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Literature summary for 3.5.1.11 extracted from

  • Carboni, C.; Kierkels, H.G.; Gardossi, L.; Tamiola, K.; Janssen, D.B.; Quaedflieg, P.J.
    Preparation of D-amino acids by enzymatic kinetic resolution using a mutant of penicillin-G acylase from E. coli (2006), Tetrahedron Asymmetry, 17, 245-251.
No PubMed abstract available

Application

Application Comment Organism
synthesis D-Gln and D-Glu can be obtained in one step in high enantiomeric excess (97% and 90%, respectively) in an enzymatic kinetic resolution of their racemates. This is achieved by enantioselective conversion of the L-enantiomers to the N-phenylacetyl derivatives with phenylacetic acid methylester as an acyl donor in aqueous solution by using an F24A mutant of PGA from Escherichia coli. The high enantiomeric excess values are mainly due to the significantly suppressed hydrolysis rate of N-phenylacetyl-L-Gln and N-phenylacetyl-L-Glu, respectively, compared to wild-type PGA Escherichia coli

Protein Variants

Protein Variants Comment Organism
F24A suppressed hydrolysis rate of N-phenylacetyl-L-Gln and N-phenylacetyl-L-Glu, respectively, compared to wild-type enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Synonyms

Synonyms Comment Organism
penicillin-G acylase
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Escherichia coli