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[大肠杆菌EF-T延伸因子中的鸟苷酸环化酶活性]

[Guanyl cyclase activity in the EF-T elongation factor of Escherichia coli].

作者信息

Macchia V, Consiglio E, Varrone S

出版信息

C R Seances Soc Biol Fil. 1977;171(3):516-25.

PMID:21022
Abstract

Highly purified EF-Ts from E. coli does contain guanylate cyclase activity, which is absent from other purified transfer factors, such as EF-Tu and EF-G. Guanylate cyclase activity has been characterized by its sensitivity to inhibitors and substrate specificity. Although the physicochemical properties of guanylate cyclase are closely related to those of EF-Ts, it does not appear to be a contaminant of this transfer factor, but a specific enzyme. The possible role of guanylate cyclase in protein synthesis is discussed.

摘要

从大肠杆菌中高度纯化得到的EF-Ts确实具有鸟苷酸环化酶活性,而其他纯化的转移因子,如EF-Tu和EF-G则没有这种活性。鸟苷酸环化酶活性已通过其对抑制剂的敏感性和底物特异性进行了表征。尽管鸟苷酸环化酶的物理化学性质与EF-Ts密切相关,但它似乎不是这种转移因子的污染物,而是一种特异性酶。本文讨论了鸟苷酸环化酶在蛋白质合成中的可能作用。

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