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Literature summary extracted from

  • Sosedov, O.; Baum, S.; Buerger, S.; Matzer, K.; Kiziak, C.; Stolz, A.
    Construction and application of variants of the Pseudomonas fluorescens EBC191 arylacetonitrilase for increased production of acids or amides (2010), Appl. Environ. Microbiol., 76, 3668-3674.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.5.5.5 A114F inactive Pseudomonas fluorescens
3.5.5.5 A116C the mutant shows activity similar to the wild type enzyme Pseudomonas fluorescens
3.5.5.5 A116F the mutant shows about 50% of wild type activity Pseudomonas fluorescens
3.5.5.5 C163A the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid Pseudomonas fluorescens
3.5.5.5 C163N the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates Pseudomonas fluorescens
3.5.5.5 C163N/A165R the mutant demonstrates increased amide formation capacity in comparison to the mutants carrying only single mutations Pseudomonas fluorescens
3.5.5.5 C163N/W110I the mutant enzyme forms about 100fold more 2-phenylpropionamide (in relation to the total amount of (R,S)-2-phenylpropionitrile converted) than the wild type, although the relative activity of this mutant for the conversion (R,S)-2-phenylpropionitrile to 2-phenylpropionic acid is only 4% of that observed for the wild type Pseudomonas fluorescens
3.5.5.5 C163Q the mutation results in significantly increased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates Pseudomonas fluorescens
3.5.5.5 C163S the mutation results in significantly decreased amounts of amides formed using (R,S)-mandelonitrile and (R,S)-2-phenylpropionitrile as substrates. The mutant demonstrates no significant difference in the enzyme activity compared to the wild type, but shows an extremely low degree of enantioselectivity for the formation of (R)-mandelic acid Pseudomonas fluorescens
3.5.5.5 G109F inactive Pseudomonas fluorescens
3.5.5.5 I117F the mutant shows about 50% of wild type activity Pseudomonas fluorescens
3.5.5.5 L111F the mutant shows about 50% of wild type activity Pseudomonas fluorescens
3.5.5.5 L113F the mutant shows activity similar to the wild type enzyme Pseudomonas fluorescens
3.5.5.5 W110F the mutant shows activity similar to the wild type enzyme Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
3.5.5.5 Pseudomonas fluorescens
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 strain EBC191
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.5.5 2 (R,S)-2-phenylpropionitrile + 3 H2O deletions of 47 to 67 amino acids (aa) from the carboxy terminus of the nitrilase resulted in variant forms that demonstrated increased amide formation and an increased formation of the (R)-acids Pseudomonas fluorescens 2-phenylpropionic acid + 2-phenylpropionamide + NH3
-
 ?
3.5.5.5 2 (R,S)-mandelonitrile + 2 H2O
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 Pseudomonas fluorescens (R)-mandelic acid + (S)-mandeloamide + NH3
-
 ?