54896-74-1Relevant articles and documents
A new biocatalytic route to enantiopure N-carbamoyl amino acids by fast enzyme screening
Trauthwein, Harald,May, Oliver,Dingerdissen, Uwe,Buchholz, Stefan,Drauz, Karlheinz
, p. 3737 - 3739 (2003)
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.
Rapid and efficient microwave-assisted synthesis of N-carbamoyl-L-amino acids
Verardo, Giancarlo,Geatti, Paola,Strazzolini, Paolo
, p. 1833 - 1844 (2008/02/02)
A rapid and efficient method for the synthesis of N-carbamoyl-L-amino acids is reported. The procedure, involving the reaction between urea and α-amino acids sodium salts, was performed under microwave conditions using an unmodified domestic microwave oven. A careful study of the operative conditions indicated proline (1d) as the less reactive substrate and phenylglycine (1e) as the more reactive one among all the α-amino acids tested. Substitution of urea with potassium cyanate produced a low conversion into the corresponding N-carbamoyl derivative, and a possible explanation of this result is reported. Copyright Taylor & Francis Group, LLC.
Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Bacillus stearothermophilus NS1122A
Ishikawa,Mukohara,Watabe,Kobayashi,Nakamura
, p. 265 - 270 (2007/10/02)
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