A new biocatalytic route to enantiopure N-carbamoyl amino acids by fast enzyme screening

✍ Scribed by Harald Trauthwein; Oliver May; Uwe Dingerdissen; Stefan Buchholz; Karlheinz Drauz

• Publisher: Elsevier Science
• Year: 2003
• Tongue: French
• Weight: 78 KB
• Volume: 44
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(03)00746-9

✦ Synopsis

The enantioselective enzymatic deamidation of (rac)-N-carbamoyl amino acid amides (Cbm-AA-NH 2 ) to enantiopure (L)-N-carbamoyl amino acids (Cbm-AA-OH) is described for the first time. Via fast screening methods of biocatalysts several proteases like Chirazyme P1, Chirazyme P2 and Subtilisin were identified, which give conversions of up to 47% and >98% ee. This conversion is most productive on aliphatic and primary amino acids.