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

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.

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: Escherichia coli K12, acylamino acids, enzymes
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 26 Jul 2013 06:43
Last Modified: 26 Jul 2013 06:43
URI: http://ir.cftri.com/id/eprint/4124

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