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Literature summary extracted from

  • Carballeira, J.D.; Krumlinde, P.; Bocola, M.; Vogel, A.; Reetz, M.T.; Baeckvall, J.E.
    Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene (2007), Chem. Commun. (Camb. ), 2007, 1913-1915.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 D20N/S53P/S155M/L162G/T180I/T234S site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L159W/L162T site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162A site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162D site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162F site-directed mutagenesis, a highly enantioselective mutant, use in combinatorial active site saturation test for kinetic resolution of an axially chiral allene, 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate, the high enantioselectivity of the mutant is rationalized by PI–PI stacking Pseudomonas aeruginosa
3.1.1.3 L162G site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162G/L159V site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162G/L159Y site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162I site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162T site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L162V site-directed mutagenesis, the mutant shows higher enantioselectivity as the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L17F site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 L231e/V232C site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 M16A site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 V232I site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa
3.1.1.3 V232I/M16L/A34T/P86L/D113G/S237T/T150A/S147N/V94A/T87S/L208H site-directed mutagenesis, the mutant shows reduced enantioselectivity compared to the wild-type enzyme with substrates 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate and 4-nitrophenyl 2-methyldecanoate Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Pseudomonas aeruginosa
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Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 additional information
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 Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl 2-methyldecanoate + H2O kinetic resolution of enantioselectivity, overview Pseudomonas aeruginosa ?
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 ?
3.1.1.3 4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate + H2O reaction via R-tetrahedral intermediate and S-tetrahedral intermediate, overview, the wild-type lipase and the mutant L162F show preference for the (+)-enantiomer, the mutant shows high enantioselectivity, kinetic resolution of enantioselectivity, overview Pseudomonas aeruginosa ?
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 ?