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针对法尼基转移酶（FTase）合成并筛选 CaaL 肽文库，揭示了数量惊人的底物。

Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates.

机构信息

Department of Medicinal Chemistry and Molecular Pharmacology and Center for Cancer Research, Purdue University, West Lafayette, IN 47907, United States.

出版信息

Bioorg Med Chem Lett. 2010 Jan 15;20(2):767-70. doi: 10.1016/j.bmcl.2009.11.011. Epub 2009 Nov 12.

DOI:10.1016/j.bmcl.2009.11.011
PMID:20005705
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2922960/
Abstract

Proteins bearing a CaaL sequence are typically geranylgeranylated to enable their proper localization and function. We found that many of the dansyl-GCaaL peptides representing mammalian CaaL proteins can be farnesylated by FTase. This result may have important implications for prenylated protein biology.

摘要

带有 CaaL 序列的蛋白质通常被 geranylgeranylated 以使其正确定位和功能。我们发现，代表哺乳动物 CaaL 蛋白的许多dansyl-GCaaL 肽可以被 FTase 法尼基化。这一结果可能对 prenylated 蛋白生物学具有重要意义。

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