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Literature summary for 4.1.1.7 extracted from
- Carboligation reactions mediated by benzoylformate decarboxylase immobilized on a magnetic solid support (2013), Chirality, 25, 415-421.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | purified recombinant His-tagged enzyme immobilized on magnetic nanoparticles, microspheres, nanospheres and ferrofluids, is used for enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes. The heterogeneous biocatalyst is offering the ease of immobilization along with the separation steps of metal affinity ligand (Cu2+-iminodiacetic acid) coated magnetic nanoparticles. Reusability of immobilized enzyme for carboligation reactions | Pseudomonas putida |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged enzyme in Escherichia coli strain SG13009 | Pseudomonas putida |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | immobilization of the purified recombinant His-tagged enzyme on magnetic nanoparticles, microspheres, nanospheres and ferrofluids, for enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes. Adsorption capacity of the Cu+2 charged magnetic solid support for His-tagged BFD is determined by standard BSA assay as 43.6 mg enzyme/g magnetic solid support | Pseudomonas putida |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 56000 | - |
x * 56000, recombinant His-tagged enzyme, SDS-PAGE | Pseudomonas putida |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Pseudomonas putida | the enzyme performs enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Pseudomonas putida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 benzaldehyde | - |
Pseudomonas putida | (R)-benzoin | i.e. (R)-2-hydroxy-1,2-diphenylethan-1-one | ? | |
| additional information | the enzyme performs enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes | Pseudomonas putida | ? | - |
? | |
| additional information | the enzyme also performs the cross acyloin reaction of benzaldehyde with acetaldehyde to give (S)-2-hydroxy-1-phenylpropanone | Pseudomonas putida | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 56000, recombinant His-tagged enzyme, SDS-PAGE | Pseudomonas putida |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BFD | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Pseudomonas putida |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Pseudomonas putida |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme functions in decarboxylation of benzoylformate to benzaldehyde in the mandalate pathway | Pseudomonas putida |
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Release 2023.1 (January 2023)
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