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Literature summary for 1.1.1.4 extracted from
- 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
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Bacillus thuringiensis serovar kurstaki |  |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.76 | - |
(2R,3R)-butane-2,3-diol | pH 10.0, 50°C, recombinant enzyme | Bacillus thuringiensis serovar kurstaki | |
| 3.67 | - |
(2R,3S)-butane-2,3-diol | pH 10.0, 50°C, recombinant enzyme | Bacillus thuringiensis serovar kurstaki | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2R,3R)-butane-2,3-diol + NAD+ | Bacillus thuringiensis serovar kurstaki | - |
(3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3R)-butane-2,3-diol + NAD+ | Bacillus thuringiensis serovar kurstaki ACCC 10066 | - |
(3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | Bacillus thuringiensis serovar kurstaki | - |
(3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | Bacillus thuringiensis serovar kurstaki ACCC 10066 | - |
(3R)-acetoin + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thuringiensis serovar kurstaki | A0A0F6FX23 | - |
- |
| Bacillus thuringiensis serovar kurstaki ACCC 10066 | A0A0F6FX23 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli by ion exchange chromatography | Bacillus thuringiensis serovar kurstaki |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, BtBDH shows good stability after storage for 3 months | Bacillus thuringiensis serovar kurstaki |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (2R,3R)-butane-2,3-diol + NAD+ | - |
Bacillus thuringiensis serovar kurstaki | (3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3R)-butane-2,3-diol + NAD+ | - |
Bacillus thuringiensis serovar kurstaki ACCC 10066 | (3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | - |
Bacillus thuringiensis serovar kurstaki | (3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | slightly preferred substrate | Bacillus thuringiensis serovar kurstaki | (3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | - |
Bacillus thuringiensis serovar kurstaki ACCC 10066 | (3R)-acetoin + NADH + H+ | - |
r | |
| (2R,3S)-butane-2,3-diol + NAD+ | slightly preferred substrate | Bacillus thuringiensis serovar kurstaki ACCC 10066 | (3R)-acetoin + NADH + H+ | - |
r | |
| 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 | ? | - |
- |
|
| 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
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 37800, about, sequence calculation, x * 40000, recombinant enzyme, SDS-PAGE | Bacillus thuringiensis serovar kurstaki |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| (2R,3R)-2,3-butanediol dehydrogenase | - |
Bacillus thuringiensis serovar kurstaki |
| BtBDH | - |
Bacillus thuringiensis serovar kurstaki |
| butanediol dehydrogenase | - |
Bacillus thuringiensis serovar kurstaki |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
reduction activity | Bacillus thuringiensis serovar kurstaki |
| 50 | - |
oxidation activity | Bacillus thuringiensis serovar kurstaki |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
stable up to | Bacillus thuringiensis serovar kurstaki |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
reduction activity | Bacillus thuringiensis serovar kurstaki |
| 10 | - |
oxidation activity | Bacillus thuringiensis serovar kurstaki |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | stable at | Bacillus thuringiensis serovar kurstaki |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Bacillus thuringiensis serovar kurstaki | |
| NADH | - |
Bacillus thuringiensis serovar kurstaki | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Bacillus thuringiensis serovar kurstaki | sequence calculation | - |
5.5 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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