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Literature summary for 3.5.1.11 extracted from

  • Cabrera, Z.; Lopez-Gallego, F.; Fernandez-Lorente, G.; Palomo, J.M.; Montes, T.; Grazu, V.; Guisan, J.M.; Fernandez-Lafuente, R.
    Asymmetric hydrolysis of dimethyl phenylmalonate by immobilized penicillin G acylase from E. coli (2007), Enzyme Microb. Technol., 40, 997-1000.
No PubMed abstract available
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Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-methyl mandelate + H2O
-
 Escherichia coli ?
-
 ?
diethyl phenylmalonate + H2O the enantiomeric excess is higher than 98%, producing mainly the (+)-ethyl phenylmalonate ester Escherichia coli (+)-ethyl phenylmalonate + ethanol
-
 ?
dimethyl phenylmalonate + H2O dimethyl phenylmalonate is fully hydrolyzed to methylphenylmalonate in only 2 h, but even after 10 h phenylmalonic acid is not detected. The enantiomeric excess is higher than 98%, producing mainly the (+)-methyl phenylmalonate ester Escherichia coli (+)-methyl phenylmalonate + methanol
-
 ?
penicillin G + H2O
-
 Escherichia coli 6-aminopenicillanic acid + phenylacetic acid
-
 ?

Synonyms

Synonyms Comment Organism
penicillin G acylase
-
 Escherichia coli