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

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Title Enzymic synthesis of N-acetyl-L-phenylalanine in Escherichia coli K12.
 
Creator Krishna, R. V.
Krishnaswamy, P. R.
Rajagopal Rao, D.
 
Subject 16 Enzyme Chemistry
 
Description 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.
 
Date 1971
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/4124/1/Biochem.%20J.%20%281971%29%20124%2C%20905-913.pdf
Krishna, R. V. and Krishnaswamy, P. R. and Rajagopal Rao, D. (1971) Enzymic synthesis of N-acetyl-L-phenylalanine in Escherichia coli K12. Biochemical Journal, 124. pp. 905-913.