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。

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

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

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

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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