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Literature summary for 3.1.1.1 extracted from
- A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases (2003), ChemBioChem, 4, 485-493.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | rational protein engineering for direct evolution of suitable enantioselective biocatalysts for synthesis of chiral substances | Bacillus subtilis |
| biotechnology | rational protein engineering for direct evolution of suitable enantioselective biocatalysts for synthesis of chiral substances | Sus scrofa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A400I | activity with 4-nitrophenol is similar to the wild-type enzyme, similar enantioselectivity in the conversion of the model substrates compared to the wild-type | Bacillus subtilis |
| A400I/G105A | inactive mutant | Bacillus subtilis |
| G105A | 90% reduced activity with 4-nitrophenol compared to the wild-type enzyme, 6fold increased enantioselectivity in the conversion of the model substrate 2-phenyl-3-butyn-2-yl acetate compared to the wild-type, inversion of enantiopreference towards linalyl acetate, slight enantioselectivity towarsd 3-methyl-1-pentyn-3-yl-acetate | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
recombinant enzyme, 4-nitrophenyl esterase, enzyme contains the GGGX sequence motif | - |
| Sus scrofa | - |
enzyme contains the GGGX sequence motif | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a carboxylic ester + H2O = an alcohol + a carboxylate | reaction and substrate binding mechanism, structure distinct binding pockets of the wild-type and mutant enzymes, Gly105 plays an important role | Bacillus subtilis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-phenyl-3-butyn-2-yl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, low enantioselectivity, overview | Sus scrofa | 2-phenyl-3-butyn-2-ol + acetate | - |
? |  |
| 2-phenyl-3-butyn-2-yl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, overview | Bacillus subtilis | 2-phenyl-3-butyn-2-ol + acetate | - |
? | |
| 3-methyl-1-pentyn-3-yl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, low enantioselectivity, overview | Sus scrofa | 3-methyl-1-pentyn-3-ol + acetate | - |
? | |
| 3-methyl-1-pentyn-3-yl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, no enantioselectivity by the wild-type enzyme, overview | Bacillus subtilis | 3-methyl-1-pentyn-3-ol + acetate | - |
? | |
| linalyl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, low enantioselectivity, overview | Sus scrofa | linalool + acetate | - |
? | |
| linalyl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, overview | Bacillus subtilis | linalool + acetate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 4-nitrophenyl esterase | - |
Bacillus subtilis |
| pig liver esterase | - |
Sus scrofa |
| PLE | - |
Sus scrofa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Bacillus subtilis |
| 40 | - |
assay at | Sus scrofa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Bacillus subtilis |
| 7.5 | - |
assay at | Sus scrofa |
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