Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: improved thermostability by a single-isoleucine mutant.
Fluorinated chloramphenicol acetyltransferase thermostability and activity profile: improved thermostability by a single-isoleucine mutant.
复制标题
氟化氯霉素乙酰转移酶热稳定性和活性特征：通过单异亮氨酸突变体提高热稳定性。
DOI：
10.1016/j.bmcl.2007.07.107
复制
发表时间：
2007
影响因子：
2.7
通讯作者：
Montclare,JinKim
中科院分区：
文献类型：
--
作者：
Voloshchuk,Natalya;Lee,ManXia;Zhu,WanWen;Tanrikulu,IsmetCaglar;Montclare,JinKim
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.
