5 mM
pyruvate
-
slight inhibition at 5 mM
succinate
-
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
-
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
0.22
(S,S)-butane-2,3-diol
-
pH 6.0
0.44
L-acetoin
-
pH 6.0
0.22
L-butanediol
-
pH 10.5
-
0.07
NAD+
-
pH 10.5; pH 6.0
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
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
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
10.5
-
oxidation of L-butanediol; oxidation of (S,S)-butane-2,3-diol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
4.9
-
isoelectric focussing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method with polyethylene glycol 4000 as precipitant; X-ray analysis
-
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
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
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
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
-
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)
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.
-
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