Enzymic synthesis of N-acetyl-L-phenylalanine in Escherichia coli K12.

Cell-free extracts of Escherichia coli K12 catalyse the synthesis of N-acetyl-
L-phenylalanine from acetyl-CoA and L-phenylalanine. 2. The acetyl-CoA-Lphenylalanine
a-N-acetyltransferase was purified 160-fold from cell-free extracts.
3. The enzyme has a pH optimum of 8 and catalyses the acetylation of L-phenylalanine.
Other L-amino acids such as histidine and alanine are acetylated at
slower rates. 4. A transacylase was also purified from E. coli extracts and its substrate
specificity studied. 5. The properties of both these enzymes were compared
with those of other known amino acid acetyltransferases and transacylases.