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Literature summary extracted from

  • Henke, E.; Bornscheuer, U.T.; Schmid, R.D.; Pleiss, J.
    A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases (2003), ChemBioChem, 4, 485-493.
    View publication on PubMed

Application

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

Protein Variants

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

Organism

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
-

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.1 liver
-
Sus scrofa
-

Substrates and Products (Substrate)

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
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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