Title of article :
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant
Author/Authors :
Natalya Voloshchuk، نويسنده , , Man Xia Lee، نويسنده , , Wan Wen Zhu، نويسنده , , Ismet Caglar Tanrikulu، نويسنده , , Jin Kim Montclare، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
5
From page :
5907
To page :
5911
Abstract :
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.
Keywords :
Trifluoroleucine , thermostability , protein engineering , mutagenesis , non-natural amino acid
Journal title :
Bioorganic & Medicinal Chemistry Letters
Serial Year :
2007
Journal title :
Bioorganic & Medicinal Chemistry Letters
Record number :
798719
Link To Document :
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