A Critical Examination of Escherichia coli Esterase Activity
A Critical Examination of Escherichia coli Esterase Activity
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DOI：
10.1074/jbc.m109.027409
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发表时间：
2009-10-16
影响因子：
4.8
通讯作者：
Tippmann, Eric M.
中科院分区：
文献类型：
--
作者：
Antonczak, Alicja K.;Simova, Zuzana;Tippmann, Eric M.
研究了大肠杆菌在一系列乙酰化和糖基化化合物上生长的能力。推测E.大肠杆菌保持低水平的非特异性酯酶活性。这一观察结果可能对以前依赖于E.大肠杆菌的基因编码非天然氨基酸。已有报道E.大肠杆菌在体内脱乙酰化三乙酰基O-连接的糖基化丝氨酸和苏氨酸。据报道，糖基化氨基酸已响应于琥珀终止密码子被遗传编码成蛋白质。然而，我们的论点是，这些氨基酸在E.杆菌目前的结果报告在体外分析的原始酶和体内分析的糖基化氨基酸。得出的结论是，琥珀抑制方法与非天然氨基酸可能需要在某些情况下使用的警告。
The ability of Escherichia coli to grow on a series of acetylated and glycosylated compounds has been investigated. It is surmised that E. coli maintains low levels of nonspecific esterase activity. This observation may have ramifications for previous reports that relied on nonspecific esterases from E. coli to genetically encode nonnatural amino acids. It had been reported that nonspecific esterases from E. coli deacetylate tri-acetyl O-linked glycosylated serine and threonine in vivo. The glycosylated amino acids were reported to have been genetically encoded into proteins in response to the amber stop codon. However, it is our contention that such amino acids are not utilized in this manner within E. coli. The current results report in vitro analysis of the original enzyme and an in vivo analysis of a glycosylated amino acid. It is concluded that the amber suppression method with nonnatural amino acids may require a caveat for use in certain instances.