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Literature summary extracted from

  • Lingen, B.; Kolter-Jung, D.; Dunkelmann, P.; Feldmann, R.; Grotzinger, J.; Pohl, M.; Muller, M.
    Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution (2003), ChemBioChem, 4, 721-726.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.7 expression of mutant enzyme L476Q and M365L/L461S in Escherichia coli Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.7 L476Q mutant enzyme selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme. Vmax and Km-value for decraboxylation of benzoylformate are not effected Pseudomonas putida
4.1.1.7 M365L/L461S mutant enzyme selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme. Mutant enzyme retains only 9% of the wild-type BFD carboligase activity. Decrease in Vmax value as well as an increase in the Km-value for decarboxylation of benzoylformate by mutant enzyme compared to that of wild-type enzyme Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.7 benzoylformate substrate inhibition Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.7 0.54
-
 benzoylformate wild-type enzyme Pseudomonas putida
4.1.1.7 0.58
-
 benzoylformate mutant enzyme L476Q Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.7 Pseudomonas putida P20906
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.7 benzoylformate
-
 Pseudomonas putida benzaldehyde + CO2
-
 ?
4.1.1.7 m-bromo-benzoylformate wild-type enzyme: 68% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 97% conversion with more than 98% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 98.5% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida m-bromo-benzaldehyde + CO2
-
 ?
4.1.1.7 m-chloro-benzoylformate wild-type enzyme: 94% conversion with 94% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida m-chloro-benzaldehyde + CO2
-
 ?
4.1.1.7 m-fluoro-benzoylformate wild-type enzyme: 100% conversion with 87% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 94% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida m-fluoro-benzaldehyde + CO2
-
 ?
4.1.1.7 m-methoxy-benzoylformate wild-type enzyme: 94% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida m-methoxy-benzaldehyde + CO2
-
 ?
4.1.1.7 m-methyl-benzoylformate wild-type enzyme: 99% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida m-methyl-benzaldehyde + CO2
-
 ?
4.1.1.7 o-bromo-benzoylformate wild-type enzyme: no activity, mutant enzyme L476Q: 98% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 90% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida o-bromo-benzaldehyde + CO2
-
 ?
4.1.1.7 o-chloro-benzoylformate wild-type enzyme: no activity, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 85% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida o-chloro-benzaldehyde + CO2
-
 ?
4.1.1.7 o-fluoro-benzoylformate wild-type enzyme: 91% conversion with 89% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 83% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida o-fluoro-benzaldehyde + CO2
-
 ?
4.1.1.7 o-methoxy-benzoylformate wild-type enzyme: no conversion, mutant enzyme L476Q: 97% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 46% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida o-methoxy-benzaldehyde + CO2
-
 ?
4.1.1.7 o-methyl-benzoylformate wild-type enzyme: 4% conversion, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 83% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida o-methyl-benzaldehyde + CO2
-
 ?
4.1.1.7 o-methylbenzaldehyde + acetaldehyde mutant enzyme L476Q and M365L/L461S selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme Pseudomonas putida (2S)-2-hydroxy-1-(2-methylphenyl)propan-1-one
-
 ?
4.1.1.7 p-bromo-benzoylformate wild-type enzyme: 42% conversion with 83% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with 96.5% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida p-bromo-benzaldehyde + CO2
-
 ?
4.1.1.7 p-chloro-benzoylformate wild-type enzyme: 85% conversion with 82% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 96.5% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 95.5% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida p-chloro-benzaldehyde + CO2
-
 ?
4.1.1.7 p-fluoro-benzoylformate wild-type enzyme: 69% conversion with 87% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 87% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida p-fluoro-benzaldehyde + CO2
-
 ?
4.1.1.7 p-methoxy-benzoylformate wild-type enzyme: 23% conversion with 92% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 67% conversion with 42% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida p-methoxy-benzaldehyde + CO2
-
 ?
4.1.1.7 p-methyl-benzoylformate wild-type enzyme: 65% conversion with 88% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 98% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 98% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone Pseudomonas putida p-methyl-benzaldehyde + CO2
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.7 100
-
 benzoylformate mutant enzyme L476Q Pseudomonas putida
4.1.1.7 143
-
 benzoylformate wild-type enzyme Pseudomonas putida