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Literature summary extracted from

  • Gong, F.; Liu, Q.; Tan, H.; Li, T.; Tan, C.; Yin, H.
    Cloning, expression and characterization of a novel (2R,3R) -2,3-butanediol dehydrogenase from Bacillus thuringiensis (2019), Biocatal. Agricult. Biotechnol., 22, 10137 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.4 additional information nonionic detergent Triton X-100 and Tween 80, as well as DMSO have no significant effect on enzyme activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 additional information nonionic detergent Triton X-100 and Tween 80, as well as DMSO have no significant effect on enzyme activity Bacillus thuringiensis serovar kurstaki

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.4 gene bdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Bacillus thuringiensis serovar kurstaki
1.1.1.B20 gene bdh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli Bacillus thuringiensis serovar kurstaki

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.4 EDTA
-
Bacillus thuringiensis serovar kurstaki
1.1.1.4 additional information nonionic detergent Triton X-100 and Tween 80, as well as DMSO have no significant effect on enzyme activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 EDTA
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 additional information nonionic detergent Triton X-100 and Tween 80, as well as DMSO have no significant effect on enzyme activity Bacillus thuringiensis serovar kurstaki

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.4 0.76
-
(2R,3R)-butane-2,3-diol pH 10.0, 50°C, recombinant enzyme Bacillus thuringiensis serovar kurstaki
1.1.1.4 3.67
-
(2R,3S)-butane-2,3-diol pH 10.0, 50°C, recombinant enzyme Bacillus thuringiensis serovar kurstaki
1.1.1.B20 0.76
-
(2R,3R)-butane-2,3-diol pH 10.0, 50°C, recombinant enzyme Bacillus thuringiensis serovar kurstaki
1.1.1.B20 3.67
-
(2R,3S)-butane-2,3-diol pH 10.0, 50°C, recombinant enzyme Bacillus thuringiensis serovar kurstaki

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.4 Zn2+ required, the enzyme has a catalytic Zn site (Cys37, His69 and Glu151) and a structural Zn site (Cys99, Cys102, Cys105 and Cys113) Bacillus thuringiensis serovar kurstaki
1.1.1.B20 Zn2+ required, the enzyme has a catalytic Zn site (Cys37, His69 and Glu151) and a structural Zn site (Cys99, Cys102, Cys105 and Cys113) Bacillus thuringiensis serovar kurstaki

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki
-
(3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki ACCC 10066
-
(3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki
-
(3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki ACCC 10066
-
(3R)-acetoin + NADH + H+
-
r
1.1.1.B20 (2R,3R)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki
-
(3R)-acetoin + NADH + H+
-
r
1.1.1.B20 (2R,3S)-butane-2,3-diol + NAD+ Bacillus thuringiensis serovar kurstaki
-
(3R)-acetoin + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.4 Bacillus thuringiensis serovar kurstaki A0A0F6FX23
-
-
1.1.1.4 Bacillus thuringiensis serovar kurstaki ACCC 10066 A0A0F6FX23
-
-
1.1.1.B20 Bacillus thuringiensis serovar kurstaki A0A0F6FX23
-
-
1.1.1.B20 Bacillus thuringiensis serovar kurstaki ACCC 10066 A0A0F6FX23
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.4 recombinant enzyme from Escherichia coli by ion exchange chromatography Bacillus thuringiensis serovar kurstaki
1.1.1.B20 recombinant enzyme from Escherichia coli by ion exchange chromatography Bacillus thuringiensis serovar kurstaki

Storage Stability

EC Number Storage Stability Organism
1.1.1.4 4°C, BtBDH shows good stability after storage for 3 months Bacillus thuringiensis serovar kurstaki
1.1.1.B20 4°C, BtBDH shows good stability after storage for 3 months Bacillus thuringiensis serovar kurstaki

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3R)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki ACCC 10066 (3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+ slightly preferred substrate Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki ACCC 10066 (3R)-acetoin + NADH + H+
-
r
1.1.1.4 (2R,3S)-butane-2,3-diol + NAD+ slightly preferred substrate Bacillus thuringiensis serovar kurstaki ACCC 10066 (3R)-acetoin + NADH + H+
-
r
1.1.1.4 additional information enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl Bacillus thuringiensis serovar kurstaki ?
-
-
1.1.1.4 additional information enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl Bacillus thuringiensis serovar kurstaki ACCC 10066 ?
-
-
1.1.1.B20 (2R,3R)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
r
1.1.1.B20 (2R,3S)-butane-2,3-diol + NAD+
-
Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
?
1.1.1.B20 (2R,3S)-butane-2,3-diol + NAD+ slightly preferred substrate Bacillus thuringiensis serovar kurstaki (3R)-acetoin + NADH + H+
-
?
1.1.1.B20 additional information enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl Bacillus thuringiensis serovar kurstaki ?
-
-
1.1.1.B20 additional information enzyme BtBDH is active with meso-2,3-butanediol and (2R,3R)-2,3-butanediol, whereas no activity is observed with (2S,3S)-2,3-butanediol. BtBDH shows similar oxidative activity toward meso-2,3-butanediol and (2R,3R)-2,3-butanediol, and it exhibits a 3fold higher reduction activity toward acetoin compared to diacetyl Bacillus thuringiensis serovar kurstaki ACCC 10066 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.4 ? x * 37800, about, sequence calculation, x * 40000, recombinant enzyme, SDS-PAGE Bacillus thuringiensis serovar kurstaki
1.1.1.B20 ? x * 37800, about, sequence calculation, x * 40000, recombinant enzyme, SDS-PAGE Bacillus thuringiensis serovar kurstaki

Synonyms

EC Number Synonyms Comment Organism
1.1.1.4 (2R,3R)-2,3-butanediol dehydrogenase
-
Bacillus thuringiensis serovar kurstaki
1.1.1.4 BtBDH
-
Bacillus thuringiensis serovar kurstaki
1.1.1.4 butanediol dehydrogenase
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 (2R,3R)-2,3-butanediol dehydrogenase
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 BtBDH
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 butanediol dehydrogenase
-
Bacillus thuringiensis serovar kurstaki

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.4 35
-
reduction activity Bacillus thuringiensis serovar kurstaki
1.1.1.4 50
-
oxidation activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 35
-
reduction activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 50
-
oxidation activity Bacillus thuringiensis serovar kurstaki

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.4 70
-
stable up to Bacillus thuringiensis serovar kurstaki
1.1.1.B20 70
-
stable up to Bacillus thuringiensis serovar kurstaki

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.4 7.5
-
reduction activity Bacillus thuringiensis serovar kurstaki
1.1.1.4 10
-
oxidation activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 7.5
-
reduction activity Bacillus thuringiensis serovar kurstaki
1.1.1.B20 10
-
oxidation activity Bacillus thuringiensis serovar kurstaki

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.4 6 10 stable at Bacillus thuringiensis serovar kurstaki
1.1.1.B20 6 10 stable at Bacillus thuringiensis serovar kurstaki

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.4 NAD+
-
Bacillus thuringiensis serovar kurstaki
1.1.1.4 NADH
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 NAD+
-
Bacillus thuringiensis serovar kurstaki
1.1.1.B20 NADH
-
Bacillus thuringiensis serovar kurstaki

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.4 Bacillus thuringiensis serovar kurstaki sequence calculation
-
5.5
1.1.1.B20 Bacillus thuringiensis serovar kurstaki sequence calculation
-
5.5

General Information

EC Number General Information Comment Organism
1.1.1.4 evolution enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family Bacillus thuringiensis serovar kurstaki
1.1.1.B20 evolution enzyme BtBDH contains a GroES-like domain at the N terminus and a NAD(P)-binding domain at the C-terminus. Phylogenetic tree analysis reveals that BtBDH is a member ofthe (2R,3R)-2,3-BDH group. BtBDH has the typical (2R,3R)-2,3-butanediol dehydrogenase properties and belongs to the MDR superfamily. According to previous reports, (2R,3R)-2,3-BDH generally belongs to the MDR family, while meso-2,3-BDH is commonly clustered in the SDR (short chain dehydrogenase/reductase) family Bacillus thuringiensis serovar kurstaki