Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant

Natalya Voloshchuk, Man Xia Lee, Wan Wen Zhu, Ismet Caglar Tanrikulu, Jin Kim Montclare

Research output: Contribution to journalArticle


A lysate-based thermostability and activity profile is described for chloramphenicol acetyltransferase (CAT) expressed in trifluoroleucine, T (CAT T). CAT and 13 single-isoleucine CAT mutants were expressed in medium supplemented with T and assayed for thermostability on cell lysates. Although fluorinated mutants, L82I T and L208I T, showed losses in thermostability, the L158I T fluorinated mutant demonstrated an enhanced thermostability relative to CAT T. Further characterization of L158I T suggested that T at position 158 contributed to a portion of the observed loss in thermostability upon global fluorination.

Original languageEnglish (US)
Pages (from-to)5907-5911
Number of pages5
JournalBioorganic and Medicinal Chemistry Letters
Issue number21
StatePublished - Nov 1 2007



  • Mutagenesis
  • Non-natural amino acid
  • Protein engineering
  • Thermostability
  • Trifluoroleucine

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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