肽底物分析揭示的人蛋白酪氨酸激酶的催化特异性。

Current chemical genomics Pub Date : 2011-01-01 Epub Date: 2011-08-22 DOI:10.2174/1875397301105010115
Julie Blouin, Philippe Roby, Mathieu Arcand, Lucille Beaudet, Francesco Lipari
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引用次数: 9

摘要

在90种人蛋白酪氨酸激酶中,有81种用短肽进行了分析,这些短肽来源于特征明确的[CDK1(Tyr15), IRS1(Tyr983)和JAK1(Tyr1023)]或一般的[polyGlu:Tyr(4:1)和poly-Glu:Ala:Tyr(1:1:1)]底物。正如预期的那样,CDK1肽是所有Src家族激酶的底物。另一方面,一些活性是新的,并导致更好地理解某些激酶的功能。具体来说,CDK1肽是许多Eph家族成员的底物。有趣的是,对几乎所有人类蛋白酪氨酸激酶的分析揭示了对CDK1和IRS1肽的独特选择性模式。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Catalytic specificity of human protein tyrosine kinases revealed by Peptide substrate profiling.

Out of the 90 human protein tyrosine kinases, 81 were assayed with short peptides derived from well-characterized [CDK1(Tyr15), IRS1(Tyr983), and JAK1(Tyr1023)] or generic [polyGlu:Tyr(4:1) and poly-Glu:Ala:Tyr(1:1:1)] substrates. As expected, the CDK1 peptide is a substrate for all Src family kinases. On the other hand, some of the activities are novel and lead to a better understanding of the function of certain kinases. Specifically, the CDK1 peptide is a substrate for many of the Eph family members. Interestingly, profiling of nearly all the human protein tyrosine kinases revealed a distinct pattern of selectivity towards the CDK1 and IRS1 peptides.

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