EC Number | Application | Comment | Organism |
---|---|---|---|
3.1.1.1 | biotechnology | rational protein engineering for direct evolution of suitable enantioselective biocatalysts for synthesis of chiral substances | Bacillus subtilis |
3.1.1.1 | biotechnology | rational protein engineering for direct evolution of suitable enantioselective biocatalysts for synthesis of chiral substances | Sus scrofa |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.1.1 | 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 |
3.1.1.1 | A400I/G105A | inactive mutant | Bacillus subtilis |
3.1.1.1 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.1.1 | Bacillus subtilis | - |
recombinant enzyme, 4-nitrophenyl esterase, enzyme contains the GGGX sequence motif | - |
3.1.1.1 | Sus scrofa | - |
enzyme contains the GGGX sequence motif | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.1.1.1 | 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 |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.1.1 | liver | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.1 | 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 | - |
? | |
3.1.1.1 | 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 | - |
? | |
3.1.1.1 | 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 | - |
? | |
3.1.1.1 | 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 | - |
? | |
3.1.1.1 | linalyl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, low enantioselectivity, overview | Sus scrofa | linalool + acetate | - |
? | |
3.1.1.1 | linalyl acetate + H2O | model substrate for study of enantioselectivity in the enzyme reaction, overview | Bacillus subtilis | linalool + acetate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.1.1 | 4-nitrophenyl esterase | - |
Bacillus subtilis |
3.1.1.1 | pig liver esterase | - |
Sus scrofa |
3.1.1.1 | PLE | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.1 | 40 | - |
assay at | Bacillus subtilis |
3.1.1.1 | 40 | - |
assay at | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.1 | 7.5 | - |
assay at | Bacillus subtilis |
3.1.1.1 | 7.5 | - |
assay at | Sus scrofa |