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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
penicillin-G acylase | - |
Escherichia coli |