BRENDA - Enzyme Database show
show all sequences of 1.1.1.4

Novel (2R,3R)-2,3-butanediol dehydrogenase from potential industrial strain Paenibacillus polymyxa ATCC 12321

Yu, B.; Sun, J.; Bommareddy, R.R.; Song, L.; Zeng, A.P.; Appl. Environ. Microbiol. 77, 4230-4233 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
open reading frame (ORF) scaffold99_orf00067, DNA and amino acid sequence determination and analysis, phylogenetic analysis
Paenibacillus polymyxa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.046
-
NADH
pH 8.0, 22C
Paenibacillus polymyxa
0.3
-
(3R,3S)-acetoin
pH 8.0, 22C
Paenibacillus polymyxa
0.54
-
NAD+
pH 11.0, 22C
Paenibacillus polymyxa
1.76
-
(2R,3R)-butane-2,3-diol
pH 11.0, 22C
Paenibacillus polymyxa
5.62
-
meso-butane-2,3-diol
pH 11.0, 22C
Paenibacillus polymyxa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
(3R,3S)-acetoin + NADH + H+
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
(3R,3S)-acetoin + NADH + H+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paenibacillus polymyxa
E7EKB8
-
-
Paenibacillus polymyxa ATCC 12321
E7EKB8
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
721345
Paenibacillus polymyxa
(3R,3S)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
721345
Paenibacillus polymyxa
(3R,3S)-acetoin + NADH + H+
preferred substrate in the reduction reaction
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
721345
Paenibacillus polymyxa ATCC 12321
(3R,3S)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
721345
Paenibacillus polymyxa ATCC 12321
(3R,3S)-acetoin + NADH + H+
preferred substrate in the reduction reaction
-
-
r
1,2-pentandiol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
1,2-propandiol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
2-propanol + NAD+
-
721345
Paenibacillus polymyxa
2-propanone + NADH + H+
-
-
-
r
2-propanol + NAD+
-
721345
Paenibacillus polymyxa ATCC 12321
2-propanone + NADH + H+
-
-
-
r
diacetyl + NADH + H+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
721345
Paenibacillus polymyxa
acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
721345
Paenibacillus polymyxa ATCC 12321
acetoin + NAD+
-
-
-
?
glycerol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
meso-butane-2,3-diol + NAD+
72% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
721345
Paenibacillus polymyxa
acetoin + NADH + H+
-
-
-
r
additional information
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
721345
Paenibacillus polymyxa
?
-
-
-
-
additional information
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
721345
Paenibacillus polymyxa ATCC 12321
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Paenibacillus polymyxa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
reduction reaction
Paenibacillus polymyxa
11
-
oxidation reaction
Paenibacillus polymyxa
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Paenibacillus polymyxa
NADH
-
Paenibacillus polymyxa
Cloned(Commentary) (protein specific)
Commentary
Organism
open reading frame (ORF) scaffold99_orf00067, DNA and amino acid sequence determination and analysis, phylogenetic analysis
Paenibacillus polymyxa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Paenibacillus polymyxa
NADH
-
Paenibacillus polymyxa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.046
-
NADH
pH 8.0, 22C
Paenibacillus polymyxa
0.3
-
(3R,3S)-acetoin
pH 8.0, 22C
Paenibacillus polymyxa
0.54
-
NAD+
pH 11.0, 22C
Paenibacillus polymyxa
1.76
-
(2R,3R)-butane-2,3-diol
pH 11.0, 22C
Paenibacillus polymyxa
5.62
-
meso-butane-2,3-diol
pH 11.0, 22C
Paenibacillus polymyxa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
(3R,3S)-acetoin + NADH + H+
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
(3R,3S)-acetoin + NADH + H+
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
721345
Paenibacillus polymyxa
(3R,3S)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
721345
Paenibacillus polymyxa
(3R,3S)-acetoin + NADH + H+
preferred substrate in the reduction reaction
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
Paenibacillus polymyxa ATCC 12321 has the ability to form almost exclusively the R isomer of 2,3-BDL (over 98%) when grown under anaerobic conditions
721345
Paenibacillus polymyxa ATCC 12321
(3R,3S)-acetoin + NADH + H+
-
-
-
r
(2R,3R)-butane-2,3-diol + NAD+
sole product in the reduction reaction, preferred substrate in the oxidation reaction
721345
Paenibacillus polymyxa ATCC 12321
(3R,3S)-acetoin + NADH + H+
preferred substrate in the reduction reaction
-
-
r
1,2-pentandiol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
1,2-propandiol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
2-propanol + NAD+
-
721345
Paenibacillus polymyxa
2-propanone + NADH + H+
-
-
-
r
2-propanol + NAD+
-
721345
Paenibacillus polymyxa ATCC 12321
2-propanone + NADH + H+
-
-
-
r
diacetyl + NADH + H+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
721345
Paenibacillus polymyxa
acetoin + NAD+
-
-
-
?
diacetyl + NADH + H+
91% activity compared to (3R,3S)-acetoin in the reduction reaction, cf. EC 1.1.1.303
721345
Paenibacillus polymyxa ATCC 12321
acetoin + NAD+
-
-
-
?
glycerol + NAD+
-
721345
Paenibacillus polymyxa
? + NADH + H+
-
-
-
r
meso-butane-2,3-diol + NAD+
72% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
721345
Paenibacillus polymyxa
acetoin + NADH + H+
-
-
-
r
additional information
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
721345
Paenibacillus polymyxa
?
-
-
-
-
additional information
the enzyme is also active in reduction reaction with diacetyl (91% compared to (2R,3S)-acetoin) and glyceraldehyde-3-phosphate (12% compared to (2R,3S)-acetoin), cf. EC 1.1.1.303 and EC 1.1.1.8, respectively, but not with dihydroxyacetone phosphate. It shows low activity in oxidation reaction with ethanol, n-propanol, n-butanol, 1,3-propanediol, and 1,5-pentanediol
721345
Paenibacillus polymyxa ATCC 12321
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Paenibacillus polymyxa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
reduction reaction
Paenibacillus polymyxa
11
-
oxidation reaction
Paenibacillus polymyxa
General Information
General Information
Commentary
Organism
evolution
the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
Paenibacillus polymyxa
General Information (protein specific)
General Information
Commentary
Organism
evolution
the (2R,3R)-2,3-butanediol dehydrogenase belongs to the mostly zinc-containing medium-chain dehydrogenase/reductase superfamily and not to the short-chain dehydrogenase/reductase superfamily, to which meso- and (2S,3S)-2,3-butanediol dehydrogenases belong, phylogenetic analysis. The enzyme contains two hydrophobic residues forming the binding site for cofactor NAD(P), Phe138 and Leu141 (numbers refer to R,R-BDH of Saccharomyces cerevisiae)
Paenibacillus polymyxa
Other publictions for EC 1.1.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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2
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1
1
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1
-
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14
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-
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-
-
-
-
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38
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-
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-
-
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12
2
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4
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-
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2
4
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-
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8
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2
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12
2
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2
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4
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5
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1
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1
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1
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-
-
15
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3
1
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19
1
2
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4
2
1
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2
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1
-
1
2
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-
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15
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4
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3
1
3
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19
1
2
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1
4
2
1
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-
-
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4
4
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28
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-
1
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21
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3
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-
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21
-
-
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2
-
-
-
-
-
1
2
-
7
-
-
-
-
21
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
21
-
-
-
-
-
-
-
-
21
21
737501
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80
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-
-
-
-
-
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-
5
-
-
-
-
-
4
-
-
-
-
-
-
-
-
6
-
-
-
-
5
-
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2
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2
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-
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5
-
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-
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-
-
-
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6
-
-
-
-
5
-
-
-
-
-
-
-
-
5
5
738472
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Utilization of excess NADH in ...
Bacillus licheniformis
J. Appl. Microbiol.
117
690-698
2014
-
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1
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2
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1
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2
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2
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1
2
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2
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2
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-
-
-
-
738637
Wang
Glycerol dehydrogenase plays a ...
Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 25955
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Crow
Properties of 2,3-butanediol d ...
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Bacterial 2,3-butanediol dehyd ...
Aeromonas hydrophila, Bacillus subtilis, Gluconobacter oxydans, Paenibacillus polymyxa
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