Title of article
A new biocatalytic route to enantiopure N-carbamoyl amino acids by fast enzyme screening
Author/Authors
Trauthwein، نويسنده , , Harald and May، نويسنده , , Oliver and Dingerdissen، نويسنده , , Uwe and Buchholz، نويسنده , , Stefan and Drauz، نويسنده , , Karlheinz، نويسنده ,
Issue Information
هفته نامه با شماره پیاپی سال 2003
Pages
3
From page
3737
To page
3739
Abstract
The enantioselective enzymatic deamidation of (rac)-N-carbamoyl amino acid amides (Cbm-AA-NH2) 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.
Keywords
Biocatalysis , N-carbamoyl amino acid amide , proteases , enantioselective enzymatic deamidation , HTS
Journal title
Tetrahedron Letters
Serial Year
2003
Journal title
Tetrahedron Letters
Record number
1662025
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